메뉴 건너뛰기




Volumn 1767, Issue 12, 2007, Pages 1418-1427

Processivity of single-headed kinesin motors

Author keywords

Kinesin; Mechanochemistry; Microtubule; Molecular motor; Processivity

Indexed keywords

ADENOSINE DIPHOSPHATE; KINESIN; MOLECULAR MOTOR;

EID: 36549042972     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2007.09.006     Document Type: Article
Times cited : (17)

References (66)
  • 1
    • 0029960345 scopus 로고    scopus 로고
    • The movement of kinesin along microtubules
    • Howard J. The movement of kinesin along microtubules. Annu. Rev. Physiol. 58 (1996) 703-729
    • (1996) Annu. Rev. Physiol. , vol.58 , pp. 703-729
    • Howard, J.1
  • 2
    • 0032559260 scopus 로고    scopus 로고
    • Kinesin and dynein superfamily proteins and the mechanism of organelle transport
    • Hirokawa N. Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science 279 (1998) 519-526
    • (1998) Science , vol.279 , pp. 519-526
    • Hirokawa, N.1
  • 3
    • 0037459061 scopus 로고    scopus 로고
    • The molecular motor toolbox for intracellular transport
    • Vale R.D. The molecular motor toolbox for intracellular transport. Cell 112 (2003) 467-480
    • (2003) Cell , vol.112 , pp. 467-480
    • Vale, R.D.1
  • 4
    • 0024463944 scopus 로고
    • Movement of microtubules by single kinesin molecules
    • Howard J., Hudspeth A.J., and Vale R.D. Movement of microtubules by single kinesin molecules. Nature 342 (1989) 154-158
    • (1989) Nature , vol.342 , pp. 154-158
    • Howard, J.1    Hudspeth, A.J.2    Vale, R.D.3
  • 5
    • 0025222347 scopus 로고
    • Bead movement by single kinesin molecules studied with optical tweezers
    • Block S.M., Goldstein L.S., and Schnapp B.J. Bead movement by single kinesin molecules studied with optical tweezers. Nature 348 (1990) 348-352
    • (1990) Nature , vol.348 , pp. 348-352
    • Block, S.M.1    Goldstein, L.S.2    Schnapp, B.J.3
  • 6
    • 0027453868 scopus 로고
    • Direct observation of kinesin stepping by optical trapping interferometry
    • Svoboda K., Schmidt C.F., Schnapp B.J., and Block S.M. Direct observation of kinesin stepping by optical trapping interferometry. Nature 365 (1993) 721-727
    • (1993) Nature , vol.365 , pp. 721-727
    • Svoboda, K.1    Schmidt, C.F.2    Schnapp, B.J.3    Block, S.M.4
  • 7
    • 0029156511 scopus 로고
    • Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains
    • Hackney D.D. Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains. Nature 377 (1995) 448-450
    • (1995) Nature , vol.377 , pp. 448-450
    • Hackney, D.D.1
  • 8
    • 0029879228 scopus 로고    scopus 로고
    • Direct observation of single kinesin molecules moving along microtubules
    • Vale R.D., Funatsu T., Pierce D.W., Romberg L., Harada Y., and Yanagida T. Direct observation of single kinesin molecules moving along microtubules. Nature 380 (1996) 451-453
    • (1996) Nature , vol.380 , pp. 451-453
    • Vale, R.D.1    Funatsu, T.2    Pierce, D.W.3    Romberg, L.4    Harada, Y.5    Yanagida, T.6
  • 9
    • 0033582814 scopus 로고    scopus 로고
    • A processive single-headed motor: kinesin superfamily protein KIF1A
    • Okada Y., and Hirokawa N. A processive single-headed motor: kinesin superfamily protein KIF1A. Science 283 (1999) 1152-1157
    • (1999) Science , vol.283 , pp. 1152-1157
    • Okada, Y.1    Hirokawa, N.2
  • 10
    • 0034681137 scopus 로고    scopus 로고
