Journal articles on the topic 'Cytoskeletal proteins'
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1
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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Muñoz-Lasso, Diana C., Carlos Romá-Mateo, Federico V. Pallardó, and Pilar Gonzalez-Cabo. "Much More Than a Scaffold: Cytoskeletal Proteins in Neurological Disorders." Cells 9, no. 2 (February 4, 2020): 358. http://dx.doi.org/10.3390/cells9020358.
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Recent observations related to the structure of the cytoskeleton in neurons and novel cytoskeletal abnormalities involved in the pathophysiology of some neurological diseases are changing our view on the function of the cytoskeletal proteins in the nervous system. These efforts allow a better understanding of the molecular mechanisms underlying neurological diseases and allow us to see beyond our current knowledge for the development of new treatments. The neuronal cytoskeleton can be described as an organelle formed by the three-dimensional lattice of the three main families of filaments: actin filaments, microtubules, and neurofilaments. This organelle organizes well-defined structures within neurons (cell bodies and axons), which allow their proper development and function through life. Here, we will provide an overview of both the basic and novel concepts related to those cytoskeletal proteins, which are emerging as potential targets in the study of the pathophysiological mechanisms underlying neurological disorders.
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Ong, Mei Shan, Shuo Deng, Clarissa Esmeralda Halim, Wanpei Cai, Tuan Zea Tan, Ruby Yun-Ju Huang, Gautam Sethi, Shing Chuan Hooi, Alan Prem Kumar, and Celestial T. Yap. "Cytoskeletal Proteins in Cancer and Intracellular Stress: A Therapeutic Perspective." Cancers 12, no. 1 (January 18, 2020): 238. http://dx.doi.org/10.3390/cancers12010238.
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Cytoskeletal proteins, which consist of different sub-families of proteins including microtubules, actin and intermediate filaments, are essential for survival and cellular processes in both normal as well as cancer cells. However, in cancer cells, these mechanisms can be altered to promote tumour development and progression, whereby the functions of cytoskeletal proteins are co-opted to facilitate increased migrative and invasive capabilities, proliferation, as well as resistance to cellular and environmental stresses. Herein, we discuss the cytoskeletal responses to important intracellular stresses (such as mitochondrial, endoplasmic reticulum and oxidative stresses), and delineate the consequences of these responses, including effects on oncogenic signalling. In addition, we elaborate how the cytoskeleton and its associated molecules present themselves as therapeutic targets. The potential and limitations of targeting new classes of cytoskeletal proteins are also explored, in the context of developing novel strategies that impact cancer progression.
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Kingston, DD. "Cytoskeletal and Extracellular Proteins." Biochemical Education 17, no. 4 (October 1989): 222. http://dx.doi.org/10.1016/0307-4412(89)90173-8.
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Hutchings, Nathan R., John E. Donelson, and Kent L. Hill. "Trypanin is a cytoskeletal linker protein and is required for cell motility in African trypanosomes." Journal of Cell Biology 156, no. 5 (February 25, 2002): 867–77. http://dx.doi.org/10.1083/jcb.200201036.
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The cytoskeleton of eukaryotic cells is comprised of a complex network of distinct but interconnected filament systems that function in cell division, cell motility, and subcellular trafficking of proteins and organelles. A gap in our understanding of this dynamic network is the identification of proteins that connect subsets of cytoskeletal structures. We previously discovered a family of cytoskeleton-associated proteins that includes GAS11, a candidate human tumor suppressor upregulated in growth-arrested cells, and trypanin, a component of the flagellar cytoskeleton of African trypanosomes. Although these proteins are intimately associated with the cytoskeleton, their function has yet to be determined. Here we use double-stranded RNA interference to block trypanin expression in Trypanosoma brucei, and demonstrate that this protein is required for directional cell motility. Trypanin(−) mutants have an active flagellum, but are unable to coordinate flagellar beat. As a consequence, they spin and tumble uncontrollably, occasionally moving backward. Immunofluorescence experiments demonstrate that trypanin is located along the flagellum/flagellum attachment zone and electron microscopic analysis revealed that cytoskeletal connections between the flagellar apparatus and subpellicular cytoskeleton are destabilized in trypanin(−) mutants. These results indicate that trypanin functions as a cytoskeletal linker protein and offer insights into the mechanisms of flagellum-based cell motility.
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Zencheck, Wendy D., Hui Xiao, and Louis M. Weiss. "Lysine post-translational modifications and the cytoskeleton." Essays in Biochemistry 52 (May 25, 2012): 135–45. http://dx.doi.org/10.1042/bse0520135.
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PTMs (post-translational modifications) of lysine residues have proven to be major regulators of gene expression, protein–protein interactions, and protein processing and degradation. This is of particular importance in regulating the cytoskeleton, an enormously complex system of proteins responsible for cell motility, intracellular trafficking, and maintenance of cell form and structure. The cytoskeleton is present in all cells, including eukaryotes and prokaryotes, and comprises structures such as flagella, cilia and lamellipodia which play critical roles in intracellular transport and cellular division. Cytoskeletal regulation relies on numerous multi-component assemblies. In this chapter, we focus on the regulation of the cytoskeleton by means of PTMs of lysine residues on the cytoskeletal subunits and their accessory proteins. We specifically address the three main classes of cytoskeletal proteins in eukaryotes that polymerize into filaments, including microfilaments (actin filaments), intermediate filaments and microtubules. We discuss the identification and biological importance of lysine acetylation, a regulator of all three filament types. We also review additional lysine modifications, such as ubiquitination and SUMOylation, and their role in protein regulation and processing.
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Haglund, Cat M., and Matthew D. Welch. "Pathogens and polymers: Microbe–host interactions illuminate the cytoskeleton." Journal of Cell Biology 195, no. 1 (October 3, 2011): 7–17. http://dx.doi.org/10.1083/jcb.201103148.
