The kinetic mechanism of kinesin

Trends in Biochemical Sciences

Volumn 29, Issue 6, 2004, Pages 301-309

  Cross, Robert A ^a  

^a MARIE CURIE RESEARCH INSTITUTE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE MAGNESIUM; APYRASE; EDETIC ACID; GLYCINE; KINESIN; OXYGEN; PHOSPHATE; SERINE;

BINDING AFFINITY; DISSOCIATION; GEL FILTRATION; HYDROLYSIS; KINETICS; MICROTUBULE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN PROTEIN INTERACTION; PROTEIN SECRETION; REVIEW; WILD TYPE;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ANIMALS; HUMANS; HYDROLYSIS; KINESIN; KINETICS; MICROTUBULES; MODELS, MOLECULAR; PHOSPHATES;

EID: 3242776257     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2004.04.010     Document Type: Review

References (78)

1. Bloom G.S., Endow S.A. Motor proteins 1: kinesins. Protein Profile. 2:1995;1105-1171
2. Crevel I., et al. What kinesin does at roadblocks: the coordination mechanism for molecular walking. EMBO J. 23:2004;23-32
3. Geeves M.A. The dynamics of actin and myosin association and the crossbridge model of muscle contraction. Biochem. J. 274:1991;1-14
4. Hackney D.D. Kinesin ATPase: rate-limiting ADP release. Proc. Natl. Acad. Sci. U. S. A. 85:1988;6314-6318
5. Ma Y.Z., Taylor E.W. Kinetic mechanism of a monomeric kinesin construct. J. Biol. Chem. 272:1997;717-723
6. Pechatnikova E., Taylor E.W. Kinetic mechanism of monomeric non-claret disjunctional protein (Ncd) ATPase. J. Biol. Chem. 272:1997;30735-30740
7. Foster K.A., et al. Equilibrium binding studies of non-claret disjunctional protein (Ncd) reveal cooperative interactions between the motor domains. J. Biol. Chem. 273:1998;35307-35318
8. Foster K.A., et al. A mechanistic model for Ncd directionality. J. Biol. Chem. 276:2001;19259-19266
9. Gilbert S.P., Johnson K.A. Pre-steady-state kinetics of the microtubule-kinesin ATPase. Biochemistry. 33:1994;1951-1960
10. Ma Y.Z., Taylor E.W. Interacting head mechanism of microtubule-kinesin ATPase. J. Biol. Chem. 272:1997;724-730
11. Saxton W.M., et al. Drosophila kinesin: characterization of microtubule motility and ATPase. Proc. Natl. Acad. Sci. U. S. A. 85:1988;1109-1113
12. Hua W., et al. Coupling of kinesin steps to ATP hydrolysis. Nature. 388:1997;390-393
13. Schnitzer M.J., Block S.M. Kinesin hydrolyses one ATP per 8-nm step. Nature. 388:1997;386-390
14. Kaseda K., et al. Alternate fast and slow stepping of a heterodimeric kinesin molecule. Nat. Cell Biol. 5:2003;1079-1082
15. Jiang W., et al. Influence of the kinesin neck domain on dimerization and ATPase kinetics. J. Biol. Chem. 272:1997;7626-7632
16. Hancock W.O., Howard J. Kinesin's processivity results from mechanical and chemical coordination between the ATP hydrolysis cycles of the two motor domains. Proc. Natl. Acad. Sci. U. S. A. 96:1999;13147-13152
17. Ma Y.Z., Taylor E.W. Kinetic mechanism of kinesin motor domain. Biochemistry. 34:1995;13233-13241
18. Cohn S.A., et al. Quantitative analysis of sea urchin egg kinesin-driven microtubule motility. J. Biol. Chem. 264:1989;4290-4297
19. Geeves M.A., et al. Kinetics of acto-S1 interaction as a guide to a model for the crossbridge cycle. J. Muscle Res. Cell Motil. 5:1984;351-361
20. Suzuki Y., et al. Hydrolysis of AMPPNP by the motor domain of Ncd, a kinesin-related protein. FEBS Lett. 409:1997;29-32
21. Crevel I.M., et al. Weak and strong states of kinesin and Ncd. J. Mol. Biol. 257:1996;66-76
22. Yajima J., et al. Direct long-term observation of kinesin processivity at low load. Curr. Biol. 12:2002;301-306
