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Academic literature on the topic 'Dynein'

Author: Grafiati

Published: 4 June 2021

Last updated: 6 September 2023

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Journal articles on the topic "Dynein"

1

Jha, Rupam, and Thomas Surrey. "Regulation of processive motion and microtubule localization of cytoplasmic dynein." Biochemical Society Transactions 43, no. 1 (January 26, 2015): 48–57. http://dx.doi.org/10.1042/bst20140252.

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The cytoplasmic dynein complex is the major minus-end-directed microtubule motor. Although its directionality is evolutionary well conserved, differences exist among cytoplasmic dyneins from different species in their stepping behaviour, maximum velocity and force production. Recent experiments also suggest differences in processivity regulation. In the present article, we give an overview of dynein's motile properties, with a special emphasis on processivity and its regulation. Furthermore, we summarize recent findings of different pathways for microtubule plus-end loading of dynein. The present review highlights how distinct functions in different cell types or organisms appear to require different mechanochemical dynein properties and localization pathways.

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Ishibashi, Kenta, Hitoshi Sakakibara, and Kazuhiro Oiwa. "Force-Generating Mechanism of Axonemal Dynein in Solo and Ensemble." International Journal of Molecular Sciences 21, no. 8 (April 18, 2020): 2843. http://dx.doi.org/10.3390/ijms21082843.

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In eukaryotic cilia and flagella, various types of axonemal dyneins orchestrate their distinct functions to generate oscillatory bending of axonemes. The force-generating mechanism of dyneins has recently been well elucidated, mainly in cytoplasmic dyneins, thanks to progress in single-molecule measurements, X-ray crystallography, and advanced electron microscopy. These techniques have shed light on several important questions concerning what conformational changes accompany ATP hydrolysis and whether multiple motor domains are coordinated in the movements of dynein. However, due to the lack of a proper expression system for axonemal dyneins, no atomic coordinates of the entire motor domain of axonemal dynein have been reported. Therefore, a substantial amount of knowledge on the molecular architecture of axonemal dynein has been derived from electron microscopic observations on dynein arms in axonemes or on isolated axonemal dynein molecules. This review describes our current knowledge and perspectives of the force-generating mechanism of axonemal dyneins in solo and in ensemble.

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3

Yoshida, T., H. Takanari, and K. Izutsu. "Distribution of cytoplasmic and axonemal dyneins in rat tissues." Journal of Cell Science 101, no. 3 (March 1, 1992): 579–87. http://dx.doi.org/10.1242/jcs.101.3.579.

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Microtubule-associated protein 1C (MAP 1C) is now defined as brain cytoplasmic dynein. Recent studies have suggested that cytoplasmic dynein is a motor protein responsible for the intracellular microtubule-based motility in neuronal and non-neuronal cells. We have prepared an antibody against bovine brain MAP 1C and have examined the localizations of cytoplasmic dynein in rat tissues. Immunoblots of extracts from the tissues showed that the dynein was present in brain, testis, liver, kidney and lung. Immunohistochemical experiments have demonstrated that dynein is localized in Purkinje cells of cerebellum and axons of central and peripheral nervous systems. In non-neuronal tissues, the antibody staining was intense in many types of cells, such as hepatocytes, epithelia of renal convoluted tubules, secretory cells of adrenal medulla and spermatids. Glomeruli of kidney, bronchial epithelia and type II pneumocytes of lung, pancreatic islets and acini, adrenal cortex and Sertoli cells were moderately positive upon exposure to the cytoplasmic dynein antibody. On the other hand, the localization of axonemal dynein was examined using antibodies against flagellar dynein of sea urchin spermatozoa. Anti-axonemal dynein labeled cilia and flagella in rat tissues whereas anti-MAP 1C did not stain axonemes. We also tested for immunological cross-reactivity between cytoplasmic and axonemal dyneins to probe for molecular similarities. Anti-axonemal dynein reacted with MAP 1C weakly. These results have confirmed that cytoplasmic dyneins are distributed widely among rat organs, not only in neuronal but also in non-neuronal tissues. There is no similarity in the localization of cytoplasmic and axonemal dyneins but there is some similarity in molecular antigenicity.

