Helix sliding in the stalk coiled coil of dynein couples ATPase and microtubule binding
Open accessAbstract
Coupling between ATPase and track binding sites is essential for molecular motors to move along cytoskeletal tracks. In dynein, these sites are separated by a long coiled coil stalk that must mediate communication between them, but the underlying mechanism remains unclear. Here we show that changes in registration between the two helices of the coiled coil can perform this function. We locked the coiled coil at three specific registrations using oxidation to disulfides of paired cysteine residues introduced into the two helices. These trapped ATPase activity either in a microtubule-independent high or low state, and microtubule binding activity either in an ATP-insensitive strong or weak state, depending on the registry of the coiled coil. Our results provide direct evidence that dynein uses sliding between the two helices of the stalk to couple ATPase and microtubule binding activities during its mechanochemical cycle.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Natural coiled coils are dynamic and play central roles in a multitude of biological functions.
“Natural coiled coils, on the other hand, are dynamic and play central roles in a multitude of biological functions.13−17”
From Assessment of the Topology and Oligomerisation States of Coiled Coils Using Metadynamics with Conformational Restraints (2025) · cites this paper as [14]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
1 retracted
Reck‐Peterson, S. L., & Vale, R. D. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2637011100 · Cited by 89 · see citing works
RetractedMechanics of Motor Proteins and the Cytoskeleton
Howard, & Clark (2002) · Applied Mechanics Reviews · doi:10.1115/1.1451234 · Cited by 2,909 · see citing works
The Molecular Motor Toolbox for Intracellular Transport
Vale, R. D. (2003) · Cell · doi:10.1016/s0092-8674(03)00111-9 · Cited by 1,982 · see citing works
Neuwald, A. F., Aravind, L., Spouge, J. L., & Koonin, E. V. (1999) · Genome Research · doi:10.1101/gr.9.1.27 · Cited by 1,811 · see citing works
Three-Dimensional Electron Microscopy of Macromolecular Assemblies
Frank, J. (2006) · Oxford University Press eBooks · doi:10.1093/acprof:oso/9780195182187.001.0001 · Cited by 1,121 · see citing works
Schliwa, M., & Woehlke, G. (2003) · Nature · doi:10.1038/nature01601 · Cited by 1,069 · see citing works
AAA+ superfamily ATPases: common structure–diverse function
Ogura, T., & Wilkinson, A. J. (2001) · Genes to Cells · doi:10.1046/j.1365-2443.2001.00447.x · Cited by 958 · see citing works
Single-molecule analysis of dynein processivity and stepping behavior.
Reck-Peterson, S., Yildiz, A., Carter, A., Gennerich, A., Zhang, N., & Vale, R. (2006) · Cell · doi:10.1016/j.cell.2006.05.046 · Cited by 649 · see citing works
Dynein: A Protein with Adenosine Triphosphatase Activity from Cilia
Gibbons, I. R., & Rowe, A. J. (1965) · Science · doi:10.1126/science.149.3682.424 · Cited by 594 · see citing works
Self-citationTwo-State Allosteric Behavior in a Single-Domain Signaling Protein
Volkman, B. F., Lipson, D., Wemmer, D. E., & Kern, D. (2001) · Science · doi:10.1126/science.291.5512.2429 · Cited by 594 · see citing works
Retrograde transport by the microtubule-associated protein MAP 1C
Paschal, B. M., & Vallée, R. (1987) · Nature · doi:10.1038/330181a0 · Cited by 551 · see citing works
Dynein structure and power stroke
Burgess, S. A., Walker, M. L., Sakakibara, H., Knight, P. J., & Oiwa, K. (2003) · Nature · doi:10.1038/nature01377 · Cited by 508 · see citing works
Self-citationLee, S., Sowa, M. E., Watanabe, Y.-H., Sigler, P. B., Chiu, W., Yoshida, M., & Tsai, F. (2003) · Cell · doi:10.1016/s0092-8674(03)00807-9 · Cited by 414 · see citing works
Dynein: An ancient motor protein involved in multiple modes of transport
Vallee, R. B., Williams, J. C., Varma, D., & Barnhart, L. E. (2003) · Journal of Neurobiology · doi:10.1002/neu.10314 · Cited by 411 · see citing works