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Intracellular pathogens subvert the host cell cytoskeleton to promote their own survival, replication, and dissemination. Study of these microbes has led to many discoveries about host cell biology, including the identification of cytoskeletal proteins, regulatory pathways, and mechanisms of cytoskeletal function. Actin is a common target of bacterial pathogens, but recent work also highlights the use of microtubules, cytoskeletal motors, intermediate filaments, and septins. The study of pathogen interactions with the cytoskeleton has illuminated key cellular processes such as phagocytosis, macropinocytosis, membrane trafficking, motility, autophagy, and signal transduction.
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Csortos, Csilla, Irina Kolosova, and Alexander D. Verin. "Regulation of vascular endothelial cell barrier function and cytoskeleton structure by protein phosphatases of the PPP family." American Journal of Physiology-Lung Cellular and Molecular Physiology 293, no. 4 (October 2007): L843—L854. http://dx.doi.org/10.1152/ajplung.00120.2007.
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Reversible phosphorylation of cytoskeletal and cytoskeleton-associated proteins is a significant element of endothelial barrier function regulation. Therefore, understanding the mechanisms of phosphorylation/dephosphorylation of endothelial cell cytoskeletal proteins is vital to the treatment of severe lung disorders such as high permeability pulmonary edema. In vivo, there is a controlled balance between the activities of protein kinases and phosphatases. Due to various external or internal signals, this balance may be shifted. The actual balances at a given time alter the phosphorylation level of certain proteins with appropriate physiological consequences. The latest information about the structure and regulation of different types of Ser/Thr protein phosphatases participating in the regulation of endothelial cytoskeletal organization and barrier function will be reviewed here.
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Li, Yuqiang, Dan Wang, Heming Ge, Cenap Güngör, Xuejun Gong, and Yongheng Chen. "Cytoskeletal and Cytoskeleton-Associated Proteins: Key Regulators of Cancer Stem Cell Properties." Pharmaceuticals 15, no. 11 (November 8, 2022): 1369. http://dx.doi.org/10.3390/ph15111369.
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Cancer stem cells (CSCs) are a subpopulation of cancer cells possessing stemness characteristics that are closely associated with tumor proliferation, recurrence and resistance to therapy. Recent studies have shown that different cytoskeletal components and remodeling processes have a profound impact on the behavior of CSCs. In this review, we outline the different cytoskeletal components regulating the properties of CSCs and discuss current and ongoing therapeutic strategies targeting the cytoskeleton. Given the many challenges currently faced in targeted cancer therapy, a deeper comprehension of the molecular events involved in the interaction of the cytoskeleton and CSCs will help us identify more effective therapeutic strategies to eliminate CSCs and ultimately improve patient survival.
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Kumeta, Masahiro, Shige H. Yoshimura, James Hejna, and Kunio Takeyasu. "Nucleocytoplasmic Shuttling of Cytoskeletal Proteins: Molecular Mechanism and Biological Significance." International Journal of Cell Biology 2012 (2012): 1–12. http://dx.doi.org/10.1155/2012/494902.
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Various nuclear functional complexes contain cytoskeletal proteins as regulatory subunits; for example, nuclear actin participates in transcriptional complexes, and actin-related proteins are integral to chromatin remodeling complexes. Nuclear complexes such as these are involved in both basal and adaptive nuclear functions. In addition to nuclear import via classical nuclear transport pathways or passive diffusion, some large cytoskeletal proteins spontaneously migrate into the nucleus in a karyopherin-independent manner. The balance of nucleocytoplasmic distribution of such proteins can be altered by several factors, such as import versus export, or capture and release by complexes. The resulting accumulation or depletion of the nuclear populations thereby enhances or attenuates their nuclear functions. We propose that such molecular dynamics constitute a form of cytoskeleton-modulated regulation of nuclear functions which is mediated by the translocation of cytoskeletal components in and out of the nucleus.
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Jackson, Wesley M., Michael J. Jaasma, Raymond Y. Tang, and Tony M. Keaveny. "Mechanical loading by fluid shear is sufficient to alter the cytoskeletal composition of osteoblastic cells." American Journal of Physiology-Cell Physiology 295, no. 4 (October 2008): C1007—C1015. http://dx.doi.org/10.1152/ajpcell.00509.2007.
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Many structural modifications have been observed as a part of the cellular response to mechanical loading in a variety of cell types. Although changes in morphology and cytoskeletal rearrangement have been widely reported, few studies have investigated the change in cytoskeletal composition. Measuring how the amounts of specific structural proteins in the cytoskeleton change in response to mechanical loading will help to elucidate cellular mechanisms of functional adaptation to the applied forces. Therefore, the overall hypothesis of this study was that osteoblasts would respond to fluid shear stress by altering the amount of specific cross-linking proteins in the composition of the cytoskeleton. Mouse osteoblats cell line MC3T3-E1 and human fetal osteoblasts (hFOB) were exposed to 2 Pa of steady fluid shear for 2 h in a parallel plate flow chamber, and then the amount of actin, vimentin, α-actinin, filamin, and talin in the cytoskeleton was measured using Western blot analyses. After mechanical loading, there was no change in the amount of actin monomers in the cytoskeleton, but the cross-linking proteins α-actinin and filamin that cofractionated with the cytoskeleton increased by 29% ( P < 0.01) and 18% ( P < 0.02), respectively. Localization of the cross-linking proteins by fluorescent microscopy revealed that they were more widely distributed throughout the cell after exposure to fluid shear. The amount of vimentin in the cytoskeleton also increased by 15% ( P < 0.01). These results indicate that osteoblasts responded to mechanical loading by altering the cytoskeletal composition, which included an increase in specific proteins that would likely enhance the mechanical resistance of the cytoskeleton.
