메뉴 건너뛰기




Volumn 354, Issue 2, 2007, Pages 379-384

The diffusive search mechanism of processive myosin class-V motor involves directional steps along actin subunits

Author keywords

5.5 nm substep; Actin filament; Myosin V; Processive movement; Scanning probe nanometry

Indexed keywords

MYOSIN V;

EID: 33846476143     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.12.200     Document Type: Article
Times cited : (25)

References (36)
  • 5
    • 0037832404 scopus 로고    scopus 로고
    • Myosin-V walks hand over hand: single fluorophore imaging with 1.5 nm localization
    • Yildiz A., Forkey J.N., McKinney S.A., Ha T., Goldman Y.E., and Selvin P.R. Myosin-V walks hand over hand: single fluorophore imaging with 1.5 nm localization. Science 300 (2003) 2061-2065
    • (2003) Science , vol.300 , pp. 2061-2065
    • Yildiz, A.1    Forkey, J.N.2    McKinney, S.A.3    Ha, T.4    Goldman, Y.E.5    Selvin, P.R.6
  • 6
    • 0037468838 scopus 로고    scopus 로고
    • Three dimensional structural dynamics of myosin-V by single-molecule fluorescence polarization
    • Forkey J.N., Quinlan M.E., Shaw M.A., Corrie J.E., and Goldman Y.E. Three dimensional structural dynamics of myosin-V by single-molecule fluorescence polarization. Nature 422 (2003) 399-404
    • (2003) Nature , vol.422 , pp. 399-404
    • Forkey, J.N.1    Quinlan, M.E.2    Shaw, M.A.3    Corrie, J.E.4    Goldman, Y.E.5
  • 8
    • 10644225267 scopus 로고    scopus 로고
    • Three myosin V structures delineate essential features of chemo-mechanical transduction
    • Coureux P.-D., Sweeney H.L., and Houdusse A. Three myosin V structures delineate essential features of chemo-mechanical transduction. EMBO J. 23 (2004) 4527-4537
    • (2004) EMBO J. , vol.23 , pp. 4527-4537
    • Coureux, P.-D.1    Sweeney, H.L.2    Houdusse, A.3
  • 10
    • 0014685163 scopus 로고
    • The mechanism of muscular contraction
    • Huxley H.E. The mechanism of muscular contraction. Science 164 (1969) 1355-1366
    • (1969) Science , vol.164 , pp. 1355-1366
    • Huxley, H.E.1
  • 11
    • 0015236610 scopus 로고
    • Proposed mechanism of force generation in striated muscle
    • Huxley A.F., and Simmons R.M. Proposed mechanism of force generation in striated muscle. Nature 233 (1971) 533-538
    • (1971) Nature , vol.233 , pp. 533-538
    • Huxley, A.F.1    Simmons, R.M.2
  • 12
    • 26944449015 scopus 로고    scopus 로고
    • Load-dependent kinetics of myosin-V can explain its high processivity
    • Veigel C., Schmitz S., Wang F., and Sellers J.R. Load-dependent kinetics of myosin-V can explain its high processivity. Nat. Cell Biol. 7 (2005) 861-869
    • (2005) Nat. Cell Biol. , vol.7 , pp. 861-869
    • Veigel, C.1    Schmitz, S.2    Wang, F.3    Sellers, J.R.4
  • 15
    • 0033552942 scopus 로고    scopus 로고
    • A single myosin head moves along an actin filament with regular steps of 5.3 nanometres
    • Kitamura K., Tokunaga M., Iwane A.H., and Yanagida T. A single myosin head moves along an actin filament with regular steps of 5.3 nanometres. Nature 397 (1999) 129-134
    • (1999) Nature , vol.397 , pp. 129-134
    • Kitamura, K.1    Tokunaga, M.2    Iwane, A.H.3    Yanagida, T.4
  • 16
    • 33846534174 scopus 로고    scopus 로고
    • K. Kitamura, M. Tokunaga, S. Esaki, A.H. Iwane, T. Yanagida, Mechanism of muscle contraction based on stochastic properties of single actomyosin motors observed in vitro, Biophysics 1 (2005) 1-19. http://www.biophys.jp/.
  • 19
    • 0034602399 scopus 로고    scopus 로고
    • 2+-dependent regulation of the motor activity of myosin-V
    • 2+-dependent regulation of the motor activity of myosin-V. J. Biol. Chem. 275 (2000) 34766-34771
    • (2000) J. Biol. Chem. , vol.275 , pp. 34766-34771
    • Homma, K.1    Saito, J.2    Ikebe, R.3    Ikebe, M.4
  • 20
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich J.A., and Watt S. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246 (1971) 4866-4871
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 22
    • 0032559298 scopus 로고    scopus 로고
    • Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin
    • Ishijima A., Kojima H., Funatsu T., Tokunaga M., Higuchi H., Tanaka H., and Yanagida T. Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin. Cell 92 (1998) 161-171
    • (1998) Cell , vol.92 , pp. 161-171
    • Ishijima, A.1    Kojima, H.2    Funatsu, T.3    Tokunaga, M.4    Higuchi, H.5    Tanaka, H.6    Yanagida, T.7
  • 23
    • 0034616649 scopus 로고    scopus 로고
    • Direct observation of processive movement by individual myosin V molecules
    • Sakamoto T., Amitani I., Yokota E., and Ando T. Direct observation of processive movement by individual myosin V molecules. Biochem. Biophys. Res. Commun. 272 (2000) 586-590
    • (2000) Biochem. Biophys. Res. Commun. , vol.272 , pp. 586-590
    • Sakamoto, T.1    Amitani, I.2    Yokota, E.3    Ando, T.4
  • 25
    • 0025934829 scopus 로고
    • A model for kinesin movement from nanometer-level movements of kinesin and cytoplasmic dynein and force measurements
    • Kuo S.C., Gelles J., Steuer E., and Sheetz M.P. A model for kinesin movement from nanometer-level movements of kinesin and cytoplasmic dynein and force measurements. J. Cell Sci. 14 (1991) 135-138
    • (1991) J. Cell Sci. , vol.14 , pp. 135-138
    • Kuo, S.C.1    Gelles, J.2    Steuer, E.3    Sheetz, M.P.4
  • 26
    • 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
  • 27
    • 0028945654 scopus 로고
    • Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution
    • Funatsu T., Harada Y., Tokunaga M., Saito K., and Yanagida T. Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution. Nature 374 (1995) 555-559
    • (1995) Nature , vol.374 , pp. 555-559
    • Funatsu, T.1    Harada, Y.2    Tokunaga, M.3    Saito, K.4    Yanagida, T.5
  • 28
    • 0031560940 scopus 로고    scopus 로고
    • Single molecule imaging of fluorophores and enzymatic reactions achieved by objective-type total internal reflection fluorescence microscopy
    • Tokunaga M., Kitamura K., Saito K., Iwane A.H., and Yanagida T. Single molecule imaging of fluorophores and enzymatic reactions achieved by objective-type total internal reflection fluorescence microscopy. Biochem. Biophys. Res. Commun. 235 (1997) 47-53
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 47-53
    • Tokunaga, M.1    Kitamura, K.2    Saito, K.3    Iwane, A.H.4    Yanagida, T.5
  • 29
    • 0028362896 scopus 로고
    • Force and velocity measured for single kinesin molecules
    • Svoboda K., and Block S.M. Force and velocity measured for single kinesin molecules. Cell 77 (1994) 773-784
    • (1994) Cell , vol.77 , pp. 773-784
    • Svoboda, K.1    Block, S.M.2
  • 30
    • 25444437003 scopus 로고    scopus 로고
    • A force-dependent state controls the coordination of processive myosin V
    • Purcell T.J., Sweeney H.L., and Spudich J.A. A force-dependent state controls the coordination of processive myosin V. Proc. Natl. Acad. Sci. USA 102 (2005) 13873-13878
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 13873-13878
    • Purcell, T.J.1    Sweeney, H.L.2    Spudich, J.A.3
  • 31
    • 0021261156 scopus 로고
    • Direct observation of motion of single F-actin filaments in the presence of myosin
    • Yanagida T., Nakase M., Nishiyama K., and Oosawa F. Direct observation of motion of single F-actin filaments in the presence of myosin. Nature 307 (1984) 58-60
    • (1984) Nature , vol.307 , pp. 58-60
    • Yanagida, T.1    Nakase, M.2    Nishiyama, K.3    Oosawa, F.4
  • 32
    • 27144435137 scopus 로고    scopus 로고
    • Cooperative structural change of actin filaments interacting with activated myosin motor domain, detected with copolymers of pyrene-labeled actin and acto-S1 chimera protein
    • Siddique Md.S.P., Mogami G., Miyazaki T., Katayama E., Ueda T.Q.P., and Suzuki M. Cooperative structural change of actin filaments interacting with activated myosin motor domain, detected with copolymers of pyrene-labeled actin and acto-S1 chimera protein. Biochem. Biophys. Res. Commun. 337 (2005) 1185-1191
    • (2005) Biochem. Biophys. Res. Commun. , vol.337 , pp. 1185-1191
    • Siddique, Md.S.P.1    Mogami, G.2    Miyazaki, T.3    Katayama, E.4    Ueda, T.Q.P.5    Suzuki, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.