Force-Induced Bidirectional Stepping of Cytoplasmic Dynein
Gennerich, A., Carter, A. P., Reck‐Peterson, S. L., & Vale, R. D. (2007) · Cell · doi:10.1016/j.cell.2007.10.016 · Cited by 376 · see citing works
Three-Dimensional Electron Microscopy of Macromolecular Assemblies
(1996) · Elsevier eBooks · doi:10.1016/b978-0-12-265040-6.x5000-0 · Cited by 342 · see citing works
King, S. M. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(00)00009-4 · Cited by 338 · see citing works
Genetic Analysis of the Cytoplasmic Dynein Subunit Families
Pfister, K. K., Shah, P. R., Hummerich, H., Russ, A., Cotton, J. A., Ahmad‐Annuar, A., King, S. M., & Fisher, E. (2006) · PLoS Genetics · doi:10.1371/journal.pgen.0020001 · Cited by 305 · see citing works
An extended microtubule-binding structure within the dynein motor domain
Gee, M. A., Heuser, J. E., & Vallee, R. B. (1997) · Nature · doi:10.1038/37663 · Cited by 292 · see citing works
Arora, K., & Brooks, C. L. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706443104 · Cited by 269 · see citing works
Structure and Functional Role of Dynein's Microtubule-Binding Domain
Carter, A. P., Garbarino, J. E., Kubalek, E. W., Shipley, W. E., Cho, C., Milligan, R. A., Vale, R. D., & Gibbons, I. R. (2008) · Science · doi:10.1126/science.1164424 · Cited by 248 · see citing works
Self-citationStructural comparison of purified dynein proteins with in situ dynein arms
Goodenough, U. W., & Heuser, J. (1984) · Journal of Molecular Biology · doi:10.1016/0022-2836(84)90272-9 · Cited by 223 · see citing works
Kon, T., Nishiura, M., Ohkura, R., Toyoshima, Y. Y., & Sutoh, K. (2004) · Biochemistry · doi:10.1021/bi048985a · Cited by 220 · see citing works
Self-citationGibbons, I. R., Garbarino, J. E., Tan, C. E., Reck‐Peterson, S. L., Vale, R. D., & Carter, A. P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501636200 · Cited by 171 · see citing works
Self-citationM Domains Couple the ClpB Threading Motor with the DnaK Chaperone Activity
Haslberger, T., Weibezahn, J., Zahn, R., Lee, S., Tsai, F., Bukau, B., & Mogk, A. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.11.008 · Cited by 163 · see citing works
ATP hydrolysis cycle–dependent tail motions in cytoplasmic dynein
Kon, T., Mogami, T., Ohkura, R., Nishiura, M., & Sutoh, K. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb930 · Cited by 160 · see citing works
Self-citationGibbons, I. R., Lee-Eiford, A., Mócz, G., Phillipson, C. A., Tang, W., & Gibbons, B. H. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61574-1 · Cited by 134 · see citing works
Self-citationStructural characterization of a dynein motor domain
Samsó, M., Radermacher, M., Frank, J., & Koonce, M. P. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1584 · Cited by 133 · see citing works
Tang, W. Y., & Gibbons, I. R. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45440-3 · Cited by 127 · see citing works
Self-citationRecent progress in dynein structure and mechanism.
Oiwa, K., & Sakakibara, H. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2004.12.006 · Cited by 108 · see citing works
Structures and organisation of AAA+ enhancer binding proteins in transcriptional activation
Schumacher, J., Joly, N., Rappas, M., Zhang, X., & Buck, M. (2006) · Journal of Structural Biology · doi:10.1016/j.jsb.2006.01.006 · Cited by 106 · see citing works
Silvanovich, A., Li, M.-G., Serr, M., Mische, S. E., & Hays, T. S. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-10-0675 · Cited by 97 · see citing works
Identification of a Microtubule-binding Domain in a Cytoplasmic Dynein Heavy Chain
Koonce, M. P. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.32.19714 · Cited by 95 · see citing works
The coordination of cyclic microtubule association/dissociation and tail swing of cytoplasmic dynein
Imamula, K., Kon, T., Ohkura, R., & Sutoh, K. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702370104 · Cited by 94 · see citing works
Self-citationPresteady state kinetic analysis of vanadate-induced inhibition of the dynein ATPase.