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Vale, R. D., and Y. Y. Toyoshima. "Microtubule translocation properties of intact and proteolytically digested dyneins from Tetrahymena cilia." Journal of Cell Biology 108, no. 6 (June 1, 1989): 2327–34. http://dx.doi.org/10.1083/jcb.108.6.2327.

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Tetrahymena cilia contain a three-headed 22S (outer arm) dynein and a single-headed 14S dynein. In this study, we have employed an in vitro assay of microtubule translocation along dynein-coated glass surfaces to characterize the motile properties of 14S dynein, 22S dynein, and proteolytic fragments of 22S dynein. Microtubule translocation produced by intact 22S dynein and 14S dynein differ in a number of respects including (a) the maximal velocities of movement; (b) the ability of 22S dynein but not 14S dynein to utilize ATP gamma S to induce movement; (c) the optimal pH and ionic conditions for movement; and (d) the effects of Triton X-100 on the velocity of movement. These results indicate that 22S and 14S dyneins have distinct microtubule translocating properties and suggest that these dyneins may have specialized roles in ciliary beating. We have also explored the function of the multiple ATPase heads of 22S dynein by preparing one- and two-headed proteolytic fragments of this three-headed molecule and examining their motile activity in vitro. Unlike the single-headed 14S dynein, the single-headed fragment of 22S dynein did not induce movement, even though it was capable of binding to microtubules. The two-headed fragment, on the other hand, translocated microtubules at velocities similar to those measured for intact 22S dynein (10 microns/sec). This finding indicates that the intact three-headed structure of 22S dynein is not essential for generating microtubule movement, which raises the possibility that multiple heads may serve some regulatory function or may be required for maximal force production in the beating cilium.

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Yamamoto, Ryosuke, Kangkang Song, Haru-aki Yanagisawa, Laura Fox, Toshiki Yagi, Maureen Wirschell, Masafumi Hirono, Ritsu Kamiya, Daniela Nicastro, and Winfield S. Sale. "The MIA complex is a conserved and novel dynein regulator essential for normal ciliary motility." Journal of Cell Biology 201, no. 2 (April 8, 2013): 263–78. http://dx.doi.org/10.1083/jcb.201211048.

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Axonemal dyneins must be precisely regulated and coordinated to produce ordered ciliary/flagellar motility, but how this is achieved is not understood. We analyzed two Chlamydomonas reinhardtii mutants, mia1 and mia2, which display slow swimming and low flagellar beat frequency. We found that the MIA1 and MIA2 genes encode conserved coiled-coil proteins, FAP100 and FAP73, respectively, which form the modifier of inner arms (MIA) complex in flagella. Cryo–electron tomography of mia mutant axonemes revealed that the MIA complex was located immediately distal to the intermediate/light chain complex of I1 dynein and structurally appeared to connect with the nexin–dynein regulatory complex. In axonemes from mutants that lack both the outer dynein arms and the MIA complex, I1 dynein failed to assemble, suggesting physical interactions between these three axonemal complexes and a role for the MIA complex in the stable assembly of I1 dynein. The MIA complex appears to regulate I1 dynein and possibly outer arm dyneins, which are both essential for normal motility.

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Sanghavi, Paulomi, Pankaj Kumar, Ankit Roy, M. S. Madhusudhan, and Roop Mallik. "On and off controls within dynein–dynactin on native cargoes." Proceedings of the National Academy of Sciences 118, no. 23 (June 1, 2021): e2103383118. http://dx.doi.org/10.1073/pnas.2103383118.

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The dynein–dynactin nanomachine transports cargoes along microtubules in cells. Why dynactin interacts separately with the dynein motor and also with microtubules is hotly debated. Here we disrupted these interactions in a targeted manner on phagosomes extracted from cells, followed by optical trapping to interrogate native dynein–dynactin teams on single phagosomes. Perturbing the dynactin–dynein interaction reduced dynein’s on rate to microtubules. In contrast, perturbing the dynactin–microtubule interaction increased dynein’s off rate markedly when dynein was generating force against the optical trap. The dynactin–microtubule link is therefore required for persistence against load, a finding of importance because disease-relevant mutations in dynein–dynactin are known to interfere with “high-load” functions of dynein in cells. Our findings call attention to a less studied property of dynein–dynactin, namely, its detachment against load, in understanding dynein dysfunction.

