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Volumn 13, Issue 1, 2012, Pages 13-26

Walking to work: Roles for class v myosins as cargo transporters

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; MESSENGER RNA; MYOSIN 4; MYOSIN V; MYOSIN VA; UNCLASSIFIED DRUG;

EID: 84355161386     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm3248     Document Type: Review
Times cited : (251)

References (146)
  • 1
    • 37549069575 scopus 로고    scopus 로고
    • Drawing the tree of eukaryotic life based on the analysis of 2269 manually annotated myosins from 328 species
    • Odronitz, F. & Kollmar, M. Drawing the tree of eukaryotic life based on the analysis of 2269 manually annotated myosins from 328 species. Genome Biol. 8, R196 (2007).
    • (2007) Genome Biol , vol.8
    • Odronitz, F.1    Kollmar, M.2
  • 2
    • 0004161470 scopus 로고    scopus 로고
    • Oxford University Press
    • Sellers, J. R. Myosins (Oxford University Press, 1999).
    • (1999) Myosins
    • Sellers, J.R.1
  • 4
    • 0030606512 scopus 로고    scopus 로고
    • Is the lever arm of myosin a molecular elastic element?
    • Howard, J. & Spudich, J. A. Is the lever arm of myosin a molecular elastic element? Proc. Natl Acad. Sci. USA 93, 4462-4464 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 4462-4464
    • Howard, J.1    Spudich, J.A.2
  • 6
    • 0035123582 scopus 로고    scopus 로고
    • Single-molecule tracking of myosins with genetically engineered amplifier domains
    • DOI 10.1038/84962
    • Ruff, C., Furch, M., Brenner, B., Manstein, D. J. & Meyhofer, E. Single-molecule tracking of myosins with genetically engineered amplifier domains. Nature Struct. Biol. 8, 226-229 (2001). (Pubitemid 32180047)
    • (2001) Nature Structural Biology , vol.8 , Issue.3 , pp. 226-229
    • Ruff, C.1    Furch, M.2    Brenner, B.3    Manstein, D.J.4    Meyhofer, E.5
  • 7
    • 24044500344 scopus 로고    scopus 로고
    • Myosins: Tails (and heads) of functional diversity
    • Krendel, M. & Mooseker, M. S. Myosins: tails (and heads) of functional diversity. Physiology (Bethesda) 20, 239-251 (2005). (Pubitemid 41215198)
    • (2005) Physiology , Issue.4 , pp. 239-251
    • Krendel, M.1    Mooseker, M.S.2
  • 12
    • 17844385071 scopus 로고    scopus 로고
    • Differential labeling of myosin V heads with quantum dots allows direct visualization of hand-over-hand processivity
    • DOI 10.1529/biophysj.105.061903
    • Warshaw, D. M. et al. Differential labeling of myosin V heads with quantum dots allows direct visualization of hand-over-hand processivity. Biophys. J. 88, L30-L32 (2005). (Pubitemid 40586558)
    • (2005) Biophysical Journal , vol.88 , Issue.5
    • Warshaw, D.M.1    Kennedy, G.G.2    Work, S.S.3    Krementsova, E.B.4    Beck, S.5    Trybus, K.M.6
  • 15
    • 0036144267 scopus 로고    scopus 로고
    • The gated gait of the processive molecular motor, myosin V
    • DOI 10.1038/ncb732
    • Veigel, C., Wang, F., Bartoo, M. L., Sellers, J. R. & Molloy, J. E. The gated gait of the precessive molecular motor, myosin V. Nature Cell Biol. 4, 59-65 (2001). (Pubitemid 34071981)
    • (2002) Nature Cell Biology , vol.4 , Issue.1 , pp. 59-65
    • Veigel, C.1    Wang, F.2    Bartoo, M.L.3    Sellers, J.R.4    Molloy, J.E.5
  • 17
    • 0037832404 scopus 로고    scopus 로고
    • Myosin V walks hand-over-hand: Single fluorophore imaging with 1.5-nm localization
    • DOI 10.1126/science.1084398
    • Yildiz, A. et al. Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization. Science 300, 2061-2065 (2003). (Pubitemid 36760126)
    • (2003) Science , vol.300 , Issue.5628 , 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
  • 18
    • 4444384544 scopus 로고    scopus 로고
    • Nanometer localization of single fluorescent proteins: Evidence that myosin V walks hand-over-hand via telemark configuration
    • DOI 10.1529/biophysj.103.036897
    • Snyder, G. E., Sakamoto, T., Hammer, J. A. III, Sellers, J. R. & Selvin, P. R. Nanometer localization of single green fluorescent proteins: evidence that myosin V walks hand-over-hand via telemark configuration. Biophys. J. 87, 1776-1783 (2004). (Pubitemid 39167033)
    • (2004) Biophysical Journal , vol.87 , Issue.3 , pp. 1776-1783
    • Snyder, G.E.1    Sakamoto, T.2    Hammer III, J.A.3    Sellers, J.R.4    Selvin, P.R.5
  • 19
    • 78149285270 scopus 로고    scopus 로고
    • Video imaging of walking myosin v by high-speed atomic force microscopy
    • Kodera, N., Yamamoto, D., Ishikawa, R. & Ando, T. Video imaging of walking myosin V by high-speed atomic force microscopy. Nature 468, 72-76 (2010).
    • (2010) Nature , vol.468 , pp. 72-76
    • Kodera, N.1    Yamamoto, D.2    Ishikawa, R.3    Ando, T.4
  • 20
    • 73349126085 scopus 로고    scopus 로고
    • Extensibility of the extended tail domain of processive and nonprocessive myosin v molecules
    • Nagy, A., Piszczek, G. & Sellers, J. R. Extensibility of the extended tail domain of processive and nonprocessive myosin V molecules. Biophys. J. 97, 3123-3131 (2009).