Shimizu, T., & Johnson, K. A. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43993-7 · Cited by 92 · see citing works
Nishiura, M., Kon, T., Shiroguchi, K., Ohkura, R., Shima, T., Toyoshima, Y. Y., & Sutoh, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313362200 · Cited by 90 · see citing works
Self-citationDynein motors of the Chlamydomonas flagellum
DiBella, L. M., & King, S. M. (2001) · International review of cytology · doi:10.1016/s0074-7696(01)10007-0 · Cited by 87 · see citing works
25Å Resolution Structure of a Cytoplasmic Dynein Motor Reveals a Seven-member Planar Ring
Samsó, M., & Koonce, M. P. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.05.063 · Cited by 79 · see citing works
Phase Partition Analysis of Nucleotide Binding to Axonemal Dynein
Mócz, G., & Gibbons, I. R. (1996) · Biochemistry · doi:10.1021/bi960662u · Cited by 72 · see citing works
Self-citationThe structure of dynein-c by negative stain electron microscopy
Burgess, S. A., Walker, M. L., Sakakibara, H., Oiwa, K., & Knight, P. J. (2003) · Journal of Structural Biology · doi:10.1016/j.jsb.2003.10.005 · Cited by 68 · see citing works
Self-citationTwo modes of microtubule sliding driven by cytoplasmic dynein
Shima, T., Kon, T., Imamula, K., Ohkura, R., & Sutoh, K. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606794103 · Cited by 64 · see citing works
Self-citationMicrotubules accelerate ADP release by dynein
Holzbaur, E. L. F., & Johnson, K. A. (1989) · Biochemistry · doi:10.1021/bi00443a034 · Cited by 59 · see citing works
Vallee, R. B., & Gee, M. A. (1998) · Trends in Cell Biology · doi:10.1016/s0962-8924(98)01379-8 · Cited by 52 · see citing works
ADP release is rate limiting in steady state turnover by the dynein adenosinetriphosphatase
Holzbaur, E. L. F., & Johnson, K. A. (1989) · Biochemistry · doi:10.1021/bi00439a036 · Cited by 51 · see citing works
Kinetic Characterization of Tail Swing Steps in the ATPase Cycle of Dictyostelium Cytoplasmic Dynein
Mogami, T., Kon, T., Ito, K., & Sutoh, K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701914200 · Cited by 47 · see citing works
Self-citationThe role of the dynein stalk in cytoplasmic and flagellar motility
Gee, M., & Vallee, R. B. (1998) · European Biophysics Journal · doi:10.1007/s002490050157 · Cited by 37 · see citing works
Coiled coils meet the chaperone world
Martin, J., Gruber, M., & Lupas, A. N. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.07.004 · Cited by 36 · see citing works
Flagged first, then by citations
1 of the 48 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Regulators of the cytoplasmic dynein motor
Kardon, J. R., & Vale, R. D. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2804 · Cited by 603 · see citing works
Functions and mechanics of dynein motor proteins
Roberts, A. J., Kon, T., Knight, P. J., Sutoh, K., & Burgess, S. A. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3667 · Cited by 537 · see citing works
Self-citationLIS1 and NudE Induce a Persistent Dynein Force-Producing State
McKenney, R. J., Vershinin, M. D., Kunwar, A., Vallee, R. B., & Gross, S. P. (2010) · Cell · doi:10.1016/j.cell.2010.02.035 · Cited by 349 · see citing works
The 2.8 Å crystal structure of the dynein motor domain
Kon, T., Oyama, T., Shimo‐Kon, R., Imamula, K., Shima, T., Sutoh, K., & Kurisu, G. (2012) · Nature · doi:10.1038/nature10955 · Cited by 260 · see citing works
Self-citationCrystal Structure of the Dynein Motor Domain
Carter, A. P., Cho, C., Jin, L., & Vale, R. D. (2011) · Science · doi:10.1126/science.1202393 · Cited by 254 · see citing works
Mechanism and Regulation of Cytoplasmic Dynein
Cianfrocco, M. A., DeSantis, M. E., Leschziner, A. E., & Reck‐Peterson, S. L. (2015) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100814-125438 · Cited by 245 · see citing works
On and Around Microtubules: An Overview
Wade, R. H. (2009) · Molecular Biotechnology · doi:10.1007/s12033-009-9193-5 · Cited by 234 · see citing works
Lis1 Acts as a “Clutch” between the ATPase and Microtubule-Binding Domains of the Dynein Motor
Huang, J., Roberts, A. J., Leschziner, A. E., & Reck‐Peterson, S. L. (2012) · Cell · doi:10.1016/j.cell.2012.07.022 · Cited by 228 · see citing works