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Mackay, A. M., D. M. Eckley, C. Chue, and W. C. Earnshaw. "Molecular analysis of the INCENPs (inner centromere proteins): separate domains are required for association with microtubules during interphase and with the central spindle during anaphase." Journal of Cell Biology 123, no. 2 (October 15, 1993): 373–85. http://dx.doi.org/10.1083/jcb.123.2.373.
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It has recently been proposed that mitotic chromosomes transport certain cytoskeletal proteins to the metaphase plate so that these proteins are able to subsequently participate in the assembly of the anaphase spindle and the cleavage furrow. To understand how such proteins accomplish their dual chromosomal: cytoskeletal role, we have begun a molecular and functional analysis of the inner centromere proteins (INCENPs), founder members of the class of "chromosome passenger proteins". cDNA clones encoding the open reading frames of the two chicken INCENPs were recovered. The predicted proteins, class I INCENP (96,357 D) and class II INCENP (100,931 D) are novel, and differ from each other by the inclusion of a 38-codon insert within the class II coding region. Transient expression of the chicken INCENPs in mammalian cells confirms that the signals and structures required for the transfer of these proteins from chromosomes to cytoskeleton are evolutionarily conserved. Furthermore, these studies reveal that INCENP association with the cytoskeleton is complex. The amino-terminal 42-amino acid residues are required for transfer of the INCENPs from the chromosomes to the mitotic spindle at anaphase, but not for binding of INCENPs to cytoplasmic microtubules. In contrast, an internal 200 amino acid coiled-coil domain was required for association with microtubules, but dispensable for spindle association. These experiments suggest that proteins required for assembly of specialized cytoskeletal structures during mitosis from anaphase onwards might be sequestered in the nucleus throughout interphase to keep them from disrupting the interphase cytoskeleton, and to ensure their correct positioning during mitosis.
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Stolz, D. B., G. Bannish, and B. S. Jacobson. "The role of the cytoskeleton and intercellular junctions in the transcellular membrane protein polarity of bovine aortic endothelial cells in vitro." Journal of Cell Science 103, no. 1 (September 1, 1992): 53–68. http://dx.doi.org/10.1242/jcs.103.1.53.
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This project examines the transcellular membrane protein polarity of bovine aortic endothelial cell (BAEC) monolayers in vitro with respect to the roles that intercellular junctions (as defined by comparing confluent and subconfluent monolayers) and the submembranous cytoskeleton play in controlling this phenomenon. Plasma membrane (PM) proteins obtained from apical (AP) and basolateral (BL) PM domains of confluent BAEC monolayers were isolated using the cationic colloidal silica technique and resolved by two-dimensional gel electrophoresis (2-D PAGE). To facilitate the identification of domain-specific PM proteins, an isoelectric point/molecular weight database of the proteins from AP and BL PM domains was constructed. Domain-specific PM proteins were assessed for their interaction with the cytoskeleton by determining whether they co-isolated with a Triton X-100 detergent-resistant cytoskeletal/extracellular matrix fraction. The maintenance of polarized PM protein segregation by intercellular junctional complexes was determined by comparing AP and BL protein patterns of confluent monolayers with patterns generated by subconfluent monolayers, which lack such junctional structures. Proteins isolated from AP and BL PM domains from both confluent states were immunoblotted with antibodies to angiotensin-converting enzyme (ACE) and collagen receptors (CR). ACE was restricted exclusively to the AP PM domain in the subconfluent condition, even though no apparent cytoskeletal interaction was observed. CRs, found to interact with the cytoskeleton in either confluence state, were predominantly segregated to the BL PM domain regardless of the presence or absence of cell-cell contact. Membrane proteins found by 2-D PAGE to be asymmetrically distributed in the absence of intercellular junctions were assessed for cytoskeletal interaction by their inability to be extracted by Triton X-100 from monolayers in the subconfluent state. Computer cross-referencing of 2-D PAGE peak lists and immunodetection generated from the above fractionation protocols identifies a set of four proteins associated with the cytoskeleton that remain segregated in the proper domain, and five proteins associated with the cytoskeleton that become equally distributed between AP and BL PM domains in the absence of intercellular junctions. Additionally, six proteins not associated with the cytoskeleton remain asymmetrically distributed to the AP domain in the subconfluent state. The data suggest that BAEC monolayers have unknown mechanisms, apart from intercellular junctions expressed at confluency or cytoskeletal binding, for maintaining transcellular PM protein polarity.
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Riederer, B. M., R. Porchet, R. A. Marugg, and L. I. Binder. "Solubility of cytoskeletal proteins in immunohistochemistry and the influence of fixation." Journal of Histochemistry & Cytochemistry 41, no. 4 (April 1993): 609–16. http://dx.doi.org/10.1177/41.4.8450200.
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For accurate and quantitative immunohistochemical localization of antigens it is crucial to know the solubility of tissue proteins and their degree of loss during processing. In this study we focused on the solubility of several cytoskeletal proteins in cat brain tissue at various ages and their loss during immunohistochemical procedures. We further examined whether fixation affected either solubility or immunocytochemical detectability of several cytoskeletal proteins. An assay was designed to measure the solubility of cytoskeletal proteins in cryostat sections. Quantity and quality of proteins lost or remaining in tissue were measured and analyzed by electrophoresis and immunoblots. Most microtubule proteins were found to be soluble in unfixed and alcohol fixed tissues. Furthermore, the microtubule proteins remaining in the tissue had a changed cellular distribution. In contrast, brain spectrin and all three neurofilament subunits were insoluble and remained in the tissue, allowing their immunocytochemical localization in alcohol-fixed tissue. Synapsin I, a protein associated with the spectrin cytoskeleton, was soluble, and aldehyde fixation is advised for its immunohistochemical localization. With aldehyde fixation, the immunoreactivity of some antibodies against neurofilament proteins was reduced in axons unveiling novel immunogenic sites in nuclei that may represent artifacts of fixation. In conclusion, protein solubility and the effects of fixation are influential factors in cytoskeletal immunohistochemistry, and should be considered before assessments for a quantitative distribution are made.
