The myosin swinging cross-bridge model

Nature Reviews Molecular Cell Biology

Volumn 2, Issue 5, 2001, Pages 387-392

  Spudich, James A ^a  

^a STANFORD UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CROSS LINKING REAGENT; MOLECULAR MOTOR; MYOSIN;

CHEMICAL STRUCTURE; CHEMISTRY; PHYSIOLOGY; REVIEW;

CROSS-LINKING REAGENTS; MODELS, MOLECULAR; MOLECULAR MOTOR PROTEINS; MYOSINS;

EID: 0035344213     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/35073086     Document Type: Review

References (47)

1. Huxley, H. E. The mechanism of muscular contraction. Science 164, 1356-1365 (1969).
2. Huxley, A. F. & Simmons, R. M. Proposed mechanism of force generation in striated muscle. Nature 233, 533-538 (1971).
3. Moore, P. B., Huxley, H. E. & de Rosier, D. J. Three-dimensional reconstruction of F-actin, thin filaments and decorated thin filaments. J. Mol. Biol. 50, 279-295 (1970).
4. Lymn, R. W. & Taylor, E. W. Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry 10, 4617-4624 (1971).
5. Yount, R. G., Ojala, D. & Babcock, D. Interaction of P-N-P and P-C-P analogs of adenosine triphosphate with heavy meromyosin, myosin, and actomyosin. Biochemistry 10, 2490-2496 (1971).
6. Goody, R. S. & Eckstein, F. Thiophosphate analogs of nucleoside di-and triphosphates. J. Am. Chem. Soc. 93, 6252-6257 (1971).
7. Goody, R. S. & Hofmann, W. Stereochemical aspects of the interaction of myosin and actomyosin with nucleotides. J. Muscle Res. Cell Motil. 1, 101-115 (1980).
8. Pollard, T. D. & Korn, E. D. Acanthamoeba myosin. I. Isolation from Acanthamoeba castellanii of an enzyme similar to muscle myosin. J. Biol. Chem. 248, 4682-4690 (1973).
9. Huxley, H. E. et al. Time-resolved X-ray diffraction studies of the myosin layer-line reflections during muscle contraction. J. Mol. Biol. 158, 637-84 (1982).
10. Sheetz, M. P. & Spudich, J. A. Movement of myosin-coated fluorescent beads on actin cables in vitro. Nature 303, 31-35 (1983).
11. Vale, R. D., Reese, T. S. & Sheetz, M. P. Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility. Cell 42, 39-50 (1985).
12. Kron, S. J. & Spudich, J. A. Fluorescent actin filaments move on myosin fixed to a glass surface. Proc. Natl Acad. Sci. USA 83, 6272-6276 (1986).
13. Rice, S. et al. A structural change in the kinesin motor protein that drives motility. Nature 402, 778-784 (1999).
14. Vale, R. D. & Milligan, R. A. The way things move: looking under the hood of molecular motor proteins. Science 288, 88-95 (2000).
15. Goldstein, L. S. & Philp, A. V. The road less traveled: emerging principles of kinesin motor utilization. Annu. Rev. Cell. Dev. Biol. 15, 141-83 (1999).
16. Toyoshima, Y. Y. et al. Myosin subfragment-1 is sufficient to move actin filaments in vitro. Nature 328, 536-539 (1987).
17. Kabsch, W. et al. Atomic structure of the actin:DNase 1 complex. Nature 347, 37-44 (1990).
18. Rayment, I. et al. Three-dimensional structure of myosin subfragment-1: a molecular motor. Science 261, 50-58 (1993).
19. Dominguez, R. et al. Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: visualization of the pre-power stroke state. Cell 94, 559-571 (1998).
20. Houdusse, A., Szent-Gyorgyi, A. G. & Cohen, C. Three conformational states of scallop myosin S1. Proc. Natl Acad. Sci. USA 97, 11238-11243 (2000).
21. Smith, C. A. & Rayment, I. X-ray structure of the magnesium (II) ADP. vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Å resolution. Biochemistry 35, 5404-5417 (1996).
