Relevant bibliographies by topics / Cytoskeletal proteins

Academic literature on the topic 'Cytoskeletal proteins'

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Published: 4 June 2021
Last updated: 26 February 2023

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Journal articles on the topic "Cytoskeletal proteins"

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Letek, Michal, María Fiuza, Almudena F. Villadangos, Luís M. Mateos, and José A. Gil. "Cytoskeletal Proteins ofActinobacteria." International Journal of Cell Biology 2012 (2012): 1–10. http://dx.doi.org/10.1155/2012/905832.

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Although bacteria are considered the simplest life forms, we are now slowly unraveling their cellular complexity. Surprisingly, not only do bacterial cells have a cytoskeleton but also the building blocks are not very different from the cytoskeleton that our own cells use to grow and divide. Nonetheless, despite important advances in our understanding of the basic physiology of certain bacterial models, little is known aboutActinobacteria, an ancient group of Eubacteria. Here we review current knowledge on the cytoskeletal elements required for bacterial cell growth and cell division, focusing on actinobacterial genera such asMycobacterium, Corynebacterium, andStreptomyces. These include some of the deadliest pathogens on earth but also some of the most prolific producers of antibiotics and antitumorals.
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Miura, Tetsuji. "Cytoskeletal Proteins." Circulation Journal 74, no. 11 (2010): 2295–96. http://dx.doi.org/10.1253/circj.cj-10-0935.

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Albrecht, D. L., and R. J. Noelle. "Membrane Ig-cytoskeletal interactions. I. Flow cytofluorometric and biochemical analysis of membrane IgM-cytoskeletal interactions." Journal of Immunology 141, no. 11 (December 1, 1988): 3915–22. http://dx.doi.org/10.4049/jimmunol.141.11.3915.

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Abstract Membrane IgM (mIgM) and mIgD are the receptors for Ag on the surface of B lymphocytes, mIg is soluble in detergent; however, when mIg is cross-linked with anti-Ig, the mIg becomes associated with the cytoskeletal matrix and is rendered detergent-insoluble. By a novel flow cytofluorometric assay and by biochemical analysis, it has been shown that anti-isotype-specific antibodies induce mIgM and mIgD to associate with the cytoskeleton of B lymphocytes in an isotype-specific fashion. The detergent solubility of other prominent B lymphocyte surface proteins, such as class I and class II MHC proteins were unaffected by cross-linking of mIg. A panel of mu-specific mAb was analyzed for their ability to induce mIgM-cytoskeletal association. Although all mAb bound mIgM, only three out of seven rendered mIgM cytoskeletally associated. Further analysis revealed a strict correlation in the capacity of mu-specific mAb to induce capping and to induce the association of mIgM with the cytoskeleton.
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Dvořáková, Kateřina, Harry D. M. Moore, Nataša Šebková, and Jiří Paleček. "Cytoskeleton localization in the sperm head prior to fertilization." Reproduction 130, no. 1 (July 2005): 61–69. http://dx.doi.org/10.1530/rep.1.00549.

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Three major cytoskeletal proteins, actin, tubulin and spectrin, are present in the head of mammalian spermatozoa. Although cytoskeletal proteins are implicated in the regulation of capacitation and the acrosome reaction (AR), their exact role remains poorly understood. The aim of this study was to compare the distribution of the sperm head cytoskeleton before and after the AR in spermatozoa representing a range of acrosome size and shape. Spermatozoa from the human and three rodents (rat, hamster and grey squirrel) were fixed before and after the AR in appropriate mediumin vitro. Indirect immunofluorescent localization of cytoskeletal proteins was undertaken with antibodies recognizing actin, spectrin and α-tubulin. Preparations were counterstained with propidium iodide and examined by epifluorescent and confocal microscopy. Our results clearly demonstrated changes in localization of cytoskeleton during the AR, mainly in the apical acrosome with further changes to the equatorial segment and post-acrosomal regions. The pattern of cytoskeletal proteins in the sperm head of all the species was similar in respect to various sub-compartments. These observations indicated that the sperm head cortical cytoskeleton exhibits significant changes during the AR and, therefore, support the image of cytoskeletal proteins as highly dynamic structures participating actively in processes prior to fertilization.
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Fox, Joan. "Cytoskeletal Proteins and Platelet Signaling." Thrombosis and Haemostasis 86, no. 07 (2001): 198–213. http://dx.doi.org/10.1055/s-0037-1616218.

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SummaryThe actin filament network fills the cytoplasm of unstimulated platelets and connects with a submembranous latticework of short cross-linked actin filaments, known as the membrane skeleton. One function of the cytoskeleton is to direct the contours of the membrane in the unstimulated platelet and the rapid changes in shape in the activated platelet. Activation-induced changes result from events such as phosphorylation or calpain-induced cleavage of cytoskeletal proteins. The specific reorganizations depend upon the combination of signals to which platelets are exposed. A second function of the cytoskeleton is to bind other cellular components; it binds signaling molecules, localizing them to specific cellular locations; it binds the plasma membrane regulating properties of the membrane, maintaining microdomains in the membrane, or regulating activities of membrane proteins. In this way, the cytoskeleton plays a critical role in regulation of spatial organizations and, thus, in the integration of cellular activities.
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Perry, G., D. A. Zelasko, L. M. Sayre, and M. A. Smith. "Oxidative Damage to Axonal Cytoskeletal Proteins." Microscopy and Microanalysis 3, S2 (August 1997): 43–44. http://dx.doi.org/10.1017/s1431927600007108.

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Proteins of the axonal cytoskeleton, particularly neurofilament and microtubule-associated protein τ, should be particularly sensitive to the effects of oxidative modification due to their high content of lysine, an amino acid that is particularly susceptible to direct oxidization as well as adduction by carbonyls produced from lipid and sugar oxidation. To understand the susceptibility of the cytoskeleton to oxidative modification and whether such modification is related to the physiological function of the cytoskeleton, we undertook a cytological analysis of motor neurons isolated from mouse spinal cord. These neurons contain an abundant axonal cytoskeleton that can be readily analyzed distinct from the cell body. Immunocytochemistry, using antibodies against protein-adducts of the highly reactive lipid peroxidation product, hydroxynonenal (HNE), representing Michael addition or pyrrole formation, revealed that HNE-immunoreactive adducts are found in all axons. This in situ distribution of HNE-adducts is consistent with immunoblots prepared from axons which show selective HNE modification of neurofilament heavy subunit (NFH) but not of other cytoskeletal proteins.
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Paradžik, Tina, Iva I. Podgorski, Tanja Vojvoda Zeljko, and Mladen Paradžik. "Ancient Origins of Cytoskeletal Crosstalk: Spectraplakin-like Proteins Precede the Emergence of Cortical Microtubule Stabilization Complexes as Crosslinkers." International Journal of Molecular Sciences 23, no. 10 (May 17, 2022): 5594. http://dx.doi.org/10.3390/ijms23105594.