Self-citationDynein achieves processive motion using both stochastic and coordinated stepping
Qiu, W., Derr, N. D., Goodman, B. S., Villa, E., Wu, D., Shih, W. M., & Reck‐Peterson, S. L. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2205 · Cited by 202 · see citing works
Moving into the cell: single-molecule studies of molecular motors in complex environments
Veigel, C., & Schmidt, C. F. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3062 · Cited by 177 · see citing works
Multiple modes of cytoplasmic dynein regulation
Vallee, R. B., McKenney, R. J., & Ori-McKenney, K. M. (2012) · Nature Cell Biology · doi:10.1038/ncb2420 · Cited by 172 · see citing works
Structure of human cytoplasmic dynein-2 primed for its power stroke
Schmidt, H., Zalyte, R., Urnavicius, L., & Carter, A. P. (2014) · Nature · doi:10.1038/nature14023 · Cited by 165 · see citing works
Structural Basis for Microtubule Binding and Release by Dynein
Redwine, W. B., Hernández-López, R. A., Zou, S., Huang, J., Reck‐Peterson, S. L., & Leschziner, A. E. (2012) · Science · doi:10.1126/science.1224151 · Cited by 163 · see citing works
An endosomal tether undergoes an entropic collapse to bring vesicles together
Murray, D. H., Jahnel, M., Lauer, J. L., Avellaneda, M. J., Brouilly, N., Cezanne, A., Morales-Navarrete, H. A., Perini, E. D., Ferguson, C., Lupas, A. N., et al. (2016) · Nature · doi:10.1038/nature19326 · Cited by 161 · see citing works
Structural mechanism of the dynein power stroke
Lin, J., Okada, K., Raytchev, M., Smith, M. C., & Nicastro, D. (2014) · Nature Cell Biology · doi:10.1038/ncb2939 · Cited by 151 · see citing works
Self‐Assembly of Coiled Coils in Synthetic Biology: Inspiration and Progress
Marsden, H. R., & Kros, A. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.200904943 · Cited by 151 · see citing works
How Dynein Moves Along Microtubules
Bhabha, G., Johnson, G. T., Schroeder, C. M., & Vale, R. D. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.11.004 · Cited by 149 · see citing works
Structure and Mechanics of Dynein Motors
Canty, J. T., Tan, R., Kusakci, E., Fernandes, J., & Yıldız, A. (2021) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-111020-101511 · Cited by 129 · see citing works
Propulsive nanomachines: the convergent evolution of archaella, flagella and cilia
Beeby, M., Ferreira, J. L., Tripp, P., Albers, S.-V., & Mitchell, D. R. (2020) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuaa006 · Cited by 110 · see citing works
Nicholas, M. P., Berger, F., Rao, L., Brenner, S., Cho, C., & Gennerich, A. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417422112 · Cited by 108 · see citing works
Review: Structure and mechanism of the dynein motor ATPase
Schmidt, H., & Carter, A. P. (2016) · Biopolymers · doi:10.1002/bip.22856 · Cited by 116 · see citing works
X-ray structure of a functional full-length dynein motor domain
Kon, T., Sutoh, K., & Kurisu, G. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2074 · Cited by 115 · see citing works
Self-citationLafrance‐Vanasse, J., Williams, G. J., & Tainer, J. A. (2015) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2014.12.004 · Cited by 107 · see citing works
Allosteric Communication in the Dynein Motor Domain
Bhabha, G., Cheng, H., Zhang, N., Moeller, A., Liao, M., Speir, J. A., Cheng, Y., & Vale, R. D. (2014) · Cell · doi:10.1016/j.cell.2014.10.018 · Cited by 104 · see citing works
Allen, W. J., Corey, R. A., Oatley, P., Sessions, R. B., Baldwin, S. A., Radford, S. E., Tuma, R., & Collinson, I. (2016) · eLife · doi:10.7554/elife.15598 · Cited by 103 · see citing works
Crystal clear insights into how the dynein motor moves
Carter, A. P. (2013) · Journal of Cell Science · doi:10.1242/jcs.120725 · Cited by 97 · see citing works
Lis1 regulates dynein by sterically blocking its mechanochemical cycle
Toropova, K., Zou, S., Roberts, A. J., Redwine, W. B., Goodman, B. S., Reck‐Peterson, S. L., & Leschziner, A. E. (2014) · eLife · doi:10.7554/elife.03372 · Cited by 97 · see citing works
Self-citationATP-Driven Remodeling of the Linker Domain in the Dynein Motor