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Kost, Benedikt, Yi-Qun Bao, and Nam-Hai Chua. "Cytoskeleton and plant organogenesis." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 357, no. 1422 (June 29, 2002): 777–89. http://dx.doi.org/10.1098/rstb.2002.1090.
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The functions of microtubules and actin filaments during various processes that are essential for the growth, reproduction and survival of single plant cells have been well characterized. A large number of plant structural cytoskeletal or cytoskeleton–associated proteins, as well as genes encoding such proteins, have been identified. Although many of these genes and proteins have been partially characterized with respect to their functions, a coherent picture of how they interact to execute cytoskeletal functions in plant cells has yet to emerge. Cytoskeleton–controlled cellular processes are expected to play crucial roles during plant cell differentiation and organogenesis, but what exactly these roles are has only been investigated in a limited number of studies in the whole plant context. The intent of this review is to discuss the results of these studies in the light of what is known about the cellular functions of the plant cytoskeleton, and about the proteins and genes that are required for them. Directions are outlined for future work to advance our understanding of how the cytoskeleton contributes to plant organogenesis and development.
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Tashiro, Tomoko. "Axonal transport of cytoskeletal proteins." SEIBUTSU BUTSURI KAGAKU 30, no. 1 (1986): 37–44. http://dx.doi.org/10.2198/sbk.30.37.
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&NA;. "SKELETAL MUSCLE CYTOSKELETAL PROTEINS 319." Medicine & Science in Sports & Exercise 28, Supplement (May 1996): 54. http://dx.doi.org/10.1097/00005768-199605001-00319.
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Biancone, L., P. Vavassori, I. Monteleone, G. Del Vecchia Blanco, F. Pallone, A. Colantoni, L. Spagnoli, F. Tonelli, G. Palmieri, and A. Lombardi. "Cytoskeletal proteins and resident flora." Digestive and Liver Disease 34 (September 2002): S34—S36. http://dx.doi.org/10.1016/s1590-8658(02)80161-x.
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Lippincott-Schwartz, Jennifer. "Cytoskeletal proteins and Golgi dynamics." Current Opinion in Cell Biology 10, no. 1 (February 1998): 52–59. http://dx.doi.org/10.1016/s0955-0674(98)80086-0.
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Wasserman, Steven. "FH proteins as cytoskeletal organizers." Trends in Cell Biology 8, no. 3 (March 1998): 111–15. http://dx.doi.org/10.1016/s0962-8924(97)01217-8.
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Horenberg, Allison L., Alisa M. Houghton, Saurav Pandey, Vikram Seshadri, and William H. Guilford. "S‐nitrosylation of cytoskeletal proteins." Cytoskeleton 76, no. 3 (March 2019): 243–53. http://dx.doi.org/10.1002/cm.21520.
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Gillespie, C. S., R. Wilson, A. Davidson, and P. J. Brophy. "Characterization of a cytoskeletal matrix associated with myelin from rat brain." Biochemical Journal 260, no. 3 (June 15, 1989): 689–96. http://dx.doi.org/10.1042/bj2600689.
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Extraction of rat brain myelin in a buffer containing Triton X-100 yielded a soluble fraction and an insoluble residue that was enriched in cytoskeletal elements. Immunoblot analysis of the detergent-soluble fraction and the insoluble cytoskeletal residue showed that all of the tubulin and more than half of the actin were found within the cytoskeletal fraction. The distribution of myelin-specific proteins was also examined, and revealed that 2′,3′-cyclic nucleotide 3′-phosphohydrolase (CNPase) I and most of the myelin basic proteins (MBPs) were equally distributed between both fractions. By contrast, the large MBP (21.5 kDa) and CNPase II (50 kDa) were observed to partition almost entirely with the cytoskeletal fraction. Proteolipid protein was found predominantly in the detergent-soluble fraction, as was DM-20 protein. Analysis of the cytoskeletal fraction by sucrose-density-gradient centrifugation demonstrated that a distinct subset of lipids was tightly bound to the cytoskeletal protein residue. The cytoskeleton-associated lipid was considerably enriched in cerebroside and sphingomyelin by comparison with total myelin lipids. These results indicate that a cytoskeletal matrix is associated with multilamellar myelin, and suggest that this structure may play a fundamental role in myelinogenesis.
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Ramos-León, Félix, and Kumaran S. Ramamurthi. "Cytoskeletal proteins: lessons learned from bacteria." Physical Biology 19, no. 2 (February 17, 2022): 021005. http://dx.doi.org/10.1088/1478-3975/ac4ef0.
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Abstract Cytoskeletal proteins are classified as a group that is defined functionally, whose members are capable of polymerizing into higher order structures, either dynamically or statically, to perform structural roles during a variety of cellular processes. In eukaryotes, the most well-studied cytoskeletal proteins are actin, tubulin, and intermediate filaments, and are essential for cell shape and movement, chromosome segregation, and intracellular cargo transport. Prokaryotes often harbor homologs of these proteins, but in bacterial cells, these homologs are usually not employed in roles that can be strictly defined as ‘cytoskeletal’. However, several bacteria encode other proteins capable of polymerizing which, although they do not appear to have a eukaryotic counterpart, nonetheless appear to perform a more traditional ‘cytoskeletal’ function. In this review, we discuss recent reports that cover the structures and functions of prokaryotic proteins that are broadly termed as cytoskeletal, either by sequence homology or by function, to highlight how the enzymatic properties of traditionally studied cytoskeletal proteins may be used for other types of cellular functions; and to demonstrate how truly ‘cytoskeletal’ functions may be performed by uniquely bacterial proteins that do not display homology to eukaryotic proteins.