23. Shimizu T., et al. Nucleotide specificity of the enzymatic and motile activities of dynein, kinesin, and heavy meromyosin. J. Cell Biol. 112:1991;1189-1197
24. Romberg L., Vale R.D. Chemomechanical cycle of kinesin differs from that of myosin. Nature. 361:1993;168-170
25. Kull F.J., Endow S.A. Kinesin: switch I & II and the motor mechanism. J. Cell Sci. 115:2002;15-23
26. Rice S., et al. A structural change in the kinesin motor protein that drives motility. Nature. 402:1999;778-784
27. Farrell C.M., et al. The role of ATP hydrolysis for kinesin processivity. J. Biol. Chem. 277:2002;17079-17087
28. Klumpp L.M., et al. A kinesin switch I arginine to lysine mutation rescues microtubule function. J. Biol. Chem. 278:2003;39059-39067
29. Schief W.R., Howard J. Conformational changes during kinesin motility. Curr. Opin. Cell Biol. 13:2001;19-28
30. Kovacs M., et al. Analysis of nucleotide binding to Dictyostelium myosin II motor domains containing a single tryptophan near the active site. J. Biol. Chem. 277:2002;28459-28467
31. Alonso M.C., et al. Proteolytic mapping of kinesin/Ncd-microtubule interface: nucleotide-dependent conformational changes in the loops L8 and L12. EMBO J. 17:1998;945-951
32. Xing J., et al. Kinesin has three nucleotide-dependent conformations. Implications for strain-dependent release. J. Biol. Chem. 275:2000;35413-35423
33. Kikkawa M., et al. Switch-based mechanism of kinesin motors. Nature. 411:2001;439-445
34. Amos L.A., Cross R.A. Structure and dynamics of molecular motors. Curr. Opin. Struct. Biol. 7:1997;239-246
35. Reubold T.F., et al. A structural model for actin-induced nucleotide release in myosin. Nat. Struct. Biol. 10:2003;826-830
36. Hackney D.D. Pathway of ADP-stimulated ADP release and dissociation of tethered kinesin from microtubules. Implications for the extent of processivity. Biochemistry. 41:2002;4437-4446
37. Gilbert S.P., et al. Pathway of processive ATP hydrolysis by kinesin. Nature. 373:1995;671-676
38. Klumpp L.M., et al. Kinesin's second step. Proc. Natl. Acad. Sci. U. S. A. 101:2004;3444-3449
39. Rosenfeld S.S., et al. Equilibrium studies of kinesin-nucleotide intermediates. J. Biol. Chem. 271:1996;9473-9482
40. Schief W.R., et al. Inhibition of kinesin motility by ADP and phosphate supports a hand-over-hand mechanism. Proc. Natl. Acad. Sci. U. S. A. 101:2004;1183-1188
41. Hackney D.D. Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis. Proc. Natl. Acad. Sci. U. S. A. 91:1994;6865-6869
42. Sadhu A., Taylor E.W. A kinetic study of the kinesin ATPase. J. Biol. Chem. 267:1992;11352-11359
43. Lockhart A., Cross R.A. Origins of reversed directionality in the Ncd molecular motor. EMBO J. 13:1994;751-757
44. Gilbert S.P., et al. Alternating site mechanism of the kinesin ATPase. Biochemistry. 37:1998;792-799
45. Crevel I., et al. Coupled chemical and mechanical reaction steps in a processive Neurospora kinesin. EMBO J. 18:1999;5863-5872
46. Lockhart A., et al. ADP release is the rate-limiting step of the MT activated ATPase of non-claret disjunctional and kinesin. FEBS Lett. 368:1995;531-535
47. Ma Y.Z., Taylor E.W. Mechanism of microtubule kinesin ATPase. Biochemistry. 34:1995;13242-13251
48. Cheng J.Q., et al. Interaction of mant-adenosine nucleotides and magnesium with kinesin. Biochemistry. 37:1998;5288-5295
49. Okada Y., Hirokawa N. Mechanism of the single-headed processivity: diffusional anchoring between the K-loop of kinesin and the C terminus of tubulin. Proc. Natl. Acad. Sci. U. S. A. 97:2000;640-645
50. Rogers K.R., et al. KIF1D is a fast non-processive kinesin that demonstrates novel K-loop-dependent mechanochemistry. EMBO J. 20:2001;5101-5113