    • (2009) Biophys. J. , vol.97 , pp. 3123-3131
    • Nagy, A.1    Piszczek, G.2    Sellers, J.R.3
  • 21
    • 33746132537 scopus 로고    scopus 로고
    • An elastically tethered viscous load imposes a regular gait on the motion of myosin-V. Simulation of the effect of transient force relaxation on a stochastic process
    • DOI 10.1098/rsif.2005.0098
    • Schilstra, M. J. & Martin, S. R. An elastically tethered viscous load imposes a regular gait on the motion of myosin-V. Simulation of the effect of transient force relaxation on a stochastic process. J. R. Soc. Interface 3, 153-165 (2005). (Pubitemid 46682214)
    • (2006) Journal of the Royal Society Interface , vol.3 , Issue.6 , pp. 153-165
    • Schilstra, M.J.1    Martin, S.R.2
  • 23
    • 0036000020 scopus 로고    scopus 로고
    • Rab27a is an essential component of melanosome receptor for myosin Va
    • DOI 10.1091/mbc.01-12-0595
    • Wu, X., Wang, F., Rao, K., Sellers, J. R. & Hammer, J. A. III. Rab27a is an essential component of melanosome receptor for myosin Va. Mol. Biol. Cell 13, 1735-1749 (2002). (Pubitemid 34522652)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.5 , pp. 1735-1749
    • Wu, X.1    Wang, F.2    Rao, K.3    Sellers, J.R.4    Hammer III, J.A.5
  • 24
    • 0037023745 scopus 로고    scopus 로고
    • Slac2-a/melanophilin, the missing link between Rab27 and myosin Va: Implications of a tripartite protein complex for melanosome transport
    • DOI 10.1074/jbc.C200005200
    • Fukuda, M., Kuroda, T. S. & Mikoshiba, K. Slac2-a/melanophilin, the missing link between Rab27 and myosin Va: implications of a tripartite protein complex for melanosome transport. J. Biol. Chem. 277, 12432-12436 (2002). (Pubitemid 34952817)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.14 , pp. 12432-12436
    • Fukuda, M.1    Kuroda, T.S.2    Mikoshiba, K.3
  • 25
    • 0037067673 scopus 로고    scopus 로고
    • A family of Rab27-binding proteins: Melanophilin links Rab27a and myosin Va function in melanosome transport
    • DOI 10.1074/jbc.M202574200
    • Strom, M., Hume, A. N., Tarafder, A. K., Barkagianni, E. & Seabra, M. C. A family of Rab27-binding proteins. Melanophilin links Rab27a and myosin Va function in melanosome transport. J. Biol. Chem. 277, 25423-25430 (2002). (Pubitemid 34951855)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.28 , pp. 25423-25430
    • Strom, M.1    Hume, A.N.2    Tarafder, A.K.3    Barkagianni, E.4    Seabra, M.C.5
  • 26
    • 0037165662 scopus 로고    scopus 로고
    • Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions
    • DOI 10.1016/S0014-5793(02)02634-0, PII S0014579302026340
    • Nagashima, K. et al. Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions. FEBS Lett. 517, 233-238 (2002). (Pubitemid 34327666)
    • (2002) FEBS Letters , vol.517 , Issue.1-3 , pp. 233-238
    • Nagashima, K.1    Torii, S.2    Yi, Z.3    Igarashi, M.4    Okamoto, K.5    Takeuchi, T.6    Izumi, T.7
  • 27
    • 33749012287 scopus 로고    scopus 로고
    • The binding of DYNLL2 to myosin Va requires alternatively spliced exon B and stabilizes a portion of the myosin's coiled-coil domain
    • DOI 10.1021/bi061142u
    • Wagner, W., Fodor, E., Ginsburg, A. & Hammer, J. A. III. The binding of DYNLL2 to myosin Va requires alternatively spliced exon B and stabilizes a portion of the myosin's coiled-coil domain. Biochemistry 45, 11564-11577 (2006). (Pubitemid 44454004)
    • (2006) Biochemistry , vol.45 , Issue.38 , pp. 11564-11577
    • Wagner, W.1    Fodor, E.2    Ginsburg, A.3    Hammer III, J.A.4
  • 28
    • 33750054653 scopus 로고    scopus 로고
    • Alternatively spliced exon B of myosin Va is essential for binding the tail-associated light chain shared by dynein
    • DOI 10.1021/bi060991e
    • Hodi, Z. et al. Alternatively spliced exon B of myosin Va is essential for binding the tail-associated light chain shared by dynein. Biochemistry 45, 12582-12595 (2006). (Pubitemid 44583700)
    • (2006) Biochemistry , vol.45 , Issue.41 , pp. 12582-12595
    • Hodi, Z.1    Nemeth, A.L.2    Radnai, L.3    Hetenyi, C.4    Schlett, K.5    Bodor, A.6    Perczel, A.7    Nyitray, L.8
  • 29
    • 77951207269 scopus 로고    scopus 로고
    • Motor number controls cargo switching at actin-microtubule intersections in vitro
    • Schroeder, H. W. III, Mitchell, C., Shuman, H., Holzbaur, E. L. & Goldman, Y. E. Motor number controls cargo switching at actin-microtubule intersections in vitro. Curr. Biol. 20, 687-696 (2010).
    • (2010) Curr. Biol. , vol.20 , pp. 687-696
    • Schroeder Iii, H.W.1    Mitchell, C.2    Shuman, H.3    Holzbaur, E.L.4    Goldman, Y.E.5
  • 32
    • 26944449015 scopus 로고    scopus 로고
    • Load-dependent kinetics of myosin-V can explain its high processivity
    • DOI 10.1038/ncb1287, PII N1287
    • Veigel, C., Schmitz, S., Wang, F. & Sellers, J. R. Load-dependent kinetics of myosin-V can explain its high processivity. Nature Cell Biol. 7, 861-869 (2005). (Pubitemid 41486286)
    • (2005) Nature Cell Biology , vol.7 , Issue.9 , pp. 861-869
    • Veigel, C.1    Schmitz, S.2    Wang, F.3    Sellers, J.R.4
  • 33
    • 4544232738 scopus 로고    scopus 로고
    • A model of myosin V processivity
    • DOI 10.1074/jbc.M402583200
    • Rosenfeld, S. S. & Sweeney, H. L. A model of myosin V processivity. J. Biol. Chem. 279, 40100-40111 (2004). (Pubitemid 39258285)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.38 , pp. 40100-40111
    • Rosenfeld, S.S.1    Sweeney, H.L.2
  • 35
    • 38149111237 scopus 로고    scopus 로고
    • Kinetics of ADP dissociation from the trail and lead heads of actomyosin v following the power stroke
    • Forgacs, E. et al. Kinetics of ADP dissociation from the trail and lead heads of actomyosin V following the power stroke. J. Biol. Chem. 283, 766-773 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 766-773
    • Forgacs, E.1
  • 36
    • 51349088578 scopus 로고    scopus 로고
    • Direct observation of the mechanochemical coupling in myosin va during processive movement
    • Sakamoto, T., Webb, M. R., Forgacs, E., White, H. D. & Sellers, J. R. Direct observation of the mechanochemical coupling in myosin Va during processive movement. Nature 455, 128-132 (2008).