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Asai, D. J., S. M. Beckwith, K. A. Kandl, H. H. Keating, H. Tjandra, and J. D. Forney. "The dynein genes of Paramecium tetraurelia. Sequences adjacent to the catalytic P-loop identify cytoplasmic and axonemal heavy chain isoforms." Journal of Cell Science 107, no. 4 (April 1, 1994): 839–47. http://dx.doi.org/10.1242/jcs.107.4.839.

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Paramecium tetraurelia is a unicellular organism that utilizes both axonemal and cytoplasmic dyneins. The highly conserved region containing the catalytic P-loop of the dynein heavy chain was amplified by RNA-directed polymerase chain reaction. Eight different P-loop-containing cDNA fragments were cloned. Southern hybridization analysis indicated that each fragment corresponds to a separate dynein gene and that there are at least 12 dynein heavy chain genes expressed in Paramecium. Seven of the eight cloned contain sequence motif A, which is found in axonemal dyneins, and one contains sequence motif B, which is found in the dyneins from cell types that do not have cilia or flagella. Two of the Paramecium dynein genes were further investigated: DHC-6 which contains motif A, and DHC-8 which contains motif B. Additional sequencing of the central portions of these genes showed that DHC-6 most closely matches sea urchin ciliary beta heavy chain and DHC-8 is similar to the cytoplasmic dynein from Dictyostelium. Deciliation of the cells resulted in a substantial increase in the steady state concentration of DHC-6 mRNA but only a small change in DHC-8 mRNA. Antisera were produced against synthetic peptides derived from sequence motifs A and B. Competitive solid-phase binding assays demonstrated that each antiserum was peptide-specific. In western blots, the antiserum to motif A reacted with both ciliary and cytoplasmic dyneins. In contrast, the antiserum to motif B reacted with the cytoplasmic dyneins of Paramecium and bovine brain but did not react with ciliary dynein.(ABSTRACT TRUNCATED AT 250 WORDS)

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Canty, John T., Ruensern Tan, Emre Kusakci, Jonathan Fernandes, and Ahmet Yildiz. "Structure and Mechanics of Dynein Motors." Annual Review of Biophysics 50, no. 1 (May 6, 2021): 549–74. http://dx.doi.org/10.1146/annurev-biophys-111020-101511.

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Dyneins make up a family of AAA+ motors that move toward the minus end of microtubules. Cytoplasmic dynein is responsible for transporting intracellular cargos in interphase cells and mediating spindle assembly and chromosome positioning during cell division. Other dynein isoforms transport cargos in cilia and power ciliary beating. Dyneins were the least studied of the cytoskeletal motors due to challenges in the reconstitution of active dynein complexes in vitro and the scarcity of high-resolution methods for in-depth structural and biophysical characterization of these motors. These challenges have been recently addressed, and there have been major advances in our understanding of the activation, mechanism, and regulation of dyneins. This review synthesizes the results of structural and biophysical studies for each class of dynein motors. We highlight several outstanding questions about the regulation of bidirectional transport along microtubules and the mechanisms that sustain self-coordinated oscillations within motile cilia.

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9

Roberts, Anthony J. "Emerging mechanisms of dynein transport in the cytoplasm versus the cilium." Biochemical Society Transactions 46, no. 4 (July 31, 2018): 967–82. http://dx.doi.org/10.1042/bst20170568.

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Two classes of dynein power long-distance cargo transport in different cellular contexts. Cytoplasmic dynein-1 is responsible for the majority of transport toward microtubule minus ends in the cell interior. Dynein-2, also known as intraflagellar transport dynein, moves cargoes along the axoneme of eukaryotic cilia and flagella. Both dyneins operate as large ATP-driven motor complexes, whose dysfunction is associated with a group of human disorders. But how similar are their mechanisms of action and regulation? To examine this question, this review focuses on recent advances in dynein-1 and -2 research, and probes to what extent the emerging principles of dynein-1 transport could apply to or differ from those of the less well-understood dynein-2 mechanoenzyme.

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Antony, Dinu, Han G. Brunner, and Miriam Schmidts. "Ciliary Dyneins and Dynein Related Ciliopathies." Cells 10, no. 8 (July 25, 2021): 1885. http://dx.doi.org/10.3390/cells10081885.