22. Rayment, I. et al. Structure of the actin-myosin complex and its implications for muscle contraction. Science 261, 58-65 (1993).
23. Schröder, R. R. et al. Three-dimensional atomic model of F-actin decorated with Dictyostelium myosin S1. Nature 364, 171-174 (1993).
24. Jontes, J. D., Wilson-Kubalek, E. M. & Milligan, R. A. A 32 degree tail swing in brush border myosin I on ADP release. Nature 378, 751-753 (1995).
25. Whittaker, M. et al. A 35-Å movement of smooth muscle myosin on ADP release. Nature 387, 748-751 (1995).
26. Cooke, R., Crowder, M. S. 4 Thomas, D. D. Orientation of spin labels attached to cross-bridges in contracting muscle fibres. Nature 300, 776-778 (1982).
27. Cooke, R. The mechanism of muscle contraction. CRC Crit. Rev. Biochem. 21, 53-118 (1986).
28. Shih, W. M. et al. A FRET-based sensor reveals large ATP hydrolysis-induced conformational changes and three distinct states of the molecular motor myosin. Cell 102, 683-694 (2000).
29. Yanagida, T., Arata, T. & Oosawa, F. Sliding distance of actin filament induced by a myosin crossbridge during one ATP hydrolysis cycle. Nature 316, 366-369 (1985).
30. Harada, Y. et al. Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay. J. Mol. Biol. 216, 49-68 (1990).
31. Finer, J. T., Simmons, R. M. & Spudich, J. A. Single myosin molecule mechanics: piconewton forces and nanometre steps. Nature 368, 113-119 (1994).
32. Yanagida, T. & Iwane, A. H. A large step for myosin. Proc. Natl Acad. Sci. USA 97, 9357-9359 (2000).
33. Ruppel, K. M. & Spudich, J. A. Structure-function analysis of the motor domain of myosin. Annu. Rev. Cell Dev. Biol. 12, 543-73 (1996).
34. Mercer, J. A., et al. Novel myosin heavy chain encoded by murine dilute coat colour locus. Nature 349, 709-713 (1991).
35. Cheney, R. E. et al. Brain myosin-V is a two-headed unconventional myosin with motor activity. Cell 75, 13-23 (1993).
36. Mehta, A. D. et al. Myosin-V is a processive actin-based motor. Nature 400, 590-593 (1999).
37. Rief, M. et al. Myosin-V stepping kinetics: a molecular model for processivity. Proc. Natl Acad. Sci. USA 97, 9482-9486 (2000).
38. Sakamoto, T. et al. Direct observation of processive movement by individual myosin V molecules. Biochem. Biophys. Res. Commun. 272, 586-590 (2000).
39. Walker, M. L. et al. Two-headed binding of a processive myosin to F-actin. Nature 405, 804-807 (2000).
40. De La Cruz, E. M. et al. The kinetic mechanism of myosin V. Proc. Natl Acad. Sci. USA 96, 13726-13731 (1999).
41. De La Cruz, E. M., Sweeney, H. L. & Ostap, E. M. ADP inhibition of Myosin V ATPase Activity. Biophys. J. 79, 1524-1429 (2000).
42. Trybus, K. M., Krementsova, E. & Freyzon, Y. Kinetic characterization of a monomeric unconventional myosin V construct. J. Biol. Chem. 274, 27448-27456 (1999).
43. Wang, F. et al. Effect of ADP and ionic strength on the kinetic and motile properties of recombinant mouse myosin V. J. Biol. Chem. 275, 4329-4335 (2000).
44. Holmes, K. C. et al. Atomic model of the actin filament. Nature 347, 44-49 (1990).
45. Lorenz, M., Popp, D. & Holmes, K. C. Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 234, 826-836 (1993).
46. Funatsu, T. et al. Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution. Nature 374, 555-559 (1995).
47. Visscher, K., Schnitzer, M. J. & Block, S. M. Single kinesin molecules studied with a molecular force clamp. Nature 400, 184-189 (1999).