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Adhesion between cells and the extracellular matrix (ECM) is one of the prerequisites for multicellularity, motility, and tissue specialization. Focal adhesions (FAs) are defined as protein complexes that mediate signals from the ECM to major components of the cytoskeleton (microtubules, actin, and intermediate filaments), and their mutual communication determines a variety of cellular processes. In this study, human cytoskeletal crosstalk proteins were identified by comparing datasets with experimentally determined cytoskeletal proteins. The spectraplakin dystonin was the only protein found in all datasets. Other proteins (FAK, RAC1, septin 9, MISP, and ezrin) were detected at the intersections of FAs, microtubules, and actin cytoskeleton. Homology searches for human crosstalk proteins as queries were performed against a predefined dataset of proteomes. This analysis highlighted the importance of FA communication with the actin and microtubule cytoskeleton, as these crosstalk proteins exhibit the highest degree of evolutionary conservation. Finally, phylogenetic analyses elucidated the early evolutionary history of spectraplakins and cortical microtubule stabilization complexes (CMSCs) as model representatives of the human cytoskeletal crosstalk. While spectraplakins probably arose at the onset of opisthokont evolution, the crosstalk between FAs and microtubules is associated with the emergence of metazoans. The multiprotein complexes contributing to cytoskeletal crosstalk in animals gradually gained in complexity from the onset of metazoan evolution.
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Chifflet, Silvia, and Julio A. Hernández. "The Plasma Membrane Potential and the Organization of the Actin Cytoskeleton of Epithelial Cells." International Journal of Cell Biology 2012 (2012): 1–13. http://dx.doi.org/10.1155/2012/121424.

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The establishment and maintenance of the polarized epithelial phenotype require a characteristic organization of the cytoskeletal components. There are many cellular effectors involved in the regulation of the cytoskeleton of epithelial cells. Recently, modifications in the plasma membrane potential (PMP) have been suggested to participate in the modulation of the cytoskeletal organization of epithelia. Here, we review evidence showing that changes in the PMP of diverse epithelial cells promote characteristic modifications in the cytoskeletal organization, with a focus on the actin cytoskeleton. The molecular paths mediating these effects may include voltage-sensitive integral membrane proteins and/or peripheral proteins sensitive to surface potentials. The voltage dependence of the cytoskeletal organization seems to have implications in several physiological processes, including epithelial wound healing and apoptosis.
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Scott, J. D. "A-kinase-anchoring proteins and cytoskeletal signalling events." Biochemical Society Transactions 31, no. 1 (February 1, 2003): 87–89. http://dx.doi.org/10.1042/bst0310087.

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Targeting of protein kinases and phosphatases to the cytoskeleton enhances the regulation of many signalling events. Cytoskeletal signalling complexes facilitate this process by optimizing the relay of messages from membrane receptors to specific sites on the actin cytoskeleton. These signals influence fundamental cell properties such as shape, movement and division. Targeting of the cAMP-dependent kinase (protein kinase A) and other enzymes to this compartment is achieved through interaction with A-kinase-anchoring proteins (AKAPs). The present paper discusses recent progress on dissecting the biological role of WAVE1 (Wiskott–Alrich syndrome protein family verprolin homology protein 1), an AKAP that assembles a cytoskeletal transduction complex in response to signals that emanate from the low-molecular-mass GTPase, Rac.
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Chinthalapudi, Krishna, Erumbi Rangarajan, Dipak Patil, and Tina Izard. "Lipid-directed cytoskeletal protein oligomerization at sites of cell adhesion." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C1833. http://dx.doi.org/10.1107/s2053273314081674.

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Vertebrate cell growth, division, migration, morphogenesis, and development, rely on the dynamic interactions of cells with components the extracellular matrix (ECM) via cell surface complexes. These focal adhesions (FAs) are comprised of integrin receptors, associated signaling molecules, and talin, which is required for "inside-out" signaling that stabilizes contacts of integrin receptors with the ECM by linking FAs to the actin cytoskeleton by binding to vinculin. The highly dynamic interactions with the actin cytoskeleton are also essential for the formation of membrane protrusions (lamellopodia and filopodia). Second messengers are found at the plasma cell membrane and include signaling lipids such as phosphoinositides, which play essential roles in signal transduction pathways and in directing the oligomerization of cytoskeletal proteins that function as essential links of FAs to the actin cytoskeleton. Notably, the most abundant phosphoinositide, phosphatidyl (4,5) bisphosphate (PIP2), directly binds to key cytoskeletal proteins, where it triggers homotypic and heterotypic interactions that amplify binding to the actin network. Binding of the inositol head group and the hydrophobic acyl chain pose difficulties in generating protein/PIP2 complex crystals and here we present the only second non-membrane protein structure of such a complex. Our crystal structure and biochemical approaches define the roles of PIP2 in controlling the oligomerization of cytoskeletal proteins and their binding to adhesion receptors and to the actin cytoskeleton. Importantly, we also determined the contribution of PIP2-directed oligomerization of cytoskeletal proteins to the formation and stabilization of adhesion complexes. These studies provide important new insights into how dynamic interactions of cytoskeletal proteins with the lipid membrane, adhesion complexes, and the actin network direct the mechanical behaviors of cells.
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Dissertations / Theses on the topic "Cytoskeletal proteins"

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Liu, Gang. "Cytoskeletal proteins of Dictyostelium." Thesis, University of Oxford, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.292634.

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Baisden, Joseph M. "AFAP-110 is a cSrc activator." Morgantown, W. Va. : [West Virginia University Libraries], 2003. http://etd.wvu.edu/templates/showETD.cfm?recnum=2766.

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Thesis (Ph. D.)--West Virginia University, 2003.
Title from document title page. Document formatted into pages; contains v, 149 p. : ill. (some col.). Vita. Includes abstract. Includes bibliographical references.
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Alwash, Ban Hussein Kadhim. "S100 proteins control cytoskeletal dynamics in cancer." Thesis, University of Leicester, 2018. http://hdl.handle.net/2381/42867.

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The S100 family of calcium binding proteins exhibits a unique pattern of cell type specific expression. These proteins are found in the cytoplasm and/or nucleus of a variety of cells, and involved in the control of a wide range of cellular processes such as cell cycle progression and differentiation. S100A4 and S100A6 are members of the S100 protein family that interact with several molecular targets including the heavy chain of non-muscle myosin IIA (NM IIA) and annexin II, respectively. NM IIA is a major actin-associated motor protein, which is involved in cell motility and cytokinesis. Assembly/disassembly of myosin filaments is primarily controlled by myosin light chain phosphorylation. However, small calcium-binding proteins of the S100 family also play an active role in the dynamics of actin-myosin filaments, leading to an increase in the dissemination of tumour cells. Accordingly, the main aim of this work was to study the molecular mechanism underlying S100A4/A6 function in epithelial mesenchymal transition (EMT) and provide in vivo data highlighting their role in the regulation of myosin dynamics. Intriguingly, we employed a novel transition electron microscopy approach to study the function of non-muscle IIA isoforms and their interactions with S100A4/A6 in A431/ZEB2 cells undergoing an EMT. Our data confirmed that both 6S and 10S myosin isoforms do exist in cells and directly interact with S100A4/A6 in vivo. Depletion of S100A4 resulted in the disappearance of the peaks corresponding to monomeric myosin indicating that S100A4 is required for balancing monomer-polymer equilibrium in cells. In blot overlay, both S100A4 and S100A6 showed similar binding site on myosin fragment 4 (C-terminus). However, a new S100A6 binding site was mapped on myosin heavy chain represented in M53 fragment which is a part of rod domain. In addition to the solubility of myosin in high ionic buffer, S100A4 and S100A6 are able to solubilise the myosin which was measured by the turbidity assay. Moreover, a decrease in ATPase activity of actomyosin complex in cells undergoing EMT was observed in the presence of S100A4/A6. In conclusion: This study shows that S100A4/A6 protein interacts with NM IIA. There is no redundancy and both proteins promote myosin dynamics, cell migration and invasion. S100A4 and S100A6 are up-regulated by ZEB2 and is implicated in the dynamic regulation of myosin filaments by switching the balance towards monomeric myosin.
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Snyder, Heidi Ghent. "Fiber type-specific desmin content in human single muscle fibers /." Diss., CLICK HERE for online access, 2006. http://contentdm.lib.byu.edu/ETD/image/etd1253.pdf.