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Although ubiquitously present, the relevance of cilia for vertebrate development and health has long been underrated. However, the aberration or dysfunction of ciliary structures or components results in a large heterogeneous group of disorders in mammals, termed ciliopathies. The majority of human ciliopathy cases are caused by malfunction of the ciliary dynein motor activity, powering retrograde intraflagellar transport (enabled by the cytoplasmic dynein-2 complex) or axonemal movement (axonemal dynein complexes). Despite a partially shared evolutionary developmental path and shared ciliary localization, the cytoplasmic dynein-2 and axonemal dynein functions are markedly different: while cytoplasmic dynein-2 complex dysfunction results in an ultra-rare syndromal skeleto-renal phenotype with a high lethality, axonemal dynein dysfunction is associated with a motile cilia dysfunction disorder, primary ciliary dyskinesia (PCD) or Kartagener syndrome, causing recurrent airway infection, degenerative lung disease, laterality defects, and infertility. In this review, we provide an overview of ciliary dynein complex compositions, their functions, clinical disease hallmarks of ciliary dynein disorders, presumed underlying pathomechanisms, and novel developments in the field.

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Dissertations / Theses on the topic "Dynein"

1

Malkova, Barbora. "Structural studies of cytoplasmic dynein." Thesis, University of Leeds, 2010. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.540206.

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Liu, Siming. "TESTING THE MULTI-DYNEIN HYPOTHESIS BY MUTATING INNER ARM DYNEIN HEAVY CHAINS IN TETRAHYMENA THERMOPHILA." Miami University / OhioLINK, 2004. http://rave.ohiolink.edu/etdc/view?acc_num=miami1077152822.

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Villemant, Cecile Madeleine. "Investigating dynein light intermediate chains function." Thesis, University of Manchester, 2010. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.518455.

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Kardon, Julia R. "Regulation of the cytoplasmic dynein motor." Diss., Search in ProQuest Dissertations & Theses. UC Only, 2009. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&res_dat=xri:pqdiss&rft_dat=xri:pqdiss:3359552.

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Gleave, Emma Sarah. "Structural and single-molecule studies of the cytoplasmic dynein motor domain." Thesis, University of Cambridge, 2014. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.708182.

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Diamant, Aristides G. "The structure of the cytoplasmic dynein tail." Thesis, University of Cambridge, 2015. https://www.repository.cam.ac.uk/handle/1810/249014.

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Cytoplasmic dynein is a molecular motor that moves cargos along microtubules. Dynein, together with its large co-factor dynactin, is responsible for the vast majority of traffic towards the centre of the cell. The largest subunit of the dynein complex is called the dynein heavy chain (DHC). The DHC includes a C-terminal motor domain, which converts ATP hydrolysis into mechanical force, an N-terminal tail domain, and a flexible linker domain to join the two together. An intermediate chain (DIC) and light intermediate chain (DLIC) bind directly to the DHC tail, while light chains (DLCs) bind to the DIC. This tail complex is important for both cargo binding as well as homodimerisation of the DHC, which is necessary for processive movement. Previous studies suggest that the DLCs play an important role in homodimerisation, but it remains unclear how else the DHCs are held together. Using S. cerevisiae as a model system, I co-expressed all four dynein subunits and purified functional dynein motors. In this background, I found that truncating the DHC to include only the first 1004 residues (out of the total 4092) eliminates the motor domain as well as the flexible linker domain, while preserving binding to the DIC, DLIC and DLC. However, truncating just another 50 residues off of the C-terminus led to a loss of all accessory subunits. I developed a protocol for expressing and purifying large quantities of the 1004 residue construct, thus I provide the first description of a recombinant dynein tail domain. Using negative stain electron microscopy (EM), I also present the first 3D structural information for the tail region of the cytoplasmic dynein motor. I then describe a construct including only the first 557 residues of the DHC, which dimerises despite not being able to bind any of the other subunits. I present a crystal structure of this smaller DHC fragment, which shows that the N-terminal 180 residues of the DHC constitute an intricate dimerisation domain made up of a β-sheet sandwiched between α-helices. Not only is this the first crystal structure of any part of the DHC N-terminus, but it reveals a previously undocumented dimerisation domain within the DHC itself. Furthermore, information garnered from this crystal structure allowed for interpretation of a recent cryo-EM structure of a triple complex containing the dynein tail, dynactin and the cargo adaptor BICD2 (TDB) that was solved by my colleagues in the Carter group. Only by docking the DHC N-terminus crystal structure within the TDB EM density did it become clear that the N-terminus of the DHC is responsible for the majority of the contacts the dynein tail makes with both dynactin and BICD2. Therefore the work that I present here sheds new light on the unexpected importance of the DHC N-terminus and allows two important conclusions to be made. First, the N-terminal 180 residues of the DHC constitute a dimerisation domain of its own. Second, the next ~400 residues of the DHC form a domain that plays a key role in the complex interface between dynein, dynactin and BICD2.