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Wickstead, Bill, and Keith Gull. "The evolution of the cytoskeleton." Journal of Cell Biology 194, no. 4 (August 22, 2011): 513–25. http://dx.doi.org/10.1083/jcb.201102065.
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The cytoskeleton is a system of intracellular filaments crucial for cell shape, division, and function in all three domains of life. The simple cytoskeletons of prokaryotes show surprising plasticity in composition, with none of the core filament-forming proteins conserved in all lineages. In contrast, eukaryotic cytoskeletal function has been hugely elaborated by the addition of accessory proteins and extensive gene duplication and specialization. Much of this complexity evolved before the last common ancestor of eukaryotes. The distribution of cytoskeletal filaments puts constraints on the likely prokaryotic line that made this leap of eukaryogenesis.
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Truman, P., and H. C. Ford. "Proteins of human placental microvilli: I. Cytoskeletal proteins." Placenta 7, no. 2 (March 1986): 95–110. http://dx.doi.org/10.1016/s0143-4004(86)80001-7.
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Bezanilla, Magdalena, Amy S. Gladfelter, David R. Kovar, and Wei-Lih Lee. "Cytoskeletal dynamics: A view from the membrane." Journal of Cell Biology 209, no. 3 (May 11, 2015): 329–37. http://dx.doi.org/10.1083/jcb.201502062.
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Many aspects of cytoskeletal assembly and dynamics can be recapitulated in vitro; yet, how the cytoskeleton integrates signals in vivo across cellular membranes is far less understood. Recent work has demonstrated that the membrane alone, or through membrane-associated proteins, can effect dynamic changes to the cytoskeleton, thereby impacting cell physiology. Having identified mechanistic links between membranes and the actin, microtubule, and septin cytoskeletons, these studies highlight the membrane’s central role in coordinating these cytoskeletal systems to carry out essential processes, such as endocytosis, spindle positioning, and cellular compartmentalization.
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Knecht, David A. "The effect of cytoskeletal protein mutations on cell motility and morphogenesis." Proceedings, annual meeting, Electron Microscopy Society of America 50, no. 1 (August 1992): 594–95. http://dx.doi.org/10.1017/s0424820100123374.
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The cortical cytoskeleton of eukaryotic cells is composed of actin filaments and a variety of associated proteins. The polymerization, depolymerization, cross-linking and bundling of these filaments, are presumed to be intimately involved in such processes as cell motility, cell adhesion and cell shape. In developing systems, all of these processes are involved in the morphogenetic mechanisms that shape tissues, organs and organisms.We are investigating the complex interactions among cytoskeletal proteins using the simple eukaryotic amoebae, Dictyostelium discoideum. Our approach is to determine the function of the components of the cytoskeleton by creating mutants lacking particular proteins, or containing specific alterations in these proteins. Mutants lacking myosin heavy chain have been created using antisense RNA and homologous gene targetting. These cells have alterations in their shape and movement, and are incapable of accomplishing normal morphogenesis. Another cytoskeletal protein is ABP-120, which is capable of cross-linking actin filaments into orthogonal arrays, leading to the formation of an actin gel in vitro. ABP-120 is found in newly formed pseudopods extended during the chemotactic respose to extracellular cAMP. Mutants lacking this protein have been created by disruption of the chromosomal gene with a transformation vector. These cells are not as dramatically affected as the myosin mutants, but have clear alterations in their motility and in the pathway of responses in the cytoskeleton that correlate with the expected function of this protein. Mutations in several other cytoskeletal genes are currently being constructed.
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Fanning, Alan S., Christina M. Van Itallie, and James M. Anderson. "Zonula occludens-1 and -2 regulate apical cell structure and the zonula adherens cytoskeleton in polarized epithelia." Molecular Biology of the Cell 23, no. 4 (February 15, 2012): 577–90. http://dx.doi.org/10.1091/mbc.e11-09-0791.
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The structure and function of both adherens (AJ) and tight (TJ) junctions are dependent on the cortical actin cytoskeleton. The zonula occludens (ZO)-1 and -2 proteins have context-dependent interactions with both junction types and bind directly to F-actin and other cytoskeletal proteins, suggesting ZO-1 and -2 might regulate cytoskeletal activity at cell junctions. To address this hypothesis, we generated stable Madin-Darby canine kidney cell lines depleted of both ZO-1 and -2. Both paracellular permeability and the localization of TJ proteins are disrupted in ZO-1/-2–depleted cells. In addition, immunocytochemistry and electron microscopy revealed a significant expansion of the perijunctional actomyosin ring associated with the AJ. These structural changes are accompanied by a recruitment of 1-phosphomyosin light chain and Rho kinase 1, contraction of the actomyosin ring, and expansion of the apical domain. Despite these changes in the apical cytoskeleton, there are no detectable changes in cell polarity, localization of AJ proteins, or the organization of the basal and lateral actin cytoskeleton. We conclude that ZO proteins are required not only for TJ assembly but also for regulating the organization and functional activity of the apical cytoskeleton, particularly the perijunctional actomyosin ring, and we speculate that these activities are relevant both to cellular organization and epithelial morphogenesis.
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Stødkilde, Lene, Johan Palmfeldt, Line Nilsson, Inge Carlsen, Yan Wang, Rikke Nørregaard, and Jørgen Frøkiær. "Proteomic identification of early changes in the renal cytoskeleton in obstructive uropathy." American Journal of Physiology-Renal Physiology 306, no. 12 (June 15, 2014): F1429—F1441. http://dx.doi.org/10.1152/ajprenal.00244.2013.