Roberts, A. J., Malkova, B., Walker, M. L., Sakakibara, H., Numata, N., Kon, T., Ohkura, R., Edwards, T. A., Knight, P. J., Sutoh, K., et al. (2012) · Structure · doi:10.1016/j.str.2012.07.003 · Cited by 94 · see citing works
Self-citationTension on the linker gates the ATP-dependent release of dynein from microtubules
Cleary, F. B., DeWitt, M. A., Bilyard, T., Htet, Z. M., Belyy, V., Chan, D. D., Chang, A. Y., & Yıldız, A. (2014) · Nature Communications · doi:10.1038/ncomms5587 · Cited by 93 · see citing works
Structural Biology of TRP Channels
Hellmich, U. A., & Gaudet, R. (2014) · Handbook of experimental pharmacology · doi:10.1007/978-3-319-05161-1_10 · Cited by 92 · see citing works
Lis1 Has Two Opposing Modes of Regulating Cytoplasmic Dynein
DeSantis, M. E., Cianfrocco, M. A., Htet, Z. M., Tran, P. T., Reck‐Peterson, S. L., & Leschziner, A. E. (2017) · Cell · doi:10.1016/j.cell.2017.08.037 · Cited by 90 · see citing works
ATP Consumption of Eukaryotic Flagella Measured at a Single-Cell Level
Chen, D. T. N., Heymann, M., Fraden, S., Nicastro, D., & Dogic, Z. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.11.003 · Cited by 89 · see citing works
Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule
Lacey, S. E., He, S., Scheres, S. H. W., & Carter, A. P. (2019) · eLife · doi:10.7554/elife.47145 · Cited by 89 · see citing works
Activation and Regulation of Cytoplasmic Dynein
Canty, J. T., & Yıldız, A. (2020) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.02.002 · Cited by 89 · see citing works
The AAA3 domain of cytoplasmic dynein acts as a switch to facilitate microtubule release
DeWitt, M. A., Cypranowska, C. A., Cleary, F. B., Belyy, V., & Yıldız, A. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2930 · Cited by 87 · see citing works
Kressler, D., Hurt, E., Bergler, H., & Baßler, J. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.06.017 · Cited by 87 · see citing works
Toropova, K., Mladenov, M., & Roberts, A. J. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3391 · Cited by 85 · see citing works
Self-citationMarzo, M. G., Griswold, J. M., & Markus, S. M. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-0492-1 · Cited by 78 · see citing works
Function and regulation of dynein in mitotic chromosome segregation
Raaijmakers, J. A., & Medema, R. H. (2014) · Chromosoma · doi:10.1007/s00412-014-0468-7 · Cited by 75 · see citing works
Nudel/NudE and Lis1 promote dynein and dynactin interaction in the context of spindle morphogenesis
Wang, S., Ketcham, S. A., Schön, A., Goodman, B. E., Wang, Y., Yates, J. R., Freire, E., Schroer, T. A., & Zheng, Y. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-05-0283 · Cited by 71 · see citing works
Synergistic autoinhibition and activation mechanisms control kinesin-1 motor activity
Chiba, K., Ori-McKenney, K. M., Niwa, S., & McKenney, R. J. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110900 · Cited by 70 · see citing works
Imai, H., Shima, T., Sutoh, K., Walker, M., Knight, P. J., Kon, T., & Burgess, S. A. (2015) · Nature Communications · doi:10.1038/ncomms9179 · Cited by 65 · see citing works
Self-citationGao, Y., Sirinakis, G., & Zhang, Y. (2011) · Journal of the American Chemical Society · doi:10.1021/ja204005r · Cited by 65 · see citing works
Directionality of dynein is controlled by the angle and length of its stalk
Can, S., Lacey, S. E., Gür, M., Carter, A. P., & Yıldız, A. (2019) · Nature · doi:10.1038/s41586-019-0914-z · Cited by 65 · see citing works
Molecular mechanism of cytoplasmic dynein tension sensing
Rao, L., Berger, F., Nicholas, M. P., & Gennerich, A. (2019) · Nature Communications · doi:10.1038/s41467-019-11231-8 · Cited by 65 · see citing works
Molecular mechanics of coiled coils loaded in the shear geometry
Goktas, M., Luo, C., Sullan, R. M. A., Bergues-Pupo, A. E., Lipowsky, R., Verde, A. V., & Blank, K. G. (2018) · Chemical Science · doi:10.1039/c8sc01037d · Cited by 64 · see citing works
The mechanism of dynein motility: Insight from crystal structures of the motor domain
Cho, C., & Vale, R. D. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.10.009 · Cited by 56 · see citing works
Single-molecule observation of helix staggering, sliding, and coiled coil misfolding