    • Mechanism of the single-headed processivity: diffusional anchoring between the K-loop of kinesin and the C terminus of tubulin
    • Okada Y., and 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
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 640-645
    • Okada, Y.1    Hirokawa, N.2
  • 12
    • 0030844286 scopus 로고    scopus 로고
    • Coupling of kinesin steps to ATP hydrolysis
    • Hua W., Young E.C., Fleming M.L., and Gelles J. Coupling of kinesin steps to ATP hydrolysis. Nature 388 (1997) 390-393
    • (1997) Nature , vol.388 , pp. 390-393
    • Hua, W.1    Young, E.C.2    Fleming, M.L.3    Gelles, J.4
  • 13
    • 0033536183 scopus 로고    scopus 로고
    • Single kinesin molecules studied with a molecular force clamp
    • Visscher K., Schnitzer M.J., and Block S.M. Single kinesin molecules studied with a molecular force clamp. Nature 400 (1999) 184-189
    • (1999) Nature , vol.400 , pp. 184-189
    • Visscher, K.1    Schnitzer, M.J.2    Block, S.M.3
  • 14
    • 0030744142 scopus 로고    scopus 로고
    • Kinesin hydrolyzes one ATP per 8-nm step
    • Schnitzer M.J., and Block S.M. Kinesin hydrolyzes one ATP per 8-nm step. Nature 388 (1997) 386-390
    • (1997) Nature , vol.388 , pp. 386-390
    • Schnitzer, M.J.1    Block, S.M.2
  • 15
    • 0030824684 scopus 로고    scopus 로고
    • Mechanics of single kinesin molecules measured by optical trapping nanometry
    • Kojima H., Muto E., Higuchi H., and Yanagida T. Mechanics of single kinesin molecules measured by optical trapping nanometry. Biophys. J. 73 (1997) 2012-2022
    • (1997) Biophys. J. , vol.73 , pp. 2012-2022
    • Kojima, H.1    Muto, E.2    Higuchi, H.3    Yanagida, T.4
  • 17
    • 0036798857 scopus 로고    scopus 로고
    • Chemomechanical coupling of the ATPase cycle to the forward and backward movements of single kinesin molecules
    • Nishiyama M., Higuchi H., and Yanagida T. Chemomechanical coupling of the ATPase cycle to the forward and backward movements of single kinesin molecules. Nat. Cell Biol. 4 (2002) 790-797
    • (2002) Nat. Cell Biol. , vol.4 , pp. 790-797
    • Nishiyama, M.1    Higuchi, H.2    Yanagida, T.3
  • 18
    • 0037390461 scopus 로고    scopus 로고
    • Loading direction regulates the affinity of ADP for kinesin
    • Uemura S., and Ishiwata S. Loading direction regulates the affinity of ADP for kinesin. Nat. Struct. Biol. 4 (2003) 308-311
    • (2003) Nat. Struct. Biol. , vol.4 , pp. 308-311
    • Uemura, S.1    Ishiwata, S.2
  • 20
    • 0347623370 scopus 로고    scopus 로고
    • Kinesin moves by an asymmetric hand-over-hand mechanism
    • Asbury C.L., Fehr A.N., and Block S.M. Kinesin moves by an asymmetric hand-over-hand mechanism. Science 302 (2003) 2130-2134
    • (2003) Science , vol.302 , pp. 2130-2134
    • Asbury, C.L.1    Fehr, A.N.2    Block, S.M.3
  • 21
    • 0345257160 scopus 로고    scopus 로고
    • Alternate fast and slow stepping of a heterodimeric kinesin molecule
    • Kaseda K., Higuchi H., and Horose K. Alternate fast and slow stepping of a heterodimeric kinesin molecule. Nat. Cell Biol. 5 (2003) 1079-1082
    • (2003) Nat. Cell Biol. , vol.5 , pp. 1079-1082
    • Kaseda, K.1    Higuchi, H.2    Horose, K.3
  • 22
    • 4143146576 scopus 로고    scopus 로고
    • Rapid double 8-nm steps by a kinesin mutant
    • Higuchi H., Bronner C.E., Park H.W., and Endow S.A. Rapid double 8-nm steps by a kinesin mutant. EMBO J. 23 (2004) 2993-2999
    • (2004) EMBO J. , vol.23 , pp. 2993-2999