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Bilateral ureteral obstruction (BUO) is associated with renal damage and impaired ability to concentrate urine and is known to induce alterations in an array of kidney proteins. The aim of this study was to identify acute proteomic alterations induced by BUO. Rats were subjected to BUO for 2, 6, or 24 h. Mass spectrometry-based proteomics was performed on the renal inner medulla, and protein changes in the obstructed group were identified. Significant changes were successfully identified for 109 proteins belonging to different biological classes. Interestingly, proteins belonging to the cytoskeleton and proteins related to cytoskeletal regulation were found to be biologically enriched in BUO using online-accessible tools. Western blots confirmed the selected results, demonstrating acute downregulation of proteins belonging to all three cytoskeletal components. The microfilament protein β-actin and the intermediate filament proteins pankeratin and vimentin were all downregulated. β-Tubulin, an important microtubular protein, was found to be significantly downregulated after 24 h. Also, there was significant upregulation of cofilin, an actin-binding protein known to be upregulated in other nephropathy models. Furthermore, both upregulation and downregulation of cytoskeletal motor and regulatory proteins were observed. These findings were confirmed by immunohistochemistry, which clearly showed alterations in labeling in the inner medulla. Interestingly, we were able to confirm selected results in mpkCCD cells exposed to mechanical stretch. Our findings add to the knowledge of BUO-induced acute changes in the renal cytoskeleton and suggest that these molecular changes are partly mediated by increased stretch of the cells during obstruction.
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Toyoda, Hideki, Keiji Nakai, Serdar B. Omay, Hiroshi Shima, Minako Nagao, Hiroshi Shiku, and Masakatsu Nishikawa. "Differential Association of Protein Ser/Thr Phosphatase Types 1 and 2A with the Cytoskeleton upon Platelet Activation." Thrombosis and Haemostasis 76, no. 06 (1996): 1053–62. http://dx.doi.org/10.1055/s-0038-1650706.
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SummaryThe association of protein Ser/Thr phosphatase type 1(PP1) and type 2A (PP2A) with the cytoskeleton (Triton X-100 insoluble residue) during human platelet activation was investigated. In unstimulated platelets, 40% of total PPl-like activity was present in the Triton-insoluble cytoskeleton, while only 10% of the total PP2A-like activity was present in this fraction. Stimulation with 1 U/ml thrombin produced a 1.8-fold increase in PPl-like activity and a 7-fold increase in PP2A-like activity, respectively, in the cytoskeletal fraction, under aggregating conditions. Immunoblot analysis revealed that thrombin treatment increased association of PP1 catalytic subunit isozymes (PPlα, PPlβ, PP1γ) and PP2A catalytic subunit with the cytoskeleton, with concomitant decrease of these enzymes in Triton-soluble fractions. The amounts of cytoskeleton-associated PP1 and PP2A depended on the dose of thrombin which could activate platelets. Agonist-induced redistribution of PP1 and PP2A into the cytoskeleton was inhibited by OP-41483 (a prostaglandin I2 analog). Interaction of PP2A with cytoskeletal proteins strongly correlates with aggregation, whereas the association of PP1 with cytoskeleton can be detected upon platelet activation, even in the absence of aggregation. Co-extraction of protein kinase C and myosin light chain kinase with the cytoskeleton eventually translocated to the cytoskeleton, but only during aggregation. These results suggest that differential translocation of PP1 and PP2A to the cytoskeleton is involved in platelet activation, and their association with cytoskeletal proteins may regulate phosphorylation levels together with protein kinases in platelets.
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Carpenter, David A., Sohaib A. Khan, and Wallace Ip. "Discrimination of the assembly states of cytoskeletal proteins in cultured cells using confocal microscopy." Proceedings, annual meeting, Electron Microscopy Society of America 51 (August 1, 1993): 270–71. http://dx.doi.org/10.1017/s0424820100147193.
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The cytoskeleton is a three-dimensional network of cytoplasmic filaments that mediates many processes involving motility, and the specification and maintenance of cell form. In recent years, it has become evident that all three major components of the cytoskeleton- microfilaments, microtubules, and intermediate filaments (IF)-are dynamic structures that undergo reversible assembly-disassembly as required by the physiologic needs of the cell. While the assembled form of the cytoskeleton-the filamentous network-is readily visible by conventional immunofluorescence microscopy, it is often difficult to visualize the nonfilamentous form of a cytoskeletal protein because the subunits or oligomeric assemblies are small and because the images tend to be diffused due to interference from fluorescently labelled subunits above and below the plane of focus. Confocal microscopy offers a convenient solution to this problem at the light microscope level, because optical sections of fluorescently immunolabelled cytoskeletal networks do not suffer from such out-of-focus interference.
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Harris, Andrew R., Pamela Jreij, and Daniel A. Fletcher. "Mechanotransduction by the Actin Cytoskeleton: Converting Mechanical Stimuli into Biochemical Signals." Annual Review of Biophysics 47, no. 1 (May 20, 2018): 617–31. http://dx.doi.org/10.1146/annurev-biophys-070816-033547.
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Force transmission through the actin cytoskeleton plays a central role in cell movements, shape change, and internal organization. Dynamic reorganization of actin filaments by an array of specialized binding proteins creates biochemically and architecturally distinct structures, many of which are finely tuned to exert or resist mechanical loads. The molecular complexity of the actin cytoskeleton continues to be revealed by detailed biochemical assays, and the architectural diversity and dynamics of actin structures are being uncovered by advances in super-resolution fluorescence microscopy and electron microscopy. However, our understanding of how mechanical forces feed back on cytoskeletal architecture and actin-binding protein organization is comparatively limited. In this review, we discuss recent work investigating how mechanical forces applied to cytoskeletal proteins are transduced into biochemical signals. We explore multiple mechanisms for mechanical signal transduction, including the mechanosensitive behavior of actin-binding proteins, the effect of mechanical force on actin filament dynamics, and the influence of mechanical forces on the structure of single actin filaments. The emerging picture is one in which the actin cytoskeleton is defined not only by the set of proteins that constitute a network but also by the constant interplay of mechanical forces and biochemistry.