Xi, Z., Gao, Y., Sirinakis, G., Guo, H., & Zhang, Y. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1116784109 · Cited by 55 · see citing works
Controlling Self-Assembly of a Peptide-Based Material via Metal-Ion Induced Registry Shift
Anzini, P., Xu, C., Hughes, S. A., Magnotti, E. L., Jiang, T., Hemmingsen, L., Demeler, B., & Conticello, V. P. (2013) · Journal of the American Chemical Society · doi:10.1021/ja404677c · Cited by 55 · see citing works
Creating biomolecular motors based on dynein and actin-binding proteins
Furuta, A., Amino, M., Yoshio, M., Oiwa, K., Kojima, H., & Furuta, K. (2016) · Nature Nanotechnology · doi:10.1038/nnano.2016.238 · Cited by 51 · see citing works
Uchimura, S., Fujii, T., Takazaki, H., Ayukawa, R., Nishikawa, Y., Minoura, I., Hachikubo, Y., Kurisu, G., Sutoh, K., Kon, T., et al. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201407039 · Cited by 48 · see citing works
Self-citationLy, S., & Lehrer, S. S. (2012) · Biochemistry · doi:10.1021/bi3006835 · Cited by 44 · see citing works
Stewart, C. M., Buffalo, C. Z., Valderrama, J. A., Henningham, A., Cole, J. N., Nizet, V., & Ghosh, P. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1606160113 · Cited by 41 · see citing works
Nanometer-accuracy distance measurements between fluorophores at the single-molecule level
Niekamp, S., Sung, J., Huynh, W., Bhabha, G., Vale, R. D., & Stuurman, N. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1815826116 · Cited by 37 · see citing works
Angular measurements of the dynein ring reveal a stepping mechanism dependent on a flexible stalk
Lippert, L. G., Dadosh, T., Hadden‐Perilla, J. A., Karnawat, V., Diroll, B. T., Murray, C. B., Holzbaur, E. L. F., Schulten, K. J., Reck‐Peterson, S. L., & Goldman, Y. E. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1620149114 · Cited by 40 · see citing works
Li, L., Alper, J., & Alexov, E. G. (2016) · Scientific Reports · doi:10.1038/srep31523 · Cited by 39 · see citing works
Soluble adenylyl cyclase of sea urchin spermatozoa
Vacquier, V. D., Loza-Huerta, A., García-Rincón, J., Darszon, A., & Beltrán, C. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.07.011 · Cited by 33 · see citing works
Structure of the Entire Stalk Region of the Dynein Motor Domain
Nishikawa, Y., Oyama, T., Kamiya, N., Kon, T., Toyoshima, Y. Y., Nakamura, H., & Kurisu, G. (2014) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.06.023 · Cited by 33 · see citing works
Self-citationCarter, A. P., & Vale, R. D. (2010) · Biochemistry and Cell Biology · doi:10.1139/o09-127 · Cited by 33 · see citing works
Seeing cilia: imaging modalities for ciliary motion and clinical connections
Lever, J. E. P., Shei, R., Bermingham, B., Phillips, S. E., Turner, B., Rowe, S. M., & Solomon, G. M. (2018) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00556.2017 · Cited by 31 · see citing works
Structural basis for two-way communication between dynein and microtubules
Nishida, N., Komori, Y., Takarada, O., Watanabe, A., Tamura, S., Kubo, S., Shimada, I., & Kikkawa, M. (2020) · Nature Communications · doi:10.1038/s41467-020-14842-8 · Cited by 31 · see citing works
Nucleotide‐dependent behavior of single molecules of cytoplasmic dynein on microtubules in vitro
Miura, M., Matsubara, A., Kobayashi, T., Edamatsu, M., & Toyoshima, Y. Y. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.04.016 · Cited by 31 · see citing works
Lü, X., Heeley, D. H., Smillie, L. B., & Kawai, M. (2010) · Journal of Muscle Research and Cell Motility · doi:10.1007/s10974-010-9213-x · Cited by 30 · see citing works
Snoberger, A., Brettrager, E. J., & Smith, D. M. (2018) · Nature Communications · doi:10.1038/s41467-018-04731-6 · Cited by 30 · see citing works
Zheng, W. (2012) · The Journal of Chemical Physics · doi:10.1063/1.4704661 · Cited by 29 · see citing works
Coupling of ATPase activity, microtubule binding, and mechanics in the dynein motor domain
Niekamp, S., Coudray, N., Zhang, N., Vale, R. D., & Bhabha, G. (2019) · The EMBO Journal · doi:10.15252/embj.2018101414 · Cited by 26 · see citing works
Kubo, S., Li, W., & Takada, S. (2017) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1005748 · Cited by 28 · see citing works
Structural biology of cytoplasmic and axonemal dyneins