    • Higuchi, H.1    Bronner, C.E.2    Park, H.W.3    Endow, S.A.4
  • 23
    • 19644377414 scopus 로고    scopus 로고
    • Mechanics of the kinesin step
    • Carter N.J., and Cross R.A. Mechanics of the kinesin step. Nature 435 (2005) 308-312
    • (2005) Nature , vol.435 , pp. 308-312
    • Carter, N.J.1    Cross, R.A.2
  • 25
    • 0032559690 scopus 로고    scopus 로고
    • Leading the procession: new insights into kinesin motors
    • Block S.M. Leading the procession: new insights into kinesin motors. J. Cell Biol. 140 (1998) 1281-1284
    • (1998) J. Cell Biol. , vol.140 , pp. 1281-1284
    • Block, S.M.1
  • 26
    • 0031771084 scopus 로고    scopus 로고
    • The structural and mechanochemical cycle of kinesin
    • Mandelkow E., and Johnson K.A. The structural and mechanochemical cycle of kinesin. Trends Biochem. Sci. 23 (1998) 429-433
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 429-433
    • Mandelkow, E.1    Johnson, K.A.2
  • 27
    • 0032548489 scopus 로고    scopus 로고
    • Alternating site mechanism of the kinesin ATPase
    • Gilbert S.P., Moyer M.L., and Johnson K.A. Alternating site mechanism of the kinesin ATPase. Biochemistry 37 (1998) 792-799
    • (1998) Biochemistry , vol.37 , pp. 792-799
    • Gilbert, S.P.1    Moyer, M.L.2    Johnson, K.A.3
  • 28
    • 0033539520 scopus 로고    scopus 로고
    • Kinesin's processivity results from mechanical and chemical coordination between the ATP hydrolysis cycles of the two motor domains
    • Hancock W.O., and 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
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 13147-13152
    • Hancock, W.O.1    Howard, J.2
  • 29
    • 0343415156 scopus 로고    scopus 로고
    • The way things move: looking under the hood of molecular motor proteins
    • Vale R.D., and Milligan R.A. The way things move: looking under the hood of molecular motor proteins. Science 288 (2000) 88-95
    • (2000) Science , vol.288 , pp. 88-95
    • Vale, R.D.1    Milligan, R.A.2
  • 31
    • 0038380203 scopus 로고    scopus 로고
    • Processive and nonprocessive models of kinesin movement
    • Endow S.A., and Barker D.S. Processive and nonprocessive models of kinesin movement. Annu. Rev. Physiol. 65 (2003) 161-175
    • (2003) Annu. Rev. Physiol. , vol.65 , pp. 161-175
    • Endow, S.A.1    Barker, D.S.2
  • 32
    • 0038381479 scopus 로고    scopus 로고
    • Stepping and Stretching: how kinesin uses internal strain to walk processively
    • Rosenfeld S.S., Fordyce P.M., Jefferson G.M., King P.H., and Block S.M. Stepping and Stretching: how kinesin uses internal strain to walk processively. J. Biol. Chem. 278 (2003) 18550-18556
    • (2003) J. Biol. Chem. , vol.278 , pp. 18550-18556
    • Rosenfeld, S.S.1    Fordyce, P.M.2    Jefferson, G.M.3    King, P.H.4    Block, S.M.5
  • 33
    • 3242776257 scopus 로고    scopus 로고
    • The kinetic mechanism of kinesin
    • Cross R.A. The kinetic mechanism of kinesin. Trends Biochem. Sci. 29 (2004) 301-309
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 301-309
    • Cross, R.A.1
  • 36
    • 12344259551 scopus 로고    scopus 로고
    • Kinesin: world's tiniest biped
    • Asbury C.L. Kinesin: world's tiniest biped. Curr. Opin. Cell Biol. 17 (2005) 89-97
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 89-97
    • Asbury, C.L.1
  • 37
    • 13244273546 scopus 로고    scopus 로고
    • Kinesin: walking, crawling or sliding along?