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Kuznetsov, Andrey V., Sabzali Javadov, Michael Grimm, Raimund Margreiter, Michael J. Ausserlechner, and Judith Hagenbuchner. "Crosstalk between Mitochondria and Cytoskeleton in Cardiac Cells." Cells 9, no. 1 (January 16, 2020): 222. http://dx.doi.org/10.3390/cells9010222.
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Elucidation of the mitochondrial regulatory mechanisms for the understanding of muscle bioenergetics and the role of mitochondria is a fundamental problem in cellular physiology and pathophysiology. The cytoskeleton (microtubules, intermediate filaments, microfilaments) plays a central role in the maintenance of mitochondrial shape, location, and motility. In addition, numerous interactions between cytoskeletal proteins and mitochondria can actively participate in the regulation of mitochondrial respiration and oxidative phosphorylation. In cardiac and skeletal muscles, mitochondrial positions are tightly fixed, providing their regular arrangement and numerous interactions with other cellular structures such as sarcoplasmic reticulum and cytoskeleton. This can involve association of cytoskeletal proteins with voltage-dependent anion channel (VDAC), thereby, governing the permeability of the outer mitochondrial membrane (OMM) to metabolites, and regulating cell energy metabolism. Cardiomyocytes and myocardial fibers demonstrate regular arrangement of tubulin beta-II isoform entirely co-localized with mitochondria, in contrast to other isoforms of tubulin. This observation suggests the participation of tubulin beta-II in the regulation of OMM permeability through interaction with VDAC. The OMM permeability is also regulated by the specific isoform of cytolinker protein plectin. This review summarizes and discusses previous studies on the role of cytoskeletal proteins in the regulation of energy metabolism and mitochondrial function, adenosine triphosphate (ATP) production, and energy transfer.
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Kriho, V., G. D. Pappas, N. Lieska, C. M. Wu, and H. Y. Yang. "Rat Reactive Astrocyte Marker (IFAP-70/280KD) is Expressed in Rat Spinal Cord Motor Neurons Following Transection of Sciatic Nerve." Microscopy and Microanalysis 3, S2 (August 1997): 159–60. http://dx.doi.org/10.1017/s1431927600007686.
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Following injury to peripheral nerves, processes involved in regeneration must be activated, restoring the original architecture and synaptic connections of the neuron. This is essential for the efficient operation of the sophisticated communications network of the nervous system. In order to accomplish these tasks, complex changes occur in gene expression. Regenerating neurons shift into a growth mode wherein large amounts of cytoskeletal proteins and other growth-associated proteins are produced. These materials, which are synthesized and produced in the neuronal cell body, are then transferred to the axon via axonal transport systems. Among the cytoskeletal and associated proteins upregulated following injury to the CNS are actin, tubulin and the intermediate filament-associated protein, IFAP-70/280kD. The latter is the subject of this investigation.Intermediate filaments (IF) are a major constituent of the cytoskeleton of most eukaryotic cells. The IF cytoskeleton is a highly dynamic structure that reorganizes continuously as the cell divides and changes shape in response to its environment.
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Bloch, Wilhelm, Yun Fan, Ji Han, Sheng Xue, Torsten Schöneberg, Guanju Ji, Zhong J. Lu, et al. "Disruption of cytoskeletal integrity impairs Gi-mediated signaling due to displacement of Gi proteins." Journal of Cell Biology 154, no. 4 (August 20, 2001): 753–62. http://dx.doi.org/10.1083/jcb.200103011.
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β1 integrins play a crucial role as cytoskeletal anchorage proteins. In this study, the coupling of the cytoskeleton and intracellular signaling pathways was investigated in β1 integrin deficient (−/−) embryonic stem cells. Muscarinic inhibition of the L-type Ca2+ current (ICa) and activation of the acetylcholine-activated K+ current (IK,ACh) was found to be absent in β1 integrin−/− cardiomyocytes. Conversely, β adrenoceptor-mediated modulation of ICa was unaffected by the absence of β1 integrins. This defect in muscarinic signaling was due to defective G protein coupling. This was supported by deconvolution microscopy, which demonstrated that Gi exhibited an atypical subcellular distribution in the β1 integrin−/− cardiomyocytes. A critical role of the cytoskeleton was further demonstrated using cytochalasin D, which displaced Gi and impaired muscarinic signaling. We conclude that cytoskeletal integrity is required for correct localization and function of Gi-associated signaling microdomains.
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Zhang, Hong, Yuan Liu, Cencen Li, and Weiya Zhang. "ITGβ6 Facilitates Skeletal Muscle Development by Maintaining the Properties and Cytoskeleton Stability of Satellite Cells." Life 12, no. 7 (June 21, 2022): 926. http://dx.doi.org/10.3390/life12070926.