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McCarthy, David James. "Analysis of the novel Lyn-associated cytoskeletal modular protein, LACM." University of Western Australia. School of Medicine and Pharmacology, 2009. http://theses.library.uwa.edu.au/adt-WU2009.0180.

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A yeast-two hybrid screen with Lyn identified a novel 130 kDa multidomain protein with a 36% identity to Actin Filament Associated Protein (AFAP) 110 and similar domains, including PH domains, potential sites of tyrosine and serine/threonine phosphorylation, a leucine-zipper domain, a potential actin binding site and multimerization site. AFAP110 has been shown to have a role in modulating actin filament integrity and induce lamellipodia formation, and is known to interact with Src family kinases. The aim of this thesis was to characterize this novel protein named Lyn-Associated Cytoskeletal Modulator (LACM) and determine any molecular interactions in order to attempt to elucidate a role for the protein in cell signaling through Lyn. LACM is encoded by a gene consisting of 18 exons and is located on human chromosome 5q33.1 and mouse chromosome 18 E1. LACM protein is expressed through a number of cell types including the R11 erythroid cell line, and mouse tissues including brain, lung, heart and embryos. LACM was shown to multimerize, and subcellular localization of the protein was observed to concentrate around the cell membrane at sites of filamentous actin in filopodia, lamellipodia and stress fibres. The carboxy-terminus of LACM was observed to localize the protein to sites at the cell membrane and through the cytoplasm. Removal of this terminal region resulted in all LACM protein localizing to the nucleus in punctuate spots. LACM protein was observed in heart muscle and potentially has a role at sites of nerve junctions on cardiac myocytes. LACM was shown to interact with the SH3 domain of Lyn at a polyproline motif on LACM. LACM was observed to co-localize and co-immunoprecipitate with Lyn and was tyrosine phosphorylated by the kinase domain of Lyn. Interestingly, the consititutively active Lyn and LACM caused transfected cells to
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MacDonald, Louisa M. "Characterisation of the benzimidazole-binding site on the cytoskeletal protein tubulin." Thesis, MacDonald, Louisa M. (2003) Characterisation of the benzimidazole-binding site on the cytoskeletal protein tubulin. PhD thesis, Murdoch University, 2003. https://researchrepository.murdoch.edu.au/id/eprint/173/.

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The binding kinetics of several benzimidazole compounds were determined with recombinant tubulin monomers and heterodimers from benzimidazole-sensitive and -insensitive organisms. This study utilised the naturally occurring high efficacy of the benzimdazoles for the parasitic protozoa Giardia duodenalis and Encephalitozoon intestinalis. The benzimidazoles are not active against the protozoan Cryptosporidium parvum or mammalian hosts, including humans. The affinity of several benzimidazole derivatives for monomeric and heterodimeric beta-tubulin was clearly demonstrated, thus supporting previous studies of drug-resistant nematode and fungal populations. A homology model of protozoan alpha beta-tubulin, produced using the three-dimensionalstructure of mammalian alpha beta-tubulin, identified a strongly hydrophobic domain only on the beta-tubulin protein of sensitive protozoa. This domain is proposed to be the benzimidazole-binding domain and the amino acid residues within it include three key residues which are substituted between benzimidazole-sensitive and -insensitive organisms. These residues are Ile-189, Val-199, and Phe-200 that all have non-polar, hydrophobic side groups and are proposed to bind with the R5 side chain of several benzimidazole derivatives. In addition to this, the benzimidazole derivatives were able to bind irreversibly with assembling microtubules from sensitive parasites. The incorporation of benzimidazole-bound alpha beta-heterodimers into assembling microtubules was shown to arrest polymerisation in vitro although the addition of benzimidazole compounds to assembled microtubules did not result in depolymerisation. Taken together, these results suggest that the mechanism of action of these compounds is through disruption of the dynamic equilibrium that balances the cycle of microtubule polymerisation and disintegration within these protozoa. Further, this effect is brought about by preferential binding of the benzimidazoles to a hydrophobic region on the beta-tubulin protein.
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MacDonald, Louisa M. "Characterisation of the benzimidazole-binding site on the cytoskeletal protein tubulin." Murdoch University, 2003. http://wwwlib.murdoch.edu.au/adt/browse/view/adt-MU20050107.94048.

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The binding kinetics of several benzimidazole compounds were determined with recombinant tubulin monomers and heterodimers from benzimidazole-sensitive and -insensitive organisms. This study utilised the naturally occurring high efficacy of the benzimdazoles for the parasitic protozoa Giardia duodenalis and Encephalitozoon intestinalis. The benzimidazoles are not active against the protozoan Cryptosporidium parvum or mammalian hosts, including humans. The affinity of several benzimidazole derivatives for monomeric and heterodimeric â-tubulin was clearly demonstrated, thus supporting previous studies of drug-resistant nematode and fungal populations. A homology model of protozoan áâ-tubulin, produced using the three-dimensionalstructure of mammalian áâ-tubulin, identified a strongly hydrophobic domain only on the â-tubulin protein of sensitive protozoa. This domain is proposed to be the benzimidazole-binding domain and the amino acid residues within it include three key residues which are substituted between benzimidazole-sensitive and –insensitive organisms. These residues are Ile-189, Val-199, and Phe-200 that all have non-polar, hydrophobic side groups and are proposed to bind with the R5 side chain of several benzimidazole derivatives. In addition to this, the benzimidazole derivatives were able to bind irreversibly with assembling microtubules from sensitive parasites. The incorporation of benzimidazole-bound áâ-heterodimers into assembling microtubules was shown to arrest polymerisation in vitro although the addition of benzimidazole compounds to assembled microtubules did not result in depolymerisation. Taken together, these results suggest that the mechanism of action of these compounds is through disruption of the dynamic equilibrium that balances the cycle of microtubule polymerisation and disintegration within these protozoa. Further, this effect is brought about by preferential binding of the benzimidazoles to a hydrophobic region on the â- tubulin protein.
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Ritchie, Sian. "Identification of cytoskeletal proteins as substrates for Ca'2'+ dependent protein kinase." Thesis, University of Reading, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.240317.

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Höng, J. "Investigating the structures of evolutionarily conserved cytoskeletal proteins." Thesis, University of Cambridge, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.604097.