    • Yildiz A., and Selvin P.R. Kinesin: walking, crawling or sliding along?. Trends Cell Biol. 15 (2005) 112-120
    • (2005) Trends Cell Biol. , vol.15 , pp. 112-120
    • Yildiz, A.1    Selvin, P.R.2
  • 38
    • 33644585049 scopus 로고    scopus 로고
    • Model for kinetics of wild-type and mutant kinesins
    • Xie P., Dou S.-X., and Wang P.-Y. Model for kinetics of wild-type and mutant kinesins. Biosystems 84 (2006) 24-38
    • (2006) Biosystems , vol.84 , pp. 24-38
    • Xie, P.1    Dou, S.-X.2    Wang, P.-Y.3
  • 39
    • 33746908180 scopus 로고    scopus 로고
    • Mechanochemical couplings of kinesin motors
    • Xie P., Dou S.-X., and Wang P.-Y. Mechanochemical couplings of kinesin motors. Biophys. Chemist. 123 (2006) 58-76
    • (2006) Biophys. Chemist. , vol.123 , pp. 58-76
    • Xie, P.1    Dou, S.-X.2    Wang, P.-Y.3
  • 40
    • 33846592701 scopus 로고    scopus 로고
    • Limping of homodimeric kinesin motors
    • Xie P., Dou S.-X., and Wang P.-Y. Limping of homodimeric kinesin motors. J. Mol. Biol. 366 (2007) 976-985
    • (2007) J. Mol. Biol. , vol.366 , pp. 976-985
    • Xie, P.1    Dou, S.-X.2    Wang, P.-Y.3
  • 42
    • 0041522803 scopus 로고    scopus 로고
    • Processivity of the single-headed kinesin KIF1A through biased binding to tubulin
    • Okada Y., Higuchi H., and Hirokawa N. Processivity of the single-headed kinesin KIF1A through biased binding to tubulin. Nature 424 (2003) 574-577
    • (2003) Nature , vol.424 , pp. 574-577
    • Okada, Y.1    Higuchi, H.2    Hirokawa, N.3
  • 44
    • 0034765827 scopus 로고    scopus 로고
    • Motility of one-headed kinesin molecules along microtubules
    • Inoue Y., Iwane A.H., Miyai T., Muto E., and Yanagida T. Motility of one-headed kinesin molecules along microtubules. Biophys. J. 81 (2001) 2838-2850
    • (2001) Biophys. J. , vol.81 , pp. 2838-2850
    • Inoue, Y.1    Iwane, A.H.2    Miyai, T.3    Muto, E.4    Yanagida, T.5
  • 45
    • 0028899953 scopus 로고
    • Failure of a single headed kinesin to track parallel to microtubule protofilaments
    • Berliner E., Young E.C., Anderson K., Mahtani H.K., and Gelles J. Failure of a single headed kinesin to track parallel to microtubule protofilaments. Nature 373 (1995) 718-721
    • (1995) Nature , vol.373 , pp. 718-721
    • Berliner, E.1    Young, E.C.2    Anderson, K.3    Mahtani, H.K.4    Gelles, J.5
  • 46
    • 0032502328 scopus 로고    scopus 로고
    • One-headed kinesin derivatives move by a nonprocessive, low-duty ratio mechanism unlike that of two-headed kinesin
    • Young E.C., Mahtani H.K., and Gelles J. One-headed kinesin derivatives move by a nonprocessive, low-duty ratio mechanism unlike that of two-headed kinesin. Biochemistry 37 (1998) 3467-3479
    • (1998) Biochemistry , vol.37 , pp. 3467-3479
    • Young, E.C.1    Mahtani, H.K.2    Gelles, J.3
  • 47
    • 0032559822 scopus 로고    scopus 로고
    • Processivity of the motor protein kinesin requires two heads
    • Hancock W.O., and Howard J. Processivity of the motor protein kinesin requires two heads. J. Cell Biol. 140 (1998) 1395-1405