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Roberts, Anthony John. "Structural studies on the mechanism of dynein." Thesis, University of Leeds, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.511146.

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Nyarko, Afua A. "Structure and interactions of subunits of cytoplasmic dynein /." View abstract, 2005. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&res_dat=xri:pqdiss&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&rft_dat=xri:pqdiss:3191709.

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9

Nettesheim, Guilherme, Rafael A. Longoria, Allyson M. Rice, and George T. Shubeita. "Kinesin and dynein respond differently to cytoplasmic drag." Universitätsbibliothek Leipzig, 2015. http://nbn-resolving.de/urn:nbn:de:bsz:15-qucosa-182714.

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Milisav-Ribaric, Irina. "Characterisation of human dynein-related genes from testis." Thesis, University of Cambridge, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.627168.

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Books on the topic "Dynein"

1

Markus, Steven M., ed. Dynein. New York, NY: Springer US, 2023. http://dx.doi.org/10.1007/978-1-0716-2958-1.

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2

King, Stephen M. Dyneins: Structure, biology and disease. Amsterdam: Academic Press, 2012.

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3

Kemal, Shahrnaz. Distinct Roles for Dynein Regulatory Proteins NudE and NudEL in Brain Development. [New York, N.Y.?]: [publisher not identified], 2013.

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4

Hu, Daniel Jun-Kit. Roles for Cytoplasmic Dynein and the Unconventional Kinesin, KIF1a, during Cortical Development. [New York, N.Y.?]: [publisher not identified], 2015.

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5

Weil, Sarah J. Novel Regulatory Mechanisms of Cytoplasmic Dynein: A Role for the Complex Base. [New York, N.Y.?]: [publisher not identified], 2013.

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6

Villarin, Joseph Manuel. Regulation of Cytoplasmic Dynein via Local Synthesis of its Cofactors, Lis1 and p150Glued. [New York, N.Y.?]: [publisher not identified], 2016.

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7

Freidlin, Mark I., ed. The Dynkin Festschrift. Boston, MA: Birkhäuser Boston, 1994. http://dx.doi.org/10.1007/978-1-4612-0279-0.

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8

1943-, Warner Fred D., Satir Peter, and Gibbons Ian R, eds. Cell movement. New York: Liss, 1989.

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9

Urabe, Tohsuke. Dynkin Graphs and Quadrilateral Singularities. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/bfb0084369.

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Urabe, Tohsuke. Dynkin graphs and quadrilateral singularities. Berlin: Springer-Verlag, 1993.

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Book chapters on the topic "Dynein"

1

Lau, Clinton K. "Reconstitution of Dynein/Dynactin Transport Using Recombinant Dynein." In Methods in Molecular Biology, 135–56. New York, NY: Springer US, 2023. http://dx.doi.org/10.1007/978-1-0716-2958-1_9.

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2

Oiwa, Kazuhiro. "Dynein Motility: Mechanism." In Encyclopedia of Biophysics, 1–15. Berlin, Heidelberg: Springer Berlin Heidelberg, 2020. http://dx.doi.org/10.1007/978-3-642-35943-9_752-1.

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Oiwa, Kazuhiro. "Dynein Motility: Mechanism." In Encyclopedia of Biophysics, 558–72. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_752.

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Diamant, Aristides G., and Andrew P. Carter. "Dynein Family Classification." In Encyclopedia of Biophysics, 552–58. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_765.