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The parasitic protist Giardia intestinalis, considered to be one of the most ancient eukaryotic organisms, contains a typical eukaryotic cytoskeleton composed of microtubules (αβ-tubulin), microfilaments (actin) and intermediate filaments. Proteins associated with the microtubules include kinesins and additional members of the tubulin superfamily. δ-Tubulin is a member of the tubulin superfamily. The methylotropic yeast P. pastoris was identified as the most suitable host for recombinant expression of G. intestinalis δ-tubulin. High-resolution crystal structures of G. intestinalis wild-type kinesin-2 GiKIN2a motor domain with docked neck linker and its hydrolysis deficient mutant GiKIN2aT104N, expressed in and purified from E. coli, were solved in complex with ADP and Mg2+ at 1.6 Å and 1.8 Å resolutions, respectively. They represent the first high-resolution structures of a kinesin-2 motor domain. They confirm that the structural fold of the kinesin motor domain is remarkably conserved and also provide insights into the nucleotide coordination within its active site. Furthermore, in vivo experiments confirmed the role of G. intestinalis kinesin-2 in intraflagellar transport. Previously, structural and functional homologues of eukaryotic cytoskeletal proteins have been identified in prokaryotes. In magnetotactic bacteria, magnetosomes are held in place by cytoskeletal filaments formed by a protein, MamK, that is predicted to be actin-like. Magnetospirillum magnetotacticum MamK was expressed, purified and crystallised with apparent space group P321 and P422. However, these crystals appear to be perfectly twinned and thus determination of MamK structure has not yet been possible. Electron microscopy analysis of filamentous sheets, assembled from MamK in the presence of AMPPCP nucleotide, showed a longitudinal repeat of 53 Å, characteristic for actin-like protofilaments.
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Holmes, Fiona Elizabeth. "A study of cytoskeletal proteins in the neuron." Thesis, University of Kent, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.242927.

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Books on the topic "Cytoskeletal proteins"

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Thomas, Kreis, and Vale Ronald, eds. Guidebook to the cytoskeletal and motor proteins. Oxford: Oxford University Press, 1993.

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Thomas, Kreis, and Vale Ronald, eds. Guidebook to the cytoskeletal and motor proteins. 2nd ed. Oxford: Oxford University Press, 1999.

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D, Burgoyne Robert, ed. The Neuronal cytoskeleton. New York: Wiley-Liss, 1991.

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Osada, Yoshihito, Ryuzo Kawamura, and Ken-Ichi Sano. Hydrogels of Cytoskeletal Proteins. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-27377-8.

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Aebi, Ueli, and Jürgen Engel, eds. Cytoskeletal and Extracellular Proteins. Berlin, Heidelberg: Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-73925-5.

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B, Amos W., ed. Molecules of the cytoskeleton. New York: Guilford Press, 1991.

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Cytoskeleton methods and protocols. 2nd ed. New York, NY: Humana Press, 2009.

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C, Froehner Stanley, and Bennett Vann, eds. Cytoskeletal regulation of membrane function. New York: Rockefeller University Press, 1997.

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M, Osborn, Weber Klaus Dr Prof, and Banbury Center, eds. Cytoskeletal proteins in tumor diagnosis. Cold Spring Harbor, N.Y: Cold Spring Harbor Laboratory, 1989.

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Akademie der Wissenschaften und der Literatur (Germany) International Symposium. Nature and function of cytoskeletal proteins in motility and transport: International Symposium of the Akademie der Wissenschaften und der Literatur, Mainz, October 9th-11th, 1986. Stuttgart: Fischer, 1987.

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Book chapters on the topic "Cytoskeletal proteins"

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Osada, Yoshihito, Ryuzo Kawamura, and Ken-Ichi Sano. "Why Cytoskeletal Gel?" In Hydrogels of Cytoskeletal Proteins, 7–19. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-27377-8_2.

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Isenberg, Gerhard. "Plasmamembrane and Organelle-Associated Cytoskeletal Proteins." In Cytoskeleton Proteins, 231–57. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79632-6_12.

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Quinlan, Roy. "Cytoskeletal Competence Requires Protein Chaperones." In Small Stress Proteins, 219–33. Berlin, Heidelberg: Springer Berlin Heidelberg, 2002. http://dx.doi.org/10.1007/978-3-642-56348-5_12.

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Osada, Yoshihito, Ryuzo Kawamura, and Ken-Ichi Sano. "Why Polymer Gel?" In Hydrogels of Cytoskeletal Proteins, 1–5. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-27377-8_1.

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Osada, Yoshihito, Ryuzo Kawamura, and Ken-Ichi Sano. "Actin Gel." In Hydrogels of Cytoskeletal Proteins, 21–34. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-27377-8_3.

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Osada, Yoshihito, Ryuzo Kawamura, and Ken-Ichi Sano. "Microtubule Gel." In Hydrogels of Cytoskeletal Proteins, 35–58. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-27377-8_4.

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Osada, Yoshihito, Ryuzo Kawamura, and Ken-Ichi Sano. "Tropomyosin Gel." In Hydrogels of Cytoskeletal Proteins, 59–70. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-27377-8_5.

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Osada, Yoshihito, Ryuzo Kawamura, and Ken-Ichi Sano. "Summary of the MHSMG." In Hydrogels of Cytoskeletal Proteins, 71. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-27377-8_6.

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Osada, Yoshihito, Ryuzo Kawamura, and Ken-Ichi Sano. "Biomimetic Functions of Synthetic Polymer Gels." In Hydrogels of Cytoskeletal Proteins, 73–79. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-27377-8_7.

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Bershadsky, Alexander D., and Juri M. Vasiliev. "Regulation of Synthesis of Cytoskeletal Proteins." In Cytoskeleton, 203–16. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4684-5278-5_7.

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Conference papers on the topic "Cytoskeletal proteins"

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Fujimura, K., T. Fujimoto, M. Takemoto, K. Oda, S. Maehama, and A. Kuramoto. "INTERACTION OF MEMBRANE GLYCOPROTEIN GPIIb AND Ilia WITH CYTOSKELETAL PROTEINS DURING PLATELET ACTIVATION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643515.

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Experiments were designed and performed to analyse the cytoskeleton assembly and the interaction of glycoprotein (GP)IIb, IIIa and cytoskeletal proteins during platelet activation. A23187 stimulated 125I labeled platelets were solubilised with Triton X-100 solution and centrifuged. The insoluble fraction were analysed by two dimensional electrophoresis and the soluble fraction were fractionated with 5-25% sucrose gradient centrifugation and analysed by SDS PAGE. In Triton X-100 insoluble fraction, high molecular weight protein fraction(MW > 106) was present after stimulation which were consisted of actin binding protein(ABP), myosin heavy chain(MHC), actin and GPIIb and IIIa. And some of the ABP and MHC formed dimer. ABP and actin in this fraction were decreased with 1 mM CaCl2 treatment but the reduction of ABP was inhibited by leupeptm. In Triton X-100 soluble fraction after stimulation, some of the ABP, MHC, P235 protein, actin and small amount of GPIIb, IIIa were sedimented in the same high density fraction but most proteins were sedimented as a monomer form or GPIIb-IIIa complex form. The GPIIb, IIIa incorporation in high molecular weight protein fraction or high density fraction was absent in Ca++ chelating condition or the presence of competitive fibrinogen binding inhibitor which blocked the platelet aggregation. It is concluded that cytoskeletal proteins and GPIIb, IIIa are assembled each other and formed high molecular weight protein fraction or dimer formation during activation. In stimulated platelets these assembled cytoskeletal proteins containing GPIIb, IIIa were also found in Triton X-100 soluble fraction as a precursor of high molecular weight fraction in Triton X-100 insoluble fraction. The binding of fibrinogen to GPIIb-IIIa complex induce the linkage of GPIIb, IIIa to assembled cytoskeletal proteins.
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Allen, Kathleen B., and Bradley Layton. "A Mechanical Model for Cytoskeleton and Membrane Interactions in Neuronal Growth Cones." In ASME 2007 International Mechanical Engineering Congress and Exposition. ASMEDC, 2007. http://dx.doi.org/10.1115/imece2007-42008.