    • (2008) Nature , vol.455 , pp. 128-132
    • Sakamoto, T.1    Webb, M.R.2    Forgacs, E.3    White, H.D.4    Sellers, J.R.5
  • 37
    • 33746152398 scopus 로고    scopus 로고
    • The cargo-binding domain regulates structure and activity of myosin 5
    • DOI 10.1038/nature04865, PII NATURE04865
    • Thirumurugan, K., Sakamoto, T., Hammer, J. A. III, Sellers, J. R. & Knight, P. J. The cargo-binding domain regulates structure and activity of myosin 5. Nature 442, 212-215 (2006). (Pubitemid 44086569)
    • (2006) Nature , vol.442 , Issue.7099 , pp. 212-215
    • Thirumurugan, K.1    Sakamoto, T.2    Hammer III, J.A.3    Sellers, J.R.4    Knight, P.J.5
  • 38
    • 33746129173 scopus 로고    scopus 로고
    • Three-dimensional structure of the myosin V inhibited state by cryoelectron tomography
    • DOI 10.1038/nature04719, PII NATURE04719
    • Liu, J., Taylor, D. W., Krementsova, E. B., Trybus, K. M. & Taylor, K. A. Three-dimensional structure of the myosin V inhibited state by cryoelectron tomography. Nature 442, 208-211 (2006). (Pubitemid 44086568)
    • (2006) Nature , vol.442 , Issue.7099 , pp. 208-211
    • Liu, J.1    Taylor, D.W.2    Krementsova, E.B.3    Trybus, K.M.4    Taylor, K.A.5
  • 40
    • 34250336101 scopus 로고    scopus 로고
    • Myosin Va becomes a low duty ratio motor in the inhibited form
    • DOI 10.1074/jbc.M610766200
    • Sato, O., Li, X. D. & Ikebe, M. Myosin Va becomes a low duty ratio motor in the inhibited form. J. Biol. Chem. 282, 13228-13239 (2007). (Pubitemid 47100520)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.18 , pp. 13228-13239
    • Sato, O.1    Li, X.-D.2    Ikebe, M.3
  • 41
    • 33845894135 scopus 로고    scopus 로고
    • Regulation of myosin V processivity by calcium at the single molecule level
    • DOI 10.1074/jbc.M605181200
    • Lu, H., Krementsova, E. B. & Trybus, K. M. Regulation of myosin V processivity by calcium at the single molecule level. J. Biol. Chem. 281, 31987-31994 (2006). (Pubitemid 46041460)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.42 , pp. 31987-31994
    • Lu, H.1    Krementsova, E.B.2    Trybus, K.M.3
  • 43
    • 15544376251 scopus 로고    scopus 로고
    • Motility of myosin v regulated by the dissociation of single calmodulin
    • Nguyen, H. & Higuchi, H. Motility of myosin V regulated by the dissociation of single calmodulin. Nature Struct. Mol. Biol. 12, 127-132 (2005).
    • (2005) Nature Struct. Mol. Biol. , vol.12 , pp. 127-132
    • Nguyen, H.1    Higuchi, H.2
  • 44
    • 33750054102 scopus 로고    scopus 로고
    • In vitro reconstitution of a transport complex containing Rab27a, melanophilin and myosin Va
    • DOI 10.1016/j.febslet.2006.09.047, PII S0014579306011598
    • Wu, X., Sakamoto, T., Zhang, F., Sellers, J. R. & Hammer, J. A. III. In vitro reconstitution of a transport complex containing Rab27a, melanophilin and myosin Va. FEBS Lett. 580, 5863-5868 (2006). (Pubitemid 44584286)
    • (2006) FEBS Letters , vol.580 , Issue.25 , pp. 5863-5868
    • Wu, X.1    Sakamoto, T.2    Zhang, F.3    Sellers, J.R.4    Hammer III, J.A.5
  • 45
    • 24044519039 scopus 로고    scopus 로고
    • Activation of myosin Va function by melanophilin, a specific docking partner of myosin Va
    • DOI 10.1074/jbc.M413295200
    • Li, X. D., Ikebe, R. & Ikebe, M. Activation of myosin Va function by melanophilin, a specific docking partner of myosin Va. J. Biol. Chem. 280, 17815-17822 (2005). (Pubitemid 41389021)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.18 , pp. 17815-17822
    • Li, X.-D.1    Ikebe, R.2    Ikebei, M.3
  • 46
    • 33644510103 scopus 로고    scopus 로고
    • Mechanoenzymatic characterization of human myosin vb
    • Watanabe, S., Mabuchi, K., Ikebe, R. & Ikebe, M. Mechanoenzymatic characterization of human myosin Vb. Biochemistry 45, 2729-2738 (2006).