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Cordova, Nicolas J., Ronald D. Vale, and George F. Oster. "Dynein-Microtubule Interactions." In Biologically Inspired Physics, 207–15. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4757-9483-0_19.

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6

Pfister, K. K. "Dynein." In Encyclopedia of Biological Chemistry, 184–87. Elsevier, 2013. http://dx.doi.org/10.1016/b978-0-12-378630-2.00424-2.

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"Dynein." In Encyclopedia of Genetics, Genomics, Proteomics and Informatics, 571. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_4972.

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Pfister, K. Kevin. "Dynein." In Encyclopedia of Biological Chemistry, 827–31. Elsevier, 2004. http://dx.doi.org/10.1016/b0-12-443710-9/00188-5.

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"dynein, n." In Oxford English Dictionary. 3rd ed. Oxford University Press, 2023. http://dx.doi.org/10.1093/oed/9123746642.

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Neisch, Amanda L., Adam W. Avery, Min-Gang Li, and Thomas S. Hays. "Drosophila cytoplasmic dynein." In Dyneins, 568–627. Elsevier, 2018. http://dx.doi.org/10.1016/b978-0-12-809471-6.00021-8.

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Conference papers on the topic "Dynein"

1

"Simple qualitative deterministic model of dynein." In Engineering Mechanics 2018. Institute of Theoretical and Applied Mechanics of the Czech Academy of Sciences, 2018. http://dx.doi.org/10.21495/91-8-717.

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2

Ueno, H., T. Yasunaga, C. Shingyoji, T. Yamaguchi, and K. Hirose. "Dynein Pulls Microtubules Without Rotating Its Stalk." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-206430.

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Dynein is a motor protein that hydrolyses ATP and moves toward the minus end of a microtubule (MT). A dynein molecule has one to three heavy chains, each consisting of three domains: a head, a stalk and a tail. ATP is bound and hydrolysed in the head, which has a ring-like structure composed of 6 AAA+ domains. The stalk is an antiparallel coiled-coil, 10–15 nm long, and has a nucleotide-dependent MT-binding domain at the tip (1) (Fig. 1). It has been proposed that the nucleotide-dependent binding affinity of the tubulin-binding site at the tip of the stalk is modulated by the two alpha helices in the coiled-coil sliding over each other (2). However, it is not known how a dynein molecule moves along a microtubule (MT).

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Chen, Duanduan, Kyosuke Shinohara, Jun Ren, and Hiroshi Hamada. "The Protein-Driven Ciliary Motility in Embryonic Nodes: A Computational Model of Ciliary Ultrastructure." In ASME 2013 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/imece2013-62460.

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The movement of embryonic cilia presents a crucial function in specifying left-right axis for vertebrates. Those mono-cilia are primary (9+0) cilia, whose characteristic architecture is based on a cylindrical arrangement of 9 microtubule doublets. Dynein motors located between adjacent doublets convert the chemical energy of ATP hydrolysis into mechanical work that induces doublet sliding. Passive components, such as the mediated cytoplasm, the ciliary membrane, and other possibly-existent structures constraint the ciliary motion and maintain the cilia structural integrity, thus resulting in the axonemal bending. Dynein motors located along microtubule doublets in a motile nodal cilium activate in a sequential manner. However, due to inherent difficulties, the dynein activation patterns in moving cilia can hardly be directly observed. The exact mechanism that controls ciliary motion is still unrevealed. In this work, we present a protein-structure model reconstructed from transmission electron microscopy image set of a wide-type embryonic cilium to study the dynein-dependent ciliary motility. This model includes time accurate three-dimensional solid mechanics analysis of the sliding between adjacent microtubule doublets and their induced ciliary bending. As a conceptual test, the mathematical model provides a platform to investigate various assumptions of dynein activity, which facilitates us to evaluate their rationality and to propose the most possible dynein activation pattern. The proposed protein-trigger pattern can reproduce the rotation-like ciliary motion as observed by experiments. Further application of this approach to mutant cilia with ultrastructural modifications also shows consistency to experimental observations. This computational model based on solid mechanics analysis may improve our understandings regarding the protein-beating problems of cilia, and may guide and inspire further experimental investigations on this topic.