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Revealing the molecular events of neuronal growth is critical to obtaining a deeper understanding of nervous system development, neural injury response, and neural tissue engineering. Central to this is the need to understand the mechanical interactions among the cytoskeleton and the cell membrane, and how these interactions affect the overall growth mechanics of neurons. Using ANSYS, the force produced by a cytoskeletal protein acting against a deformable membrane was modeled, and the deformation, stress, and strain were computed for the membrane. Parameters to represent the flexural rigidities of the well-studied actin and tubulin cytoskeletal proteins as well as the mechanical properties of neuronal growth cones were used in the simulations. Our model predicts that while a single actin filament is able to produce a force sufficient to cause membrane deformation and thus growth, it is also possible that the actin filament may cause the membrane to rupture, if a dilatational strain of more than 3–4% occurs. Additionally, neurotoxins or pharmaceuticals that alter the mechanical properties of either the cell membrane or cytoskeletal proteins could disrupt the balance of forces required for neurons to not only push out and grow correctly, but also to sustain their shapes as high-aspect-ratio structures once growth is complete. Understanding how cytoskeletal elements have coevolved mechanically with their respective cell membranes will yield insights into the events that gave rise to the sequences and quaternary structures of the major cytoskeletal elements.
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Pryse, Kenneth M., Teresa M. Abney, Guy M. Genin, and Elliot L. Elson. "Probing Cytoskeletal Mechanics Using Biochemical Inhibitors." In ASME 2010 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2010. http://dx.doi.org/10.1115/sbc2010-19451.

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Quantifying the mechanics of the cytoskeletons of living cells is important for understanding several physiologic and pathologic cellular functions, such as wound healing and cellular migration in cancer. Our laboratory develops three-dimensional tissue constructs for assaying cytoskeletal mechanics in controlled conditions. These tissue constructs consist of defined components such as chick embryo fibroblasts and reconstituted rat tail collagen; fibroblasts remodel the collagen extracellular matrix (ECM) and develop a structural environment representative of that which would exist in a natural tissue. Our protocol for quantifying the microscale mechanics of the proteins that comprise the cytoskeleton involves mechanical testing of a tissue construct first in a bath that contains nutrition medium to support the active physiologic functioning of the cells, and next in the presence of inhibitors that selectively eliminate specific cytoskeletal structures. By solving an inverse homogenization problem, the mechanical functioning of these proteins at the cellular level can be estimated. Here, we present a combination of mechanical testing and imaging results to quantify the effects of specific inhibitors on cytoskeletal and extracellular matrix form and function.
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Bathe, Mark, Claus Heussinger, Mireille Claessens, Andreas Bausch, and Erwin Frey. "Cytoskeletal Bundle Mechanics." In ASME 2007 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2007. http://dx.doi.org/10.1115/sbc2007-176170.

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Filamentous actin (F-actin) is a stiff biopolymer that is tightly crosslinked in vivo by actin-binding proteins (ABPs) to form stiff bundles that form major constituents of a multitude of slender cytoskeletal processes including stereocilia, filopodia, microvilli, neurosensory bristles, cytoskeletal stress fibers, and the acrosomal process of sperm cells (Fig. 1). The mechanical properties of these cytoskeletal processes play key roles in a broad range of cellular functions — the bending stiffness of stereocilia mediates the mechanochemical transduction of mechanical stimuli such as acoustic waves to detect sound, the critical buckling load of filopodia and acrosomal processes determines their ability to withstand compressive mechanical forces generated during cellular locomotion and fertilization, and the entropic stretching stiffness of cytoskeletal bundles mediates cytoskeletal mechanical resistance to cellular deformation. Thus, a detailed understanding of F-actin bundle mechanics is fundamental to gaining a mechanistic understanding of cytoskeletal function.
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Kaazempur-Mofrad, Mohammad R., Peter J. Mack, Helene Karcher, Javad Golji, and Roger G. Kamm. "Stress-Induced Mechanotransduction: Some Preliminaries." In ASME 2003 International Mechanical Engineering Congress and Exposition. ASMEDC, 2003. http://dx.doi.org/10.1115/imece2003-43215.

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Mechanical stimuli affect nearly every aspect of cellular function, yet the underlying mechanisms of transduction of force into biochemical signals are not clearly understood. One hypothesis is that forces transmitted via individual proteins, either at the site of cell adhesion to its surroundings or within the stress-bearing members of the cytoskeleton, cause conformational changes that change their binding affinity to other intracellular molecules. This altered equilibrium state can subsequently initiate biochemical signaling cascades of produce immediate structural changes. This paper addresses the distribution of forces within the cell resulting from specific mechanical stimuli, computed using a 3-D multi compartment, continuum, viscoelastic finite element model, and uses these to estimate the forces transmitted by individual proteins and protein complexes. These levels of force are compared to those known to produce conformational changes in cytoskeletal proteins, as speculated from magnetocytometry observations and computed by molecular dynamics.
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verhallen, P. F. J., E. M. Bevers, P. Comfurius, W. M. A. Linkskens, and R. F. A. Zwaal. "CALPAIN-MEDIATED CYTOSKELETAL DEGRADATION CORRELATES WITH STIMULATION OF PLATELET PROCOAGULANT ACTIVITY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642821.

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We have shown earlier that the negatively charged phospholipid phosphatidylserine (PS), which becomes translocated from the inner surface to the outer surface of the plasma membrane upon platelet activation, is responsible for platelet procoagulant activity. Studies with erythrocytes have suggested a role for cytoskeletal proteins in the regulation of transmembrane asymmetry of PS. The possibility that platelet cytoskeletal proteins are involved in the loss of transmembrane asymmetry of PS, was explored by correlative investigations of both platelet prooagulant activity and activity of calpain, an endogenous Ca 2+ -dependent thiol-protease, known to hydrolyze major cytoskeletal proteins (e.g.: filamin, talin, myosin). Platelet procoagulant activity was assayed by determination of the prothrombinase activity under conditions at which the catalytic PS-surface was rate-limiting. Calpain-activity was monitored by the appearance of known degradation products of major cytoskeletal proteins. The following results were obtained: (1) The ability of thrombin, collagen, collagen & thrombin, or the Ca -ionophore A23187 to stimulate platelet procoagulant activity closely correlated with their ability to stimulate platelet calpain-activity (2). Generation of platelet procoagulant activity upon platelet stimulation by collagen & thrombin or by A23187 exhibited a time course identical to the development of calpain-activity. In addition, the local anesthetics dibucaine and tetracaine, shown to gradually stimulate calpain activity, were able to generate platelet procoagulant activity with a similar time course. (3) Using a Ca2+ buffering system and A23187 to equilibrate intracellular- and extracellular free Ca2+ , it was found that the Ca2+ -response relationship of both platelet calpain- and pro-coagulant-activity was identical. From these findings we conclude that the degradation of cytoskeletal proteins destroys their putative interactions with PS, enabling this lipid to participate in transbilayer movement, leading to the formation of a procoagulant outer surface of the platelet.
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Ronan, William, Vikram S. Deshpande, Robert M. McMeeking, and J. Patrick McGarry. "Simulation of Stress Fiber Remodeling and Mixed-Mode Focal Adhesion Assembly During Cell Spreading and for Cells Adhered to Elastic Substrates." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53878.