    • (2006) Biochemistry , vol.45 , pp. 2729-2738
    • Watanabe, S.1    Mabuchi, K.2    Ikebe, R.3    Ikebe, M.4
  • 47
    • 43749114291 scopus 로고    scopus 로고
    • Human myosin vc is a low duty ratio, non-processive molecular motor
    • Takagi, Y. et al. Human myosin Vc is a low duty ratio, non-processive molecular motor. J. Biol. Chem. 283, 8527-8537 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 8527-8537
    • Takagi, Y.1
  • 48
    • 24044527127 scopus 로고    scopus 로고
    • Myosin V from Drosophila reveals diversity of motor mechanisms within the myosin V family
    • DOI 10.1074/jbc.M505209200
    • Toth, J., Kovacs, M., Wang, F., Nyitray, L. & Sellers, J. R. Myosin V from Drosophila reveals diversity of motor mechanisms within the myosin V family. J. Biol. Chem. 280, 30594-30603 (2005). (Pubitemid 41216245)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.34 , pp. 30594-30603
    • Toth, J.1    Kovacs, M.2    Wang, F.3    Nyitray, L.4    Sellers, J.R.5
  • 49
    • 44849137931 scopus 로고    scopus 로고
    • Human myosin vc is a low duty ratio nonprocessive motor
    • Watanabe, S. et al. Human myosin Vc is a low duty ratio nonprocessive motor. J. Biol. Chem. 283, 10581-10592 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 10581-10592
    • Watanabe, S.1
  • 50
    • 55249113411 scopus 로고    scopus 로고
    • Dictyostelium myosin-5b is a conditional processive motor
    • Taft, M. H. et al. Dictyostelium myosin-5b is a conditional processive motor. J. Biol. Chem. 283, 26902-26910 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 26902-26910
    • Taft, M.H.1
  • 51
    • 34748902975 scopus 로고    scopus 로고
    • Myo4p is a monomeric myosin with motility uniquely adapted to transport mRNA
    • DOI 10.1083/jcb.200707080
    • Dunn, B. D., Sakamoto, T., Hong, M. S., Sellers, J. R. & Takizawa, P. A. Myo4p is a monomeric myosin with motility uniquely adapted to transport mRNA. J. Cell Biol. 178, 1193-1206 (2007). (Pubitemid 47480226)
    • (2007) Journal of Cell Biology , vol.178 , Issue.7 , pp. 1193-1206
    • Dunn, B.D.1    Sakamoto, T.2    Hong, M.S.3    Sellers, J.R.4    Takizawa, P.A.5
  • 52
    • 72449125767 scopus 로고    scopus 로고
    • A nonprocessive class v myosin drives cargo processively when A kinesin-related protein is A passenger
    • Hodges, A. R., Bookwalter, C. S., Krementsova, E. B. & Trybus, K. M. A nonprocessive class V myosin drives cargo processively when a kinesin-related protein is a passenger. Curr. Biol. 19, 2121-2125 (2009).
    • (2009) Curr. Biol. , vol.19 , pp. 2121-2125
    • Hodges, A.R.1    Bookwalter, C.S.2    Krementsova, E.B.3    Trybus, K.M.4
  • 53
    • 43749103605 scopus 로고    scopus 로고
    • She3p binds to the rod of yeast myosin v and prevents it from dimerizing, forming a single-headed motor complex
    • Hodges, A. R., Krementsova, E. B. & Trybus, K. M. She3p binds to the rod of yeast myosin V and prevents it from dimerizing, forming a single-headed motor complex. J. Biol. Chem. 283, 6906-6914 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 6906-6914
    • Hodges, A.R.1    Krementsova, E.B.2    Trybus, K.M.3
  • 55
    • 0347416707 scopus 로고    scopus 로고
    • Yeast vacuole inheritance and dynamics
    • DOI 10.1146/annurev.genet.37.050203.103207
    • Weisman, L. S. Yeast vacuole inheritance and dynamics. Annu. Rev. Genet. 37, 435-460 (2003). (Pubitemid 38041434)
    • (2003) Annual Review of Genetics , vol.37 , pp. 435-460
    • Weisman, L.S.1
  • 56
  • 57
    • 0037033787 scopus 로고    scopus 로고
    • Secretory vesicle transport velocity in living cells depends on the myosin-V lever arm length
    • DOI 10.1083/jcb.200110086
    • Schott, D. H., Collins, R. N. & Bretscher, A. Secretory vesicles transport velocity in living cells depends on the myosin-V lever arm. J. Cell Biol. 156, 35-39 (2002). (Pubitemid 34846933)
    • (2002) Journal of Cell Biology , vol.156 , Issue.1 , pp. 35-39
    • Schott, D.H.1    Collins, R.N.2    Bretscher, A.3
  • 58
    • 57349092518 scopus 로고    scopus 로고
    • Direct interaction between a myosin v motor and the rab gtpases ypt31/32 is required for polarized secretion
    • Lipatova, Z. et al. Direct interaction between a myosin V motor and the Rab GTPases Ypt31/32 is required for polarized secretion. Mol. Biol. Cell 19, 4177-4187 (2008).
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4177-4187
    • Lipatova, Z.1
  • 59
    • 78651445373 scopus 로고    scopus 로고
    • Pi4p and rab inputs collaborate in myosin-v-dependent transport of secretory compartments in yeast
    • Santiago-Tirado, F. H., Legesse-Miller, A., Schott, D. & Bretscher, A. PI4P and Rab inputs collaborate in myosin-V-dependent transport of secretory compartments in yeast. Dev. Cell 20, 47-59 (2011).
    • (2011) Dev. Cell , vol.20 , pp. 47-59
    • Santiago-Tirado, F.H.1    Legesse-Miller, A.2    Schott, D.3    Bretscher, A.4
  • 60
    • 77952943084 scopus 로고    scopus 로고
    • Phosphatidylinositol 4-Phosphate controls both membrane recruitment and a regulatory switch of the rab GEF sec2p
    • Mizuno-Yamasaki, E., Medkova, M., Coleman, J. & Novick, P. Phosphatidylinositol 4-phosphate controls both membrane recruitment and a regulatory switch of the Rab GEF Sec2p. Dev. Cell 18, 828-840 (2010).