Ishikawa, T. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2012.05.016 · Cited by 28 · see citing works
Mechanical Response and Conformational Amplification in α-Helical Coiled Coils
Yogurtcu, O. N., Wolgemuth, C. W., & Sun, S. X. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.10.002 · Cited by 28 · see citing works
Ecklund, K. H., Morisaki, T., Lammers, L. G., Marzo, M. G., Stasevich, T. J., & Markus, S. M. (2017) · Nature Communications · doi:10.1038/s41467-017-02004-2 · Cited by 27 · see citing works
Toda, A., Nishikawa, Y., Tanaka, H., Yagi, T., & Kurisu, G. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011541 · Cited by 26 · see citing works
Molecular organization and force‐generating mechanism of dynein
Sakakibara, H., & Oiwa, K. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08253.x · Cited by 26 · see citing works
Structural resolution of switchable states of a de novo peptide assembly
Dawson, W., Lang, E. J. M., Rhys, G. G., Shelley, K. L., Williams, C., Brady, R. L., Crump, M. P., Mulholland, A. J., & Woolfson, D. N. (2021) · Nature Communications · doi:10.1038/s41467-021-21851-8 · Cited by 25 · see citing works
Coiled-Coil Helix Rotation Selects Repressing or Activating State of Transcriptional Regulator DhaR
Shi, R., McDonald, L., Cygler, M., & Ekiel, I. H. (2014) · Structure · doi:10.1016/j.str.2013.11.012 · Cited by 25 · see citing works
Selbstorganisation von Coiled‐Coils in der synthetischen Biologie: Inspiration und Fortschritt
Marsden, H. R., & Kros, A. (2010) · Angewandte Chemie · doi:10.1002/ange.200904943 · Cited by 24 · see citing works
Nishikawa, Y., Inatomi, M., Iwasaki, H., & Kurisu, G. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.11.008 · Cited by 23 · see citing works
Live cell imaging of dynamic behaviors of motile cilia and primary cilium
Ijaz, F., & Ikegami, K. (2018) · Microscopy · doi:10.1093/jmicro/dfy147 · Cited by 21 · see citing works
Force-Generating Mechanism of Axonemal Dynein in Solo and Ensemble
Ishibashi, K., Sakakibara, H., & Oiwa, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21082843 · Cited by 22 · see citing works
The regulatory function of the AAA4 ATPase domain of cytoplasmic dynein
Liu, X., Rao, L., & Gennerich, A. (2020) · Nature Communications · doi:10.1038/s41467-020-19477-3 · Cited by 22 · see citing works
Dynein motors: How AAA+ ring opening and closing coordinates microtubule binding and linker movement
Schmidt, H. (2015) · BioEssays · doi:10.1002/bies.201400215 · Cited by 22 · see citing works
Cui, H., Ali, M. Y., Goyal, P., Zhang, K.-Q., Loh, J., Trybus, K., & Solmaz, S. (2020) · Traffic : the International Journal of Intracellular Transport · doi:10.1111/tra.12734 · Cited by 21 · see citing works
Structure of the Microtubule-Binding Domain of Flagellar Dynein
Kato, Y., Yagi, T., Harris, S. A., Ohki, S., Yura, K., Shimizu, Y., Honda, S., Kamiya, R., Burgess, S. A., & Tanokura, M. (2014) · Structure · doi:10.1016/j.str.2014.08.021 · Cited by 21 · see citing works
Self-citationThe Winch Model Can Explain both Coordinated and Uncoordinated Stepping of Cytoplasmic Dynein
Šarlah, A., & Vilfan, A. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.06.022 · Cited by 20 · see citing works
Ton, W. D., Wang, Y., Chai, P., Beauchamp-Perez, C. C., Flint, N. T., Lammers, L. G., Xiong, H., Zhang, K., & Markus, S. M. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01010-x · Cited by 19 · see citing works
Dynamics of Allosteric Transitions in Dynein
Goldtzvik, Y., Mugnai, M. L., & Thirumalai, D. (2018) · Structure · doi:10.1016/j.str.2018.08.005 · Cited by 18 · see citing works
An account of a century of ATP research
Nath, S. (2025) · Biosystems · doi:10.1016/j.biosystems.2025.105527 · Cited by 17 · see citing works
Three-color single-molecule imaging reveals conformational dynamics of dynein undergoing motility
Niekamp, S., Stuurman, N., Zhang, N., & Vale, R. D. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2101391118 · Cited by 17 · see citing works
Anurag, M., Singh, G., & Dash, D. (2012) · Molecular Biosystems · doi:10.1039/c1mb05210a · Cited by 17 · see citing works
Slow Axonemal Dynein e Facilitates the Motility of Faster Dynein c