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Cell spreading is governed by two cooperative cellular processes: the association of binding proteins to form focal adhesions, and the active remodeling of the actin cytoskeleton as the cell spreads [1]. The interaction between these two processes is poorly understood, and previous computational models have only examined each process in isolation. Previous studies have established that cells possess the ability to sense and react to their physical environment, for example cells seeded on substrates of varying stiffness exhibit a different cytoskeletal response [2,3].
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Dangaria, Jhanvi H., and Peter J. Butler. "Interaction of Shear Stress, Myosin II, and Actin in Dynamic Modulation of Endothelial Cell Microrheology." In ASME 2008 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2008. http://dx.doi.org/10.1115/sbc2008-192947.

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The endothelial cell (EC) cytoskeleton mediates several biological functions such as adhesion, migration, phagocytosis, cell division, and mechanosensitivity. These functions are carried out in part through dynamic cytoskeletal polymerization, modulation of crosslinking, and development of tension between intracellular organelles and the extracellular matrix via focal adhesion plaques. One important component of the cytoskeleton is actin which polymerizes into filaments and is thought to be prestressed by virtue of crosslinking proteins such as α-actinin, filamin and myosin II molecular motors. Additionally, actomyosin interaction has been hypothesized to act as a stress dissipation mechanism by virtue of dynamic crossbridging which facilitates actin diffusion through the polymer network of the cytoplasm (Humphrey et al., 2002).
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Anders, Katie L., Kylie B. R. Belchamber, Peter J. Barnes, and Louise E. Donnelly. "Differential phosphorylation patterns of macrophage cytoskeletal proteins in COPD following phagocytosis." In ERS International Congress 2019 abstracts. European Respiratory Society, 2019. http://dx.doi.org/10.1183/13993003.congress-2019.pa1671.

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Wilkinson, J. M., N. Hack, L. I. Thorsen, and J. A. Thomas. "MONOCLONAL ANTIBODIES RECOGNISING PROTEINS OF THE OUTER AND INNER SURFACE OF THE PLATELET PLASMA MEMBRANE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644493.

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Platelet membrane preparations can be fractionated into two major subpopulations by free flow electrophoresis and these have been shown to correspond to the plasma membrane and the endoplasmic reticulum of the platelet. The plasma membrane fraction can be shown, by two-dimensional electrophoresis, to contain the major surface glycoproteins together with considerable amounts of actin and actin-associated proteins such as the 250 kDa actin-binding protein (filamin), P235 (talin), myosin, α-actinin and tropomyosin (Hack, N. … Crawford, N., Biochem. J. 222, 235 (1984). These cytoskeletal proteins are associated with the cytoplasmic face of the plasma membrane and probably interact with transmembrane glycoproteins. We have raised monoclonal antibodies to the purified plasma membrane preparation in order to investigate the nature of these glycoprotein-cytoskeletal interactions. In two fusion experiments, out of 804 tested, 104 hybrids secreted antibody to the membrane preparation and of these 24 were selected for further study. Initial assays were by ELISA using either the membrane preparation or whole fixed platelets as the target antigen. The specificity of the antibodies was investigated further by immunoblotting of SDS gels of total platelet proteins prepared under reducing and nonreducing conditions, by immunofluorescence, by immunohisto-chemistry and by crossed immunoelectrophoresis. The majority of the antibodies recognise major surface glycoproteins; of these, four bind to glycoprotein Ib under all conditions examined while another seven recognise the glycoprotein IIb/IIIa complex as detected by crossed immunoelectrophoresis. Three antibodies recognise the actin binding protein and these cross-react with the smooth muscle protein filamin in a number of different species. Further characterisation of these antibodies in both structural and functional terms will be presented.We are grateful to the Smith and Nephew Foundation for financial support for these studies
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Reports on the topic "Cytoskeletal proteins"

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Sadot, Einat, Christopher Staiger, and Zvi Kam Weizmann. functional genomic screen for new plant cytoskeletal proteins and the determination of their role in actin mediated functions and guard cells regulation. United States Department of Agriculture, January 2003. http://dx.doi.org/10.32747/2003.7587725.bard.

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The original objectives of the approved proposal were: 1. To construct a YFP fused Arabidopsis cDNA library in a mammalian expression vector. 2. To infect the library into a host fibroblast cell line and to screen for new cytoskeletal associated proteins using an automated microscope. 3. Isolate the new genes. 4. Characterize their role in plants. The project was approved as a feasibility study to allow proof of concept that would entail building the YFP library and picking up a couple of positive clones using the fluorescent screen. We report here on the construction of the YFP library, the development of the automatic microscope, the establishment of the screen and the isolation of positive clones that are plant cDNAs encoding cytoskeleton associated proteins. The rational underling a screen of plant library in fibroblasts is based on the high conservation of the cytoskeleton building blocks, actin and tubulin, between the two kingdoms (80-90% homology at the level of amino acids sequence). In addition, several publications demonstrated the recognition of mammalian cytoskeleton by plant cytoskeletal binding proteins and vice versa. The major achievements described here are: 1. The development of an automated microscope equipped with fast laser auto-focusing for high magnification and a software controlling 6 dimensions; X, Y position, auto focus, time, color, and the distribution and density of the fields acquired. This system is essential for the high throughput screen. 2. The construction of an extremely competent YFP library efficiently cloned (tens of thousands of clones collected, no empty vectors detected) with all inserts oriented 5't03'. These parameters render it well representative of the whole transcriptome and efficient in "in-frame" fusion to YFP. 3. The strategy developed for the screen allowing the isolation of individual positive cDNA clones following three rounds of microscopic scans. The major conclusion accomplished from the work described here is that the concept of using mammalian host cells for fishing new plant cytoskeletal proteins is feasible and that screening system developed is complete for addressing one of the major bottlenecks of the plant cytoskeleton field: the need for high throughput identification of functionally active cytoskeletal proteins. The new identified plant cytoskeletal proteins isolated in the pilot screen and additional new proteins which will be isolated in a comprehensive screen will shed light on cytoskeletal mediated processes playing a major role in cellular activities such as cell division, morphogenesis, and functioning such as chloroplast positioning, pollen tube and root hair elongation and the movement of guard cells. Therefore, in the long run the screen described here has clear agricultural implications.
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Sadot, Einat, Christopher Staiger, and Mohamad Abu-Abied. Studies of Novel Cytoskeletal Regulatory Proteins that are Involved in Abiotic Stress Signaling. United States Department of Agriculture, September 2011. http://dx.doi.org/10.32747/2011.7592652.bard.