    • (2010) Dev. Cell , vol.18 , pp. 828-840
    • Mizuno-Yamasaki, E.1    Medkova, M.2    Coleman, J.3    Novick, P.4
  • 62
    • 79151470948 scopus 로고    scopus 로고
    • Coordination of golgi functions by phosphatidylinositol 4-Kinases
    • Graham, T. R. & Burd, C. G. Coordination of Golgi functions by phosphatidylinositol 4-kinases. Trends Cell Biol. 21, 113-121 (2011).
    • (2011) Trends Cell Biol , vol.21 , pp. 113-121
    • Graham, T.R.1    Burd, C.G.2
  • 63
    • 0035795423 scopus 로고    scopus 로고
    • A role for actin, cdc1p, and myo2p in the inheritance of late golgi elements in saccharomyces Cerevisiae
    • Rossanese, O. W. et al. A role for actin, Cdc1p, and Myo2p in the inheritance of late Golgi elements in Saccharomyces cerevisiae. J. Cell Biol. 153, 47-62 (2001).
    • (2001) J. Cell Biol. , vol.153 , pp. 47-62
    • Rossanese, O.W.1
  • 64
    • 46049104580 scopus 로고    scopus 로고
    • Ypt11 functions in bud-directed transport of the golgi by linking myo2 to the coatomer subunit ret2
    • Arai, S., Noda, Y., Kainuma, S., Wada, I. & Yoda, K. Ypt11 functions in bud-directed transport of the Golgi by linking Myo2 to the coatomer subunit Ret2. Curr. Biol. 18, 987-991 (2008).
    • (2008) Curr. Biol. , vol.18 , pp. 987-991
    • Arai, S.1    Noda, Y.2    Kainuma, S.3    Wada, I.4    Yoda, K.5
  • 65
    • 0030470182 scopus 로고    scopus 로고
    • Actin and myosin function in directed vacuole movement during cell division in Saccharomyces cerevisiae
    • DOI 10.1083/jcb.135.6.1535
    • Hill, K. L., Catlett, N. L. & Weisman, L. S. Actin and myosin function in directed vacuole movement during cell division in Saccharomyces cerevisae. J. Cell Biol. 135, 1535-1549 (1996). (Pubitemid 26427650)
    • (1996) Journal of Cell Biology , vol.135 , Issue.6 , pp. 1535-1549
    • Hill, K.L.1    Catlett, N.L.2    Weisman, L.S.3
  • 67
    • 0037422115 scopus 로고    scopus 로고
    • Regulated degradation of a class V myosin receptor directs movement of the yeast vacuole
    • DOI 10.1038/nature01453
    • Tang, F. et al. Regulated degradation of a class V myosin receptor directs movement of the yeast vacuole. Nature 422, 87-92 (2003). (Pubitemid 36323301)
    • (2003) Nature , vol.422 , Issue.6927 , pp. 87-92
    • Tang, F.1    Kauffman, E.J.2    Novak, J.L.3    Nau, J.J.4    Catlett, N.L.5    Weisman, L.S.6
  • 68
    • 51449106266 scopus 로고    scopus 로고
    • The cyclin-dependent kinase cdk1 directly regulates vacuole inheritance
    • Peng, Y. & Weisman, L. S. The cyclin-dependent kinase Cdk1 directly regulates vacuole inheritance. Dev. Cell 15, 478-485 (2008).
    • (2008) Dev. Cell , vol.15 , pp. 478-485
    • Peng, Y.1    Weisman, L.S.2
  • 69
    • 33646093006 scopus 로고    scopus 로고
    • The peroxisomal membrane protein inp2p is the peroxisome-specific receptor for the myosin v motor myo2p of saccharomyces cerevisiae
    • Fagarasanu, A., Fagarasanu, M., Eitzen, G. A., Aitchison, J. D. & Rachubinski, R. A. The peroxisomal membrane protein Inp2p is the peroxisome-specific receptor for the myosin V motor Myo2p of Saccharomyces cerevisiae. Dev. Cell 10, 587-600 (2006).
    • (2006) Dev. Cell , vol.10 , pp. 587-600
    • Fagarasanu, A.1    Fagarasanu, M.2    Eitzen, G.A.3    Aitchison, J.D.4    Rachubinski, R.A.5
  • 70
    • 70449733045 scopus 로고    scopus 로고
    • Pex3 peroxisome biogenesis proteins function in peroxisome inheritance as class v myosin receptors
    • Chang, J. et al. Pex3 peroxisome biogenesis proteins function in peroxisome inheritance as class V myosin receptors. J. Cell Biol. 187, 233-246 (2009).
    • (2009) J. Cell Biol. , vol.187 , pp. 233-246
    • Chang, J.1
  • 71
    • 69449104537 scopus 로고    scopus 로고
    • Myosin-driven peroxisome partitioning in s. cerevisiae
    • Fagarasanu, A. et al. Myosin-driven peroxisome partitioning in S. cerevisiae. J. Cell Biol. 186, 541-554 (2009).