    • (1998) J. Cell Biol. , vol.140 , pp. 1395-1405
    • Hancock, W.O.1    Howard, J.2
  • 48
    • 21244502629 scopus 로고    scopus 로고
    • Biased binding of single molecules and continuous movement of multiple molecules of truncated single-headed kinesin
    • Kamei T., Kakuta S., and Higuchi H. Biased binding of single molecules and continuous movement of multiple molecules of truncated single-headed kinesin. Biophys. J. 88 (2005) 2068-2077
    • (2005) Biophys. J. , vol.88 , pp. 2068-2077
    • Kamei, T.1    Kakuta, S.2    Higuchi, H.3
  • 49
    • 11744379062 scopus 로고
    • Fluctuation driven ratchets: molecular motors
    • Astumian R.D., and Bier M. Fluctuation driven ratchets: molecular motors. Phys. Rev. Lett. 72 (1994) 1766-1769
    • (1994) Phys. Rev. Lett. , vol.72 , pp. 1766-1769
    • Astumian, R.D.1    Bier, M.2
  • 51
    • 27144557983 scopus 로고    scopus 로고
    • Intracellular transport of single-headed molecular motors KIF1A
    • Nishinari K., Okada Y., Schadschneider A., and Chowdhury D. Intracellular transport of single-headed molecular motors KIF1A. Phys. Rev. Lett. 95 (2005) 118101-118104
    • (2005) Phys. Rev. Lett. , vol.95 , pp. 118101-118104
    • Nishinari, K.1    Okada, Y.2    Schadschneider, A.3    Chowdhury, D.4
  • 52
    • 0032548491 scopus 로고    scopus 로고
    • Pathway of ATP hydrolysis by monomeric and dimeric kinesin
    • Moyer M.L., Gilbert S.P., and Johnson K.A. Pathway of ATP hydrolysis by monomeric and dimeric kinesin. Biochemistry 37 (1998) 800-813
    • (1998) Biochemistry , vol.37 , pp. 800-813
    • Moyer, M.L.1    Gilbert, S.P.2    Johnson, K.A.3
  • 53
    • 33644651118 scopus 로고    scopus 로고
    • A non-Markov ratchet model of molecular motors: processive movement of single-headed kinesin KIF1A
    • Xie P., Dou S.-X., and Wang P.-Y. A non-Markov ratchet model of molecular motors: processive movement of single-headed kinesin KIF1A. Chin. Phys. 15 (2006) 536-541
    • (2006) Chin. Phys. , vol.15 , pp. 536-541
    • Xie, P.1    Dou, S.-X.2    Wang, P.-Y.3
  • 55
    • 0031556947 scopus 로고    scopus 로고
    • Motor domains of kinesin and ncd interact with microtubule protofilaments with the same binding geometry
    • Hoenger A., and Milligan R.A. Motor domains of kinesin and ncd interact with microtubule protofilaments with the same binding geometry. J. Mol. Biol. 265 (2007) 553-564
    • (2007) J. Mol. Biol. , vol.265 , pp. 553-564
    • Hoenger, A.1    Milligan, R.A.2
  • 56
    • 0030930492 scopus 로고    scopus 로고
    • Three-dimensional cryoelectron microscopy of 16-protofilament microtubules: structure, polarity, and interaction with motor proteins
    • Hirose K., Amos W.B., Lockhart A., Cross R.A., and Amos L.A. Three-dimensional cryoelectron microscopy of 16-protofilament microtubules: structure, polarity, and interaction with motor proteins. J. Struct. Biol. 118 (1997) 140-148
    • (1997) J. Struct. Biol. , vol.118 , pp. 140-148
    • Hirose, K.1    Amos, W.B.2    Lockhart, A.3    Cross, R.A.4    Amos, L.A.5
  • 57