51. Rosenfeld S.S., et al. ATP reorients the neck linker of kinesin in two sequential steps. J. Biol. Chem. 276:2001;40167-40174
52. Foster K.A., Gilbert S.P. Kinetic studies of dimeric Ncd: evidence that Ncd is not processive. Biochemistry. 39:2000;1784-1791
53. Lockhart A., Cross R.A. Kinetics and motility of the Eg5 microtubule motor. Biochemistry. 35:1996;2365-2373
54. Crevel I.M., et al. Kinetic evidence for low chemical processivity in Ncd and Eg5. J. Mol. Biol. 273:1997;160-170
55. deCastro M.J., et al. Motility of dimeric Ncd on a metal-chelating surfactant: evidence that Ncd is not processive. Biochemistry. 38:1999;5076-5081
56. Naber N., et al. Closing of the nucleotide pocket of kinesin-family motors upon binding to microtubules. Science. 300:2003;798-801
57. Okada Y., et al. Processivity of the single-headed kinesin KIF1A through biased binding to tubulin. Nature. 424:2003;574-577
58. Jiang W., Hackney D.D. Monomeric kinesin head domains hydrolyze multiple ATP molecules before release from a microtubule. J. Biol. Chem. 272:1997;5616-5621
59. Moyer M.L., et al. Pathway of ATP hydrolysis by monomeric and dimeric kinesin. Biochemistry. 37:1998;800-813
60. Vugmeyster Y., et al. Release of isolated single kinesin molecules from microtubules. Biochemistry. 37:1998;747-757
61. Hancock W.O., Howard J. Processivity of the motor protein kinesin requires two heads. J. Cell Biol. 140:1998;1395-1405
62. Hirose K., et al. Nucleotide-dependent structural changes in dimeric NCD molecules complexed to microtubules. J. Mol. Biol. 278:1998;389-400
63. Coy D.L., et al. Kinesin takes one 8-nm step for each ATP that it hydrolyzes. J. Biol. Chem. 274:1999;3667-3671
64. Nishiyama M., et al. Chemomechanical coupling of the forward and backward steps of single kinesin molecules. Nat. Cell Biol. 4:2002;790-797
65. Asbury C.L., et al. Kinesin moves by an asymmetric hand-over-hand mechanism. Science. 302:2003;2130-2134
66. Rice S., et al. Thermodynamic properties of the kinesin neck-region docking to the catalytic core. Biophys. J. 84:2003;1844-1854
67. Skiniotis G., et al. Nucleotide-induced conformations in the neck region of dimeric kinesin. EMBO J. 22:2003;1518-1528
68. Hackney D.D., et al. Modulation of kinesin half-site ADP release and kinetic processivity by a spacer between the head groups. Biochemistry. 42:2003;12011-12018
69. Svoboda K., Block S.M. Force and velocity measured for single kinesin molecules. Cell. 77:1994;773-784
70. Schnitzer M.J., et al. Force production by single kinesin motors. Nat. Cell Biol. 2:2000;718-723
71. Rosenfeld S.S., et al. Stepping and stretching. How kinesin uses internal strain to walk processively. J. Biol. Chem. 278:2003;18550-18556
72. Uemura S., Ishiwata S. Loading direction regulates the affinity of ADP for kinesin. Nat. Struct. Biol. 10:2003;308-311
73. Walczak C.E. The Kin I kinesins are microtubule end-stimulated ATPases. Mol. Cell. 11:2003;286-288
74. Howard J. Mechanics of Motor Proteins and the Cytoskeleton. 2001;Sinauer Associates
75. Cross R.A., et al. The conformational cycle of kinesin. Philos. Trans. R. Soc. London Ser. B. 355:2000;459-464
76. Hackney D.D. Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains. Nature. 377:1995;448-450
77. Case R.B., et al. Role of the kinesin neck linker and catalytic core in microtubule-based motility. Curr. Biol. 10:2000;157-160
78. Tomishige M., Vale R.D. Controlling kinesin by reversible disulfide cross-linking. Identifying the motility-producing conformational change. J. Cell Biol. 151:2000;1081-1092