    • (2009) J. Cell Biol. , vol.186 , pp. 541-554
    • Fagarasanu, A.1
  • 72
    • 22344452004 scopus 로고    scopus 로고
    • Inp1p is a peroxisomal membrane protein required for peroxisome inheritance in Saccharomyces cerevisiae
    • DOI 10.1083/jcb.200503083
    • Fagarasanu, M., Fagarasanu, A., Tam, Y. Y., Aitchison, J. D. & Rachubinski, R. A. Inp1p is a peroxisomal membrane protein required for peroxisome inheritance in Saccharomyces cerevisiae. J. Cell Biol. 169, 765-775 (2005). (Pubitemid 41002882)
    • (2005) Journal of Cell Biology , vol.169 , Issue.5 , pp. 765-775
    • Fagarasanu, M.1    Fagarasanu, A.2    Tam, Y.Y.C.3    Aitchison, J.D.4    Rachubinski, R.A.5
  • 73
    • 0029914986 scopus 로고    scopus 로고
    • Asymmetric accumulation of Ash1p in postanaphase nuclei depends on a myosin and restricts yeast mating-type switching to mother cells
    • DOI 10.1016/S0092-8674(00)81048-X
    • Bobola, N., Jansen, R. P., Shin, T. H. & Nasmyth, K. Asymmetric accumulation of ASH1p in postanaphase nuclei depends on a myosin and restricts yeast mating-type switching to mother cells. Cell 84, 699-709 (1996). (Pubitemid 26094200)
    • (1996) Cell , vol.84 , Issue.5 , pp. 699-709
    • Bobola, N.1    Jansen, R.-P.2    Shin, T.H.3    Nasmyth, K.4
  • 74
    • 0030930836 scopus 로고    scopus 로고
    • Actin-dependent localization of an RNA encoding a cell-fate determinant in the yeast
    • DOI 10.1038/38015
    • Takizawa, P. A., Sil, A., Swedlow, J. R., Herskowitz, I. & Vale, R. D. Actin-dependent localization of an RNA encoding a cell-fate determinant in yeast. Nature 389, 90-93 (1997). (Pubitemid 27387697)
    • (1997) Nature , vol.389 , Issue.6646 , pp. 90-93
    • Takizawa, P.A.1    Sil, A.2    Swedlow, J.R.3    Herskowitz, I.4    Vale, R.D.5
  • 77
    • 77952327377 scopus 로고    scopus 로고
    • Multiple myo4 motors enhance ash1 mrna transport in saccharomyces cerevisiae
    • Chung, S. & Takizawa, P. A. Multiple Myo4 motors enhance ASH1 mRNA transport in Saccharomyces cerevisiae. J. Cell Biol. 189, 755-767 (2010).
    • (2010) J. Cell Biol. , vol.189 , pp. 755-767
    • Chung, S.1    Takizawa, P.A.2
  • 78
    • 0034406803 scopus 로고    scopus 로고
    • She2p is a novel rna-binding protein that recruits the myo4p-she3p complex to ash1 mrna
    • Long, R. M., Gu, W., Lorimer, E., Singer, R. H. & Chartrand, P. She2p is a novel RNA-binding protein that recruits the Myo4p-She3p complex to ASH1 mRNA. EMBO J. 19, 6592-6601 (2000).
    • (2000) EMBO J , vol.19 , pp. 6592-6601
    • Long, R.M.1    Gu, W.2    Lorimer, E.3    Singer, R.H.4    Chartrand, P.5
  • 80
    • 33751428390 scopus 로고    scopus 로고
    • Myosin-Va Facilitates the Accumulation of mRNA/Protein Complex in Dendritic Spines
    • DOI 10.1016/j.cub.2006.10.024, PII S0960982206023608
    • Yoshimura, A. et al. Myosin-Va facilitates the accumulation of mRNA/protein complex in dendritic spines. Curr. Biol. 16, 2345-2351 (2006). (Pubitemid 44821840)
    • (2006) Current Biology , vol.16 , Issue.23 , pp. 2345-2351
    • Yoshimura, A.1    Fujii, R.2    Watanabe, Y.3    Okabe, S.4    Fukui, K.5    Takumi, T.6
  • 81
    • 67349097349 scopus 로고    scopus 로고
    • Myosin-V regulates Oskar mRNA localization in the Drosophila oocyte
    • Krauss, J., Lopez de, Q. S., Nusslein-Volhard, C. & Ephrussi, A. Myosin-V regulates Oskar mRNA localization in the Drosophila oocyte. Curr. Biol. 19, 1058-1063 (2009).
    • (2009) Curr. Biol. , vol.19 , pp. 1058-1063
    • Krauss, J.1    Lopezde, Q.S.2    Nusslein-Volhard, C.3    Ephrussi, A.4
  • 83
    • 0036198747 scopus 로고    scopus 로고
    • Endoplasmic reticulum dynamics, inheritance, and cytoskeletal interactions in budding yeast
    • DOI 10.1091/mbc.01-04-0184
    • Fehrenbacher, K. L., Davis, D., Wu, M., Boldogh, I. & Pon, L. A. Endoplasmic reticulum dynamics, inheritance, and cytoskeletal interactions in budding yeast. Mol. Biol. Cell 13, 854-865 (2002). (Pubitemid 34250351)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.3 , pp. 854-865
    • Fehrenbacher, K.L.1    Davis, D.2    Wu, M.3    Boldogh, I.4    Pon, L.A.5
  • 84
    • 33746546711 scopus 로고    scopus 로고
    • Coordination of Endoplasmic Reticulum and mRNA Localization to the Yeast Bud
    • DOI 10.1016/j.cub.2006.06.025, PII S0960982206017520
    • Schmid, M., Jaedicke, A., Du, T. G. & Jansen, R. P. Coordination of endoplasmic reticulum and mRNA localization to the yeast bud. Curr. Biol. 16, 1538-1543 (2006). (Pubitemid 44142979)
    • (2006) Current Biology , vol.16 , Issue.15 , pp. 1538-1543
    • Schmid, M.1    Jaedicke, A.2    Du, T.-G.3    Jansen, R.-P.4
  • 85
    • 69449093702 scopus 로고    scopus 로고
    • The dictyostelium type v myosin myoj is responsible for the cortical association and motility of contractile vacuole membranes
    • Jung, G., Titus, M. A. & Hammer, J. A. III. The Dictyostelium type V myosin MyoJ is responsible for the cortical association and motility of contractile vacuole membranes. J. Cell Biol. 186, 555-570 (2009).
    • (2009) J. Cell Biol. , vol.186 , pp. 555-570
    • Jung, G.1    Titus, M.A.2    Hammer III, J.A.3
  • 86
    • 45849090722 scopus 로고    scopus 로고
    • Calcium-activated myosin v closes the drosophila pupil
    • Satoh, A. K., Li, B. X., Xia, H. & Ready, D. F. Calcium-activated Myosin V closes the Drosophila pupil. Curr. Biol. 18, 951-955 (2008).