Shimizu, Y., Sakakibara, H., Kojima, H., & Oiwa, K. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.04.009 · Cited by 17 · see citing works
Small stepping motion of processive dynein revealed by load-free high-speed single-particle tracking
Ando, J., Shima, T., Kanazawa, R., Shimo‐Kon, R., Nakamura, A., Yamamoto, M., Kon, T., & Iino, R. (2020) · Scientific Reports · doi:10.1038/s41598-020-58070-y · Cited by 17 · see citing works
Self-citationA unique role of dynein and nud family proteins in corticogenesis
Toba, S., & Hirotsune, S. (2012) · Neuropathology · doi:10.1111/j.1440-1789.2012.01301.x · Cited by 17 · see citing works
Protein Diffusion Along Protein and DNA Lattices: Role of Electrostatics and Disordered Regions
Bigman, L. S., & Levy, Y. (2023) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-111622-091220 · Cited by 16 · see citing works
The Generation of Dynein Networks by Multi-Layered Regulation and Their Implication in Cell Division
Torisawa, T., & Kimura, A. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00022 · Cited by 16 · see citing works
Eukaryote-Conserved Methylarginine Is Absent in Diplomonads and Functionally Compensated inGiardia
Emery‐Corbin, S. J., Hamey, J. J., Ansell, B. R. E., Balan, B., Tichkule, S., Stroehlein, A. J., Cooper, C., McInerney, B. V., Hediyeh-zadeh, S., Vuong, D., et al. (2020) · Molecular Biology and Evolution · doi:10.1093/molbev/msaa186 · Cited by 14 · see citing works
Structure and Function of Dynein’s Non-Catalytic Subunits
Rao, L., & Gennerich, A. (2024) · Cells · doi:10.3390/cells13040330 · Cited by 13 · see citing works
Rafiei, A., Tetlalmatzi, S. C., Edrington, C. H., Lee, L., Crowder, D. A., Saltzberg, D. J., Šali, A., Brouhard, G. J., & Schriemer, D. C. (2022) · eLife · doi:10.7554/elife.66975 · Cited by 13 · see citing works
Combining Structure–Function and Single-Molecule Studies on Cytoplasmic Dynein
Rao, L., Hülsemann, M., & Gennerich, A. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7271-5_4 · Cited by 12 · see citing works
Sliding Mechanism at a Coiled-Coil Interface.
Gomez, D., Gavrilov, Y., & Levy, Y. (2019) · Biophysical Journal · doi:10.1016/j.bpj.2019.02.026 · Cited by 8 · see citing works
Protein Engineering Approaches to Study the Dynein Mechanism using a Dictyostelium Expression System
Kon, T., Shima, T., & Sutoh, K. (2009) · Methods in cell biology · doi:10.1016/s0091-679x(08)92005-7 · Cited by 12 · see citing works
Self-citationA Low Affinity Ground State Conformation for the Dynein Microtubule Binding Domain
McNaughton, L., Tikhonenko, I., Banavali, N. K., LeMaster, D. M., & Koonce, M. P. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.083535 · Cited by 12 · see citing works
- Authors
- Kon, T., Imamula, K., Roberts, A. J., Ohkura, R., Knight, P. J., Gibbons, I. R., Burgess, S. A., & Sutoh, K.
- Affiliations
- The University of Tokyo (JP)
- University of Leeds (GB)
- University of California, Berkeley (US)
- Corresponding author
- Sutoh, Kazuo
- Venue
- Nature Structural & Molecular Biology
- Published
- 2009-02-08
- Volume
- 16
- Issue
- 3
- Pages
- 325-333
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- PMC
- PMC2757048
- OpenAlex
- W2120325459
- Cited by
- 169
- References
- 48
- Citations by year
- 2026: 5 · 2025: 3 · 2024: 7 · 2023: 8 · 2022: 7 · 2021: 5 · 2020: 13 · 2019: 12 · 2018: 9 · 2017: 12 · 2016: 7 · 2015: 10 · 2014: 15 · 2013: 7 · 2012: 15
- FWCI
- 7.27
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Structural & Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Wellcome Trust
- Biotechnology and Biological Sciences Research Council (BB/E00928X/1)
- National Institute of General Medical Sciences (R01GM030401, GM30401, R37GM030401)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- dynein, ATPase activity, microtubule binding, mechanochemical cycle, molecular motors, disulfide cross-linking, cysteine oxidation
- MeSH terms
- Adenosine Triphosphatases, Amino Acid Sequence, Animals, Binding Sites, Dictyostelium, Dyneins, Locomotion, Microtubules, Models, Molecular, Molecular Sequence Data, Protein Binding, Protozoan Proteins, Protein Structure, Secondary
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