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In the original proposal we planned to focus on two proteins related to the actin cytoskeleton: TCH2, a touch-induced calmodulin-like protein which was found by us to interact with the IQ domain of myosin VIII, ATM1; and ERD10, a dehydrin which was found to associate with actin filaments. As reported previously, no other dehydrins were found to interact with actin filaments. In addition so far we were unsuccessful in confirming the interaction of TCH2 with myosin VIII using other methods. In addition, no other myosin light chain candidates were found in a yeast two hybrid survey. Nevertheless we have made a significant progress in our studies of the role of myosins in plant cells. Plant myosins have been implicated in various cellular activities, such as cytoplasmic streaming (1, 2), plasmodesmata function (3-5), organelle movement (6-10), cytokinesis (4, 11, 12), endocytosis (4, 5, 13-15) and targeted RNA transport (16). Plant myosins belong to two main groups of unconventional myosins: myosin XI and myosin VIII, both closely related to myosin V (17-19). The Arabidopsis myosin family contains 17 members: 13 myosin XI and four myosin VIII (19, 20). The data obtained from our research of myosins was published in two papers acknowledging BARD funding. To address whether specific myosins are involved with the motility of specific organelles, we cloned the cDNAs from neck to tail of all 17 Arabidopsis myosins. These were fused to GFP and used as dominant negative mutants that interact with their cargo but are unable to walk along actin filaments. Therefore arrested organelle movement in the presence of such a construct shows that a particular myosin is involved with the movement of that particular organelle. While no mutually exclusive connections between specific myosins and organelles were found, based on overexpression of dominant negative tail constructs, a group of six myosins (XIC, XIE, XIK, XI-I, MYA1 and MYA2) were found to be more important for the motility of Golgi bodies and mitochondria in Nicotiana benthamiana and Nicotiana tabacum (8). Further deep and thorough analysis of myosin XIK revealed a potential regulation by head and tail interaction (Avisar et al., 2011). A similar regulatory mechanism has been reported for animal myosin V and VIIa (21, 22). In was shown that myosin V in the inhibited state is in a folded conformation such that the tail domain interacts with the head domain, inhibiting its ATPase and actinbinding activities. Cargo binding, high Ca2+, and/or phosphorylation may reduce the interaction between the head and tail domains, thus restoring its activity (23). Our collaborative work focuses on the characterization of the head tail interaction of myosin XIK. For this purpose the Israeli group built yeast expression vectors encoding the myosin XIK head. In addition, GST fusions of the wild-type tail as well as a tail mutated in the amino acids that mediate head to tail interaction. These were sent to the US group who is working on the isolation of recombinant proteins and performing the in vitro assays. While stress signals involve changes in Ca2+ levels in plants cells, the cytoplasmic streaming is sensitive to Ca2+. Therefore plant myosin activity is possibly regulated by stress. This finding is directly related to the goal of the original proposal.
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Epel, Bernard, and Roger Beachy. Mechanisms of intra- and intercellular targeting and movement of tobacco mosaic virus. United States Department of Agriculture, November 2005. http://dx.doi.org/10.32747/2005.7695874.bard.

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To cause disease, plant viruses must replicate and spread locally and systemically within the host. Cell-to-cell virus spread is mediated by virus-encoded movement proteins (MPs), which modify the structure and function of plasmodesmata (Pd), trans-wall co-axial membranous tunnels that interconnect the cytoplasm of neighboring cells. Tobacco mosaic virus (TMV) employ a single MP for cell- cell spread and for which CP is not required. The PIs, Beachy (USA) and Epel (Israel) and co-workers, developed new tools and approaches for study of the mechanism of spread of TMV that lead to a partial identification and molecular characterization of the cellular machinery involved in the trafficking process. Original research objectives: Based on our data and those of others, we proposed a working model of plant viral spread. Our model stated that MPᵀᴹⱽ, an integral ER membrane protein with its C-terminus exposed to the cytoplasm (Reichel and Beachy, 1998), alters the Pd SEL, causes the Pd cytoplasmic annulus to dilate (Wolf et al., 1989), allowing ER to glide through Pd and that this gliding is cytoskeleton mediated. The model claimed that in absence of MP, the ER in Pd (the desmotubule) is stationary, i.e. does not move through the Pd. Based on this model we designed a series of experiments to test the following questions: -Does MP potentiate ER movement through the Pd? - In the presence of MP, is there communication between adjacent cells via ER lumen? -Does MP potentiate the movement of cytoskeletal elements cell to cell? -Is MP required for cell-to-cell movement of ER membranes between cells in sink tissue? -Is the binding in situ of MP to RNA specific to vRNA sequences or is it nonspecific as measured in vitro? And if specific: -What sequences of RNA are involved in binding to MP? And finally, what host proteins are associated with MP during intracellular targeting to various subcellular targets and what if any post-translational modifications occur to MP, other than phosphorylation (Kawakami et al., 1999)? Major conclusions, solutions and achievements. A new quantitative tool was developed to measure the "coefficient of conductivity" of Pd to cytoplasmic soluble proteins. Employing this tool, we measured changes in Pd conductivity in epidermal cells of sink and source leaves of wild-type and transgenic Nicotiana benthamiana (N. benthamiana) plants expressing MPᵀᴹⱽ incubated both in dark and light and at 16 and 25 ᵒC (Liarzi and Epel, 2005 (appendix 1). To test our model we measured the effect of the presence of MP on cell-to-cell spread of a cytoplasmic fluorescent probe, of two ER intrinsic membrane protein-probes and two ER lumen protein-probes fused to GFP. The effect of a mutant virus that is incapable of cell-to-cell spread on the spread of these probes was also determined. Our data shows that MP reduces SEL for cytoplasmic molecules, dilates the desmotubule allowing cell-cell diffusion of proteins via the desmotubule lumen and reduces the rate of spread of the ER membrane probes. Replicase was shown to enhance cell-cell spread. The data are not in support of the proposed model and have led us to propose a new model for virus cell-cell spread: this model proposes that MP, an integral ER membrane protein, forms a MP:vRNAER complex and that this ER-membrane complex diffuses in the lipid milieu of the ER into the desmotubule (the ER within the Pd), and spreads cell to cell by simple diffusion in the ER/desmotubule membrane; the driving force for spread is the chemical potential gradient between an infected cell and contingent non-infected neighbors. Our data also suggests that the virus replicase has a function in altering the Pd conductivity. Transgenic plant lines that express the MP gene of the Cg tobamovirus fused to YFP under the control the ecdysone receptor and methoxyfenocide ligand were generated by the Beachy group and the expression pattern and the timing and targeting patterns were determined. A vector expressing this MPs was also developed for use by the Epel lab . The transgenic lines are being used to identify and isolate host genes that are required for cell-to-cell movement of TMV/tobamoviruses. This line is now being grown and to be employed in proteomic studies which will commence November 2005. T-DNA insertion mutagenesis is being developed to identify and isolate host genes required for cell-to-cell movement of TMV.
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Zilberstein, Aviah, Bo Liu, and Einat Sadot. Studying the Involvement of the Linker Protein CWLP and its Homologue in Cytoskeleton-plasma Membrane-cell Wall Continuum and in Drought Tolerance. United States Department of Agriculture, June 2012. http://dx.doi.org/10.32747/2012.7593387.bard.