    • 0029914906 scopus 로고    scopus 로고
    • Weak and strong states of kinesin and ncd
    • Crevel I.M., Lockhart A., and Cross R.A. Weak and strong states of kinesin and ncd. J. Mol. Biol. 257 (1996) 66-76
    • (1996) J. Mol. Biol. , vol.257 , pp. 66-76
    • Crevel, I.M.1    Lockhart, A.2    Cross, R.A.3
  • 59
    • 3442876110 scopus 로고    scopus 로고
    • KIF1A alternately uses two loops to bind microtubules
    • Nitta R., Kikkawa M., Okada Y., and Hirokawa N. KIF1A alternately uses two loops to bind microtubules. Science 305 (2004) 678-683
    • (2004) Science , vol.305 , pp. 678-683
    • Nitta, R.1    Kikkawa, M.2    Okada, Y.3    Hirokawa, N.4
  • 60
    • 4143067982 scopus 로고    scopus 로고
    • Structural dynamics of actin during active interaction with myosin: different effects of weakly and strongly bound myosin heads
    • Prochniewicz E., Walseth T.F., and Thomas D.D. Structural dynamics of actin during active interaction with myosin: different effects of weakly and strongly bound myosin heads. Biochemistry 43 (2004) 10642-10652
    • (2004) Biochemistry , vol.43 , pp. 10642-10652
    • Prochniewicz, E.1    Walseth, T.F.2    Thomas, D.D.3
  • 62
    • 34247237308 scopus 로고    scopus 로고
    • Multivariate analysis of conserved sequence-structure relationships in kinesins: coupling of the active site and a tubulin-binding sub-domain
    • Grant B.J., McCammon J.A., Caves L.S.D., and Cross R.A. Multivariate analysis of conserved sequence-structure relationships in kinesins: coupling of the active site and a tubulin-binding sub-domain. J. Mol. Biol. 368 (2007) 1231-1248
    • (2007) J. Mol. Biol. , vol.368 , pp. 1231-1248
    • Grant, B.J.1    McCammon, J.A.2    Caves, L.S.D.3    Cross, R.A.4
  • 63
    • 33745606424 scopus 로고    scopus 로고
    • A hand-over-hand diffusing model for myosin-VI molecular motors
    • Xie P., Dou S.-X., and Wang P.-Y. A hand-over-hand diffusing model for myosin-VI molecular motors. Biophys. Chemist. 122 (2006) 90-100
    • (2006) Biophys. Chemist. , vol.122 , pp. 90-100
    • Xie, P.1    Dou, S.-X.2    Wang, P.-Y.3
  • 64
    • 35949005624 scopus 로고
    • Stochastic Runge-Kutta algorithms. I. White noise
    • Honeycutt R.L. Stochastic Runge-Kutta algorithms. I. White noise. Phys. Rev., A 45 (1992) 600-603
    • (1992) Phys. Rev., A , vol.45 , pp. 600-603
    • Honeycutt, R.L.1
  • 65
    • 34547275473 scopus 로고
    • Brownian motion in a field of force and the diffusion model of chemical reactions
    • Kramers H.A. Brownian motion in a field of force and the diffusion model of chemical reactions. Physika 7 (1940) 284-304
    • (1940) Physika , vol.7 , pp. 284-304
    • Kramers, H.A.1
  • 66
    • 33644835305 scopus 로고    scopus 로고
    • A torque component in the kinesin-1 power stroke
    • Yajima J., and Cross R.A. A torque component in the kinesin-1 power stroke. Nat. Chem. Biol. 1 (2005) 338-341
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 338-341
    • Yajima, J.1    Cross, R.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.