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Integrin proteins are important receptors connecting the intracellular skeleton of satellite cells and the extracellular matrix (ECM), playing an important role in the process of skeletal muscle development. In this research, the function of ITGβ6 in regulating the differentiation of satellite cells was studied. Transcriptome and proteome analysis indicated that Itgβ6 is a key node connecting ECM-related proteins to the cytoskeleton, and it is necessary for the integrity of the membrane structure and stability of the cytoskeletal system, which are essential for satellite cell adhesion. Functional analysis revealed that the ITGβ6 protein could affect the myogenic differentiation potential of satellite cells by regulating the expression of PAX7 protein, thus regulating the formation of myotubes. Moreover, ITGβ6 is involved in muscle development by regulating cell-adhesion-related proteins, such as β-laminin, and cytoskeletal proteins such as PXN, DMD, and VCL. In conclusion, the effect of ITGβ6 on satellite cell differentiation mainly occurs before the initiation of differentiation, and it regulates terminal differentiation by affecting satellite cell characteristics, cell adhesion, and the stability of the cytoskeleton system.
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Aunis, D., and M. F. Bader. "The cytoskeleton as a barrier to exocytosis in secretory cells." Journal of Experimental Biology 139, no. 1 (September 1, 1988): 253–66. http://dx.doi.org/10.1242/jeb.139.1.253.
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Chromaffin cells of the adrenal medulla synthesize, store and secrete catecholamines. These cells contain numerous electron-dense secretory granules which discharge their contents into the extracellular space by exocytosis. The subplasmalemmal area of the chromaffin cell is characterized by the presence of a highly organized cytoskeletal network. F-Actin seems to be exclusively localized in this area and together with specific actin-binding proteins forms a dense viscoelastic gel; fodrin, vinculin and caldesmon, three actin cross-linking proteins, and gelsolin, an actin-severing protein, are found in this subplasmalemmal region. Since fodrin-, caldesmon- and alpha-actinin-binding sites exist on secretory granule membranes, actin filaments can also link secretory granules. Chromaffin granules can be entrapped in this subplasmalemmal lattice and thus the cytoskeleton acts as a barrier preventing exocytosis. When cells are stimulated, molecular rearrangements of the subplasmalemmal cytoskeleton take place: F-actin depolymerizes and fodrin reorganizes into patches. In addition, introduction of monospecific antifodrin immunoglobulins into digitonin-permeabilized cells blocks exocytosis, demonstrating the crucial role of this actin-binding protein. In bacterial toxin-permeabilized chromaffin cells, experiments using actin-perturbing agents such as cytochalasin D and DNAase I suggest that exocytosis is in part controlled by the cytoskeleton. The intracellular signal governing the cytoskeletal reorganization (associated with exocytosis) is calcium. Calcium inhibits some and activates other actin-binding proteins and consequently causes dissolution of the subplasmalemmal cytoskeleton. This dissolution of cytoskeletal filaments should result in granule detachment and permit granules free access to exocytotic sites on the plasma membrane.
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Costa, Manoel Luís. "Cytoskeleton and Adhesion in Myogenesis." ISRN Developmental Biology 2014 (April 15, 2014): 1–15. http://dx.doi.org/10.1155/2014/713631.
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The function of muscle is to contract, which means to exert force on a substrate. The adaptations required for skeletal muscle differentiation, from a prototypic cell, involve specialization of housekeeping cytoskeletal contracting and supporting systems into crystalline arrays of proteins. Here I discuss the changes that all three cytoskeletal systems (microfilaments, intermediate filaments, and microtubules) undergo through myogenesis. I also discuss their interaction, through the membrane, to extracellular matrix and to other cells, where force will be exerted during contraction. The three cytoskeletal systems are necessary for the muscle cell and must exert complementary roles in the cell. Muscle is a responsive system, where structure and function are integrated: the structural adaptations it undergoes depend on force production. In this way, the muscle cytoskeleton is a portrait of its physiology. I review the cytoskeletal proteins and structures involved in muscle function and focus particularly on their role in myogenesis, the process by which this incredible muscle machine is made. Although the focus is on skeletal muscle, some of the discussion is applicable to cardiac and smooth muscle.
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Guay-Woodford, L. M., O. Platt, and H. W. Harris. "Toad urinary bladder epithelial cells contain an analogue of cytoskeletal protein 4.1." American Journal of Physiology-Cell Physiology 260, no. 6 (June 1, 1991): C1308—C1314. http://dx.doi.org/10.1152/ajpcell.1991.260.6.c1308.
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Epithelial cell polarity and vectorial transport require cytoskeletal proteins that maintain local cell membrane structure and mediate cytoplasmic vesicle movement. The cytoskeleton of leaky epithelia, such as the intestinal mucosa and renal proximal tubule cells, has been extensively studied. However, cytoskeletal studies in tight epithelia such as the mammalian collecting duct and toad urinary bladder generally have been confined to ultrastructural investigation. Recent research in nonepithelial cell types has identified an interesting family of cytoskeletal proteins. Present in multiple cell types, these protein 4.1 analogues share a number of similar functional characteristics, yet are structurally diverse. They are multiply phosphorylated by several different kinases, and phosphorylation regulates their associations with other cytoskeletal constituents, integral membrane components, and cytoplasmic vesicles. Using a combination of immunochemical and immunofluorescent techniques, we have demonstrated that toad bladder epithelial cells contain a 65-kDa analogue of human erythrocyte protein 4.1. Toad bladder epithelial cell protein 4.1 is structurally similar to its erythrocyte counterpart and is phosphorylated. This protein 4.1 species is present throughout the toad bladder granular cell cytoplasm, suggesting that it participates in multiple granular cell functions.
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Anniko, M., and W. Arnold. "Cytoskeletal Proteins in Human Hair Cells." Acta Oto-Laryngologica 115, sup519 (January 1995): 8–12. http://dx.doi.org/10.3109/00016489509121862.
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MARAZZI, G., S. GREGO, E. CLEMENTI, and G. FUMAGALLI. "Cytoskeletal proteins in the neuromuscular junction." Cell Biology International Reports 10, no. 3 (March 1986): 210. http://dx.doi.org/10.1016/s0309-1651(86)80064-9.
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