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Xu, Gang, Kate S. Wilson, Ruth J. Okamoto, Jin-Yu Shao, Susan K. Dutcher, and Philip V. Bayly. "The Apparent Flexural Rigidity of the Flagellar Axoneme Depends on Resistance to Inter-Doublet Sliding." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80220.

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Cilia are thin subcellular organelles that bend actively to propel fluid. The ciliary cytoskeleton (the axoneme) consists of nine outer microtubule doublets surrounding a central pair of singlet microtubules. Large bending deformations of the axoneme involve relative sliding of the outer doublets, driven by the motor protein dynein. Ciliary structure and function have been studied extensively, but details of the mechanics and coordination of the axoneme remain unclear. In particular, dynein activity must be switched on and off at specific times and locations to produce an oscillatory, propulsive beat. Leading hypotheses assert that mechanical feedback plays a role in the control of dynein activity, but these ideas remain speculative.

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Anders, K. L., K. B. R. Belchamber, D. C. A. Gaboriau, P. J. Barnes, and L. E. Donnelly. "Dynein Has Defective Activity in COPD Macrophage Phagocytosis." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a3779.

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Bayly, Philip V., and Kate S. Wilson. "Unstable Oscillations and Wave Propagation in Flagella." In ASME 2015 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. American Society of Mechanical Engineers, 2015. http://dx.doi.org/10.1115/detc2015-46920.

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Flagella are active, beam-like, sub-cellular organelles that use wavelike oscillations to propel the cell. The mechanisms underlying the coordinated beating of flagella remain incompletely understood despite the fundamental importance of these organelles. The axoneme (the cytoskeletal structure of flagella) consists of microtubule doublets connected by passive and active elements. The motor protein dynein is known to drive active bending, but dynein activity must be regulated to generate oscillatory, propulsive waveforms. Mathematical models of flagella motion generate quantitative predictions that can be analyzed to test hypotheses concerning dynein regulation. Here we investigate the emergence of unstable modes in a mathematical model of flagella motion with feedback from inter-doublet separation (the “geometric clutch” or GC model). The unstable modes predicted by the model may be used to critically evaluate the underlying hypothesis. The least stable mode of the GC model exhibits switching at the base and robust base-to-tip propagation.

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anders, katie, Kylie BR Belchamber, Peter J. Barnes, and Louise E. Donnelly. "Inhibition of dynein motors improves macrophage phagocytosis in COPD." In ERS International Congress 2017 abstracts. European Respiratory Society, 2017. http://dx.doi.org/10.1183/1393003.congress-2017.pa981.

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Ashikari, N., Y. Shitaka, H. Sakaue, T. Takahagi, H. Kojima, K. Oiwa, and H. Suzuki. "Quantitative characterization of guided motion of dynein-microtubule system." In 2011 International Conference on Solid State Devices and Materials. The Japan Society of Applied Physics, 2011. http://dx.doi.org/10.7567/ssdm.2011.p-11-1.

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Tetsutaro Murakami, Takeshi Sugie, Takahide Kon, and Ryuji Yokokawa. "Unidirectional motion of microtubules and microspheres by Dynein motor protein." In 2007 IEEE 20th International Conference on Micro Electro Mechanical Systems (MEMS). IEEE, 2007. http://dx.doi.org/10.1109/memsys.2007.4433074.

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Bayly, P. V., B. L. Lewis, E. C. Ranz, R. J. Okamoto, R. B. Pless, and S. K. Dutcher. "Kinematics and Kinetics of Flagellar Locomotion in Chlamydomonas Reinhardtii." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53290.

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The forces exerted on the flagellum of the swimming alga Chlamydomonas reinhardtii by surrounding fluid are estimated from video data. “Wild-type” cells, as well as cells lacking inner dynein arms (ida3) and cells lacking outer dynein arms (oda2) were imaged (350 fps; 125 nm). Digital image registration and sorting algorithms provide high-resolution descriptions of the kinematics of the cell body and flagellum. The swimming cell is then modeled as an ellipsoid in Stokes flow, propelled by viscous forces that depend linearly on the velocity of the flagellum. The coefficients (CN and CT) that related normal and tangent forces on the flagellum to corresponding velocity components are estimated from equilibrium requirements. Their values are consistent among all three genotypes and similar to theoretical predictions.