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The study has been focused on proline-rich proteins from the HyPRP family. Three proline-rich proteins have been characterized with the CWLP as the main objective. We showed that this unique protein is assembled in the plasma membrane (PM) and forms a continuum between the cell wall (CW) and cytosol via the PM. While spanning the PM, it is arranged in lipid rafts as CWLP-aquaporin complexes that recruit PP2A-β”, as a part of PP2A enzyme, close to the aquaporin moiety where it dephosphorylates two crucial Ser residues and induces closure of the aquaporin water channels. The closure of water channels renders cells more tolerant to plasmolysis and plants to dehydration. This unique effect was observed not only in Arabidopsis, but also in potato plants over expressing the CWLP, suggesting a possible usage in crop plants as a valve that reduces loss of water or/and elevates cold resistance. The CWLP is a member of the HyPRP protein family that all possess structurally similar 8CM domain, predicted to localize to PM lipid rafts. In this study, two additional highly homologous HyPRP proteins were also studied. The GPRP showed the same localization and it’s over expression increased tolerance to lack of water. However, the third one, PRP940, despite sharing high homology in the 8CM domain, is completely different and is assembled in parallel to cortical microtubules in the cell. Moreover, our data suggest that this protein is not involved in rendering plants resistant to lack of water. We suggest implying CWLP as a tool for better regulation of water maintenance in crop plants.
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Ramesh, Vijaya. Neurofibromatosis 2 Tumor Suppressor Protein, Merlin, in Cellular Signaling to Actin Cytoskeleton. Fort Belvoir, VA: Defense Technical Information Center, October 2000. http://dx.doi.org/10.21236/ada395581.

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Woloschak, G. E., P. Felcher, and Chin-Mei Chang-Liu. Expression of cytoskeletal and matrix genes following exposure to ionizing radiation: Dose-rate effects and protein synthesis requirements. Office of Scientific and Technical Information (OSTI), May 1994. http://dx.doi.org/10.2172/10148882.

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Woloschak, G. E., P. Felcher, and Chin-Mei Chang-Liu. Expression of cytoskeletal and matrix genes following exposure to ionizing radiation: Dose-rate effects and protein synthesis requirements. Office of Scientific and Technical Information (OSTI), June 1995. http://dx.doi.org/10.2172/70715.

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Woloschak, G. E., P. Felcher, and Chin-Mei Chang-Liu. Expression of cytoskeletal and matrix genes following exposure to ionizing radiation: Dose-rate effects and protein synthesis requirements. Office of Scientific and Technical Information (OSTI), December 1992. http://dx.doi.org/10.2172/10185724.

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Woloschak, G. E., P. Felcher, and Chin-Mei Chang-Liu. Expression of cytoskeletal and matrix genes following exposure to ionizing radiation: Dose-rate effects and protein synthesis requirements. Office of Scientific and Technical Information (OSTI), December 1993. http://dx.doi.org/10.2172/10130291.

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Philosoph-Hadas, Sonia, Peter Kaufman, Shimon Meir, and Abraham Halevy. Signal Transduction Pathway of Hormonal Action in Control and Regulation of the Gravitropic Response of Cut Flowering Stems during Storage and Transport. United States Department of Agriculture, October 1999. http://dx.doi.org/10.32747/1999.7695838.bard.

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Original objectives: The basic goal of the present project was to increase our understanding of the cellular mechanisms operating during the gravitropic response of cut flowers, for solving their bending problem without affecting flower quality. Thus, several elements operating at the 3 levels o the gravity-induced signal transduction pathway, were proposed to be examined in snapdragon stems according to the following research goals: 1) Signaling: characterize the signal transduction pathway leading to the gravitropic response, regarding the involvement of [Ca2+]cyt as a mediator of IAA movement and sensitivity to auxin. 2) Transduction by plant hormones: a) Examine the involvement of auxin in the gravitropic response of flower stems with regard to: possible participation of auxin binding protein (ABP), auxin redistribution, auxin mechanism of action (activation of H+-ATPase) mediation by changes in [Ca2+]cyt and possible regulation of auxin-induced Ca2+ action b: calmodulin-activated or Ca2+-activated protein kinases (PK). b) Examine the involvement of ethylene in the gravitropic response of flower stems with regard to auxin-induced ethylene production and sensitivity of the tissue to ethylene. 3) Response: examine the effect of gravistimulation on invertase (associated with growth and elongation) activity and invertase gene expression. 4) Commercial practice: develop practical and simple treatments to prevent bending of cut flowers grown for export. Revisions: 1) Model systems: in addition to snapdragon (Antirrhinum majus L.), 3 other model shoe systems, consisting of oat (Avena sativa) pulvini, Ornithogalun 'Nova' cut flowers and Arabidopsis thaliana inflorescence, were targeted to confirm a more general mechanism for shoot gravitropism. 2 Research topics: the involvement of ABP, auxin action, PK and invertase in the gravitropic response of snapdragon stems could not be demonstrated. Alternatively, the involvement in the gravity signaling cascade of several other physiological mediators apart of [Ca2+]cyt such as: IP3, protein phosphorylation and actin cytoskeleton, was shown. Additional topics introduced: starch statolith reorientation, differential expression of early auxin responsive genes, and differential shoot growth. Background to the topic: The gravitropic bending response of flowering shoots occurring upon their horizontal placement during shipment exhibits a major horticultural problem. In spite of extensive studies in various aboveground organs, the gravitropic response was hardly investigated in flowering shoots. Being a complex multistep process that requires the participation of various cellular components acting in succession or in parallel, analysis of the negative gravitropic response of shoot includes investigation of signal transduction elements and various regulatory physiological mediators. Major achievements: 1) A correlative role for starch statoliths as gravireceptors in flowering shoot was initially established. 2) Differentially phosphorylated proteins and IP3 levels across the oat shoe pulvini, as well as a differential appearance of 2 early auxin-responsive genes in snapdragon stems were all detected within 5-30 minutes following gravistimulation. 3) Unlike in roots, involvement of actin cytoskeleton in early events of the gravitropic response of snapdragon shoots was established. 4) An asymmetric IAA distribution, followed by an asymmetric ethylene production across snapdragon stems was found following gravistimulation. 5) The gravity-induced differential growth in shoots of snapdragon was derived from initial shrinkage of the upper stem side and a subsequent elongation o the lower stem side. 6) Shoot bending could be successfully inhibited by Ca2+ antagonists (that serve as a basis for practical treatments), kinase and phosphatase inhibitors and actin-cytoskeleton modulators. All these agents did not affect vertical growth. The essential characterization of these key events and their sequence led us to the conclusion that blocking gravity perception may be the most powerful means to inhibit bending without hampering shoot and flower growth after harvest. Implications, scientific and agriculture: The innovative results of this project have provided some new insight in the basic understanding of gravitropism in flower stalks, that partially filled the gap in our knowledge, and established useful means for its control. Additionally, our analysis has advanced the understanding of important and fundamental physiological processes involved, thereby leading to new ideas for agriculture. Gravitropism has an important impact on agriculture, particularly for controlling the bending of various important agricultural products with economic value. So far, no safe control of the undesired bending problem of flower stalks has been established. Our results show for the first time that shoot bending of cut flowers can be inhibited without adverse effects by controlling the gravity perception step with Ca2+ antagonists and cytoskeleton modulators. Such a practical benefit resulting from this project is of great economic value for the floriculture industry.
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