    • (2008) Curr. Biol. , vol.18 , pp. 951-955
    • Satoh, A.K.1    Li, B.X.2    Xia, H.3    Ready, D.F.4
  • 87
    • 34249100238 scopus 로고    scopus 로고
    • Myosin V, Rab11, and dRip11 direct apical secretion and cellular morphogenesis in developing Drosophila photoreceptors
    • DOI 10.1083/jcb.200610157
    • Li, B. X., Satoh, A. K. & Ready, D. F. Myosin V, Rab11, and dRip11 direct apical secretion and cellular morphogenesis in developing Drosophila photoreceptors. J. Cell Biol. 177, 659-669 (2007). (Pubitemid 46799837)
    • (2007) Journal of Cell Biology , vol.177 , Issue.4 , pp. 659-669
    • Li, B.X.1    Satoh, A.K.2    Ready, D.F.3
  • 88
    • 66349129521 scopus 로고    scopus 로고
    • Unconventional myosins acting unconventionally
    • Woolner, S. & Bement, W. M. Unconventional myosins acting unconventionally. Trends Cell Biol. 19, 245-252 (2009).
    • (2009) Trends Cell Biol , vol.19 , pp. 245-252
    • Woolner, S.1    Bement, W.M.2
  • 89
    • 0028942256 scopus 로고
    • Actin-and microtubule-dependent organelle motors: Interrelationships between the two motility systems
    • Langford, G. M. Actin-and microtubule-dependent organelle motors: interrelationships between the two motility systems. Curr. Opin. Cell Biol. 7, 82-88 (1995).
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 82-88
    • Langford, G.M.1
  • 91
    • 0036107354 scopus 로고    scopus 로고
    • Melanophilin, the product of the leaden locus, is required for targeting of myosin-Va to melanosomes
    • DOI 10.1034/j.1600-0854.2002.030205.x
    • Provance, D. W., James, T. L. & Mercer, J. A. Melanophilin, the product of the leaden locus, is required for targeting of myosin-Va to melanosomes. Traffic. 3, 124-132 (2002). (Pubitemid 34555470)
    • (2002) Traffic , vol.3 , Issue.2 , pp. 124-132
    • Provance Jr., D.W.1    James, T.L.2    Mercer, J.A.3
  • 92
    • 0032576622 scopus 로고    scopus 로고
    • Visualization of melanosome dynamics within wild-type and dilute melanocytes suggests a paradigm for myosin v function in vivo
    • DOI 10.1083/jcb.143.7.1899
    • Wu, X., Bowers, B., Rao, K., Wei, Q. & Hammer, J. A. III. Visualization of melanosome dynamics within wild-type and dilute melanocytes suggests a paradigm for myosin V function in vivo. J. Cell Biol. 143, 1899-1918 (1998). (Pubitemid 29022612)
    • (1998) Journal of Cell Biology , vol.143 , Issue.7 , pp. 1899-1918
    • Wu, X.1    Bowers, B.2    Rao, K.3    Wei, Q.4    Hammer III, J.A.5
  • 94
    • 0032576766 scopus 로고    scopus 로고
    • Functional coordination of microtubule-based and actin-based motility in melanophores
    • Rodionov, V. I., Hope, A. J., Svitkina, T. M. & Borisy, G. G. Functional coordination of microtubule-based and actin-based motility in melanophores. Curr. Biol. 8, 165-168 (1998). (Pubitemid 28091575)
    • (1998) Current Biology , vol.8 , Issue.3 , pp. 165-168
    • Rodionov, V.I.1    Hope, A.J.2    Svitkina, T.M.3    Borisy, G.G.4
  • 95
    • 0032576778 scopus 로고    scopus 로고
    • Myosin cooperates with microtubule motors during organelle transport in melanophores
    • Rogers, S. L. & Gelfand, V. I. Myosin cooperates with microtubule motors during organelle transport in melanophores. Curr. Biol. 8, 161-164 (1998). (Pubitemid 28091574)
    • (1998) Current Biology , vol.8 , Issue.3 , pp. 161-164
    • Rogers, S.L.1    Gelfand, V.I.2
  • 96
    • 0033588979 scopus 로고    scopus 로고
    • Regulation of melanosome movement in the cell cycle by reversible association with myosin v
    • Rogers, S. L. et al. Regulation of melanosome movement in the cell cycle by reversible association with myosin V. J. Cell Biol. 146, 1265-1276 (1999).
    • (1999) J. Cell Biol. , vol.146 , pp. 1265-1276
    • Rogers, S.L.1
  • 97
    • 54149090797 scopus 로고    scopus 로고
    • Actin dynamics is essential for myosin-based transport of membrane organelles
    • Semenova, I. et al. Actin dynamics is essential for myosin-based transport of membrane organelles. Curr. Biol. 18, 1581-1586 (2008).
    • (2008) Curr. Biol. , vol.18 , pp. 1581-1586
    • Semenova, I.1
  • 100
    • 0037184989 scopus 로고    scopus 로고
    • Rab11 family interacting protein 2 associates with myosin Vb and regulates plasma membrane recycling
    • DOI 10.1074/jbc.M209270200
    • Hales, C. M., Vaerman, J. P. & Goldenring, J. R. Rab11 family interacting protein 2 associates with Myosin Vb and regulates plasma membrane recycling. J. Biol. Chem. 277, 50415-50421 (2002). (Pubitemid 36042193)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.52 , pp. 50415-50421
    • Hales, C.M.1    Vaerman, J.-P.2    Goldenring, J.R.3
  • 101
    • 32344443827 scopus 로고    scopus 로고
    • Interactions of myosin Vb with Rab11 family members and cargoes traversing the plasma membrane recycling system
    • DOI 10.1016/S0076-6879(05)03062-4, PII S0076687905030624, 62, GTPases Regulating Membrane Targeting and Fusion
    • Lapierre, L. A. & Goldenring, J. R. Interactions of myosin Vb with Rab11 family members and cargoes traversing the plasma membrane recycling system. Methods Enzymol. 403, 715-723 (2005). (Pubitemid 43216953)
    • (2005) Methods in Enzymology , vol.403 , pp. 715-723
    • Lapierre, L.A.1    Goldenring, J.R.2
  • 102
    • 77955057326 scopus 로고    scopus 로고
    • Linking molecular motors to membrane cargo
    • Akhmanova, A. & Hammer, J. A. III. Linking molecular motors to membrane cargo. Curr. Opin. Cell Biol. 22, 479-487 (2010).