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Reports on the topic "Dynein"

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Song, Chunying. Role of Dynein Light Chain 1 in Tamoxifen Resistance in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, March 2007. http://dx.doi.org/10.21236/ada469357.

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King, Megan, and Mark Lemmon. The Role of Dynamin in the Regulation of Signaling by the erbB Family of Receptor Tyrosine Kinases. Fort Belvoir, VA: Defense Technical Information Center, April 2003. http://dx.doi.org/10.21236/ada416747.

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Avni, Adi, and Gitta L. Coaker. Proteomic investigation of a tomato receptor like protein recognizing fungal pathogens. United States Department of Agriculture, January 2015. http://dx.doi.org/10.32747/2015.7600030.bard.

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Maximizing food production with minimal negative effects on the environment remains a long-term challenge for sustainable food production. Microbial pathogens cause devastating diseases, minimizing crop losses by controlling plant diseases can contribute significantly to this goal. All plants possess an innate immune system that is activated after recognition of microbial-derived molecules. The fungal protein Eix induces defense responses in tomato and tobacco. Plants recognize Eix through a leucine-rich-repeat receptor- like-protein (LRR-RLP) termed LeEix. Despite the knowledge obtained from studies on tomato, relatively little is known about signaling initiated by RLP-type immune receptors. The focus of this grant proposal is to generate a foundational understanding of how the tomato xylanase receptor LeEix2 signals to confer defense responses. LeEix2 recognition results in pattern triggered immunity (PTI). The grant has two main aims: (1) Isolate the LeEix2 protein complex in an active and resting state; (2) Examine the biological function of the identified proteins in relation to LeEix2 signaling upon perception of the xylanase elicitor Eix. We used two separate approaches to isolate receptor interacting proteins. Transgenic tomato plants expressing LeEix2 fused to the GFP tag were used to identify complex components at a resting and activated state. LeEix2 complexes were purified by mass spectrometry and associated proteins identified by mass spectrometry. We identified novel proteins that interact with LeEix receptor by proteomics analysis. We identified two dynamin related proteins (DRPs), a coiled coil – nucleotide binding site leucine rich repeat (SlNRC4a) protein. In the second approach we used the split ubiquitin yeast two hybrid (Y2H) screen system to identified receptor-like protein kinase At5g24010-like (SlRLK-like) (Solyc01g094920.2.1) as an interactor of LeEIX2. We examined the role of SlNRC4a in plant immunity. Co-immunoprecipitation demonstrates that SlNRC4a is able to associate with different PRRs. Physiological assays with specific elicitors revealed that SlNRC4a generally alters PRR-mediated responses. SlNRC4a overexpression enhances defense responses while silencing SlNRC4 reduces plant immunity. We propose that SlNRC4a acts as a non-canonical positive regulator of immunity mediated by diverse PRRs. Thus, SlNRC4a could link both intracellular and extracellular immune perception. SlDRP2A localizes at the plasma membrane. Overexpression of SlDRP2A increases the sub-population of LeEIX2 inVHAa1 endosomes, and enhances LeEIX2- and FLS2-mediated defense. The effect of SlDRP2A on induction of plant immunity highlights the importance of endomembrane components and endocytosis in signal propagation during plant immune . The interaction of LeEIX2 with SlRLK-like was verified using co- immunoprecipitation and a bimolecular fluorescence complementation assay. The defence responses induced by EIX were markedly reduced when SlRLK-like was over-expressed, and mutation of slrlk-likeusing CRISPR/Cas9 increased EIX- induced ethylene production and SlACSgene expression in tomato. Co-expression of SlRLK-like with different RLPs and RLKs led to their degradation, apparently through an endoplasmic reticulum-associated degradation process. We provided new knowledge and expertise relevant to expression of specific be exploited to enhance immunity in crops enabling the development of novel environmentally friendly disease control strategies.

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Health hazard evaluation report: HETA-83-307-1561, U.S. Environmental Protection Agency, Chem-Dyne Hazardous Waste Site, Hamilton, Ohio. U.S. Department of Health and Human Services, Public Health Service, Centers for Disease Control, National Institute for Occupational Safety and Health, January 1985. http://dx.doi.org/10.26616/nioshheta833071561.

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