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 479-487
    • Akhmanova, A.1    Hammer III, J.A.2
  • 103
    • 79952588402 scopus 로고    scopus 로고
    • Rab gtpase-myo5b complexes control membrane recycling and epithelial polarization
    • Roland, J. T. et al. Rab GTPase-Myo5B complexes control membrane recycling and epithelial polarization. Proc. Natl Acad. Sci. USA 108, 2789-2794 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 2789-2794
    • Roland, J.T.1
  • 104
    • 52949112224 scopus 로고    scopus 로고
    • Myo5b mutations cause microvillus inclusion disease and disrupt epithelial cell polarity
    • Muller, T. et al. MYO5B mutations cause microvillus inclusion disease and disrupt epithelial cell polarity. Nature Genet. 40, 1163-1165 (2008).
    • (2008) Nature Genet , vol.40 , pp. 1163-1165
    • Muller, T.1
  • 105
    • 4644287672 scopus 로고    scopus 로고
    • Recycling endosomes supply AMPA receptors for LTP
    • DOI 10.1126/science.1102026
    • Park, M., Penick, E. C., Edwards, J. G., Kauer, J. A. & Ehlers, M. D. Recycling endosomes supply AMPA receptors for LTP. Science 305, 1972-1975 (2004). (Pubitemid 39287999)
    • (2004) Science , vol.305 , Issue.5692 , pp. 1972-1975
    • Park, M.1    Penick, E.C.2    Edwards, J.G.3    Kauer, J.A.4    Ehlers, M.D.5
  • 106
    • 54549123514 scopus 로고    scopus 로고
    • Myosin vb mobilizes recycling endosomes and AMPA receptors for postsynaptic plasticity
    • Wang, Z. et al. Myosin Vb mobilizes recycling endosomes and AMPA receptors for postsynaptic plasticity. Cell 135, 535-548 (2008).
    • (2008) Cell , vol.135 , pp. 535-548
    • Wang, Z.1
  • 109
    • 0035071224 scopus 로고    scopus 로고
    • Hippocampal synaptic transmission and plasticity are preserved in myosin Va mutant mice
    • Schnell, E. & Nicoll, R. A. Hippocampal synaptic transmission and plasticity are preserved in myosin Va mutant mice. J. Neurophysiol. 85, 1498-1501 (2001). (Pubitemid 32280590)
    • (2001) Journal of Neurophysiology , vol.85 , Issue.4 , pp. 1498-1501
    • Schnell, E.1    Nicoll, R.A.2
  • 112
    • 0033636896 scopus 로고    scopus 로고
    • Local calcium release in dendritic spines required for long-term synaptic depression
    • Miyata, M. et al. Local calcium release in dendritic spines required for long-term synaptic depression. Neuron 28, 233-244 (2000).
    • (2000) Neuron , vol.28 , pp. 233-244
    • Miyata, M.1
  • 113
    • 78650515235 scopus 로고    scopus 로고
    • Myosin-va transports the endoplasmic reticulum into the dendritic spines of purkinje neurons
    • Wagner, W., Brenowitz, S. D. & Hammer, J. A. III. Myosin-Va transports the endoplasmic reticulum into the dendritic spines of Purkinje neurons. Nature Cell Biol. 13, 40-48 (2011).
    • (2011) Nature Cell Biol , vol.13 , pp. 40-48
    • Wagner, W.1    Brenowitz, S.D.2    Hammer III, J.A.3
  • 114
    • 70149094616 scopus 로고    scopus 로고
    • Cell and molecular biology of the fastest myosins
    • Higashi-Fujime, S. & Nakamura, A. Cell and molecular biology of the fastest myosins. Int. Rev. Cell Mol. Biol. 276, 301-347 (2009).
    • (2009) Int. Rev. Cell Mol. Biol. , vol.276 , pp. 301-347
    • Higashi-Fujime, S.1    Nakamura, A.2
  • 115
    • 77949542561 scopus 로고    scopus 로고
    • Cytoplasmic streaming enables the distribution of molecules and vesicles in large plant cells
    • Verchot-Lubicz, J. & Goldstein, R. E. Cytoplasmic streaming enables the distribution of molecules and vesicles in large plant cells. Protoplasma 240, 99-107 (2010).
    • (2010) Protoplasma , vol.240 , pp. 99-107
    • Verchot-Lubicz, J.1    Goldstein, R.E.2
  • 116
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • DOI 10.1016/S0092-8674(03)00120-X
    • Pollard, T. D. & Borisy, G. G. Cellular motility driven by assembly and disassembly of actin filaments. Cell 11 2, 453-465 (2003). (Pubitemid 36263079)
    • (2003) Cell , vol.112 , Issue.4 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 118
    • 77953149779 scopus 로고    scopus 로고
    • Distinct roles of myosin va in membrane remodeling and exocytosis of secretory granules
    • Kogel, T. et al. Distinct roles of myosin Va in membrane remodeling and exocytosis of secretory granules. Traffic. 11, 637-650 (2010).
    • (2010) Traffic , vol.11 , pp. 637-650
    • Kogel, T.1
  • 119
    • 68949125193 scopus 로고    scopus 로고
    • Random walk of processive, quantum dot-labeled myosin va molecules within the actin cortex of cos-7 cells
    • Nelson, S. R., Ali, M. Y., Trybus, K. M. & Warshaw, D. M. Random walk of processive, quantum dot-labeled myosin Va molecules within the actin cortex of COS-7 cells. Biophys. J. 97, 509-518 (2009).
    • (2009) Biophys. J. , vol.97 , pp. 509-518
    • Nelson, S.R.1    Ali, M.Y.2    Trybus, K.M.3    Warshaw, D.M.4
  • 120
    • 68049143191 scopus 로고    scopus 로고
    • Velocity, processivity, and individual steps of single myosin v molecules in live cells
    • Pierobon, P. et al. Velocity, processivity, and individual steps of single myosin V molecules in live cells. Biophys. J. 96, 4268-4275 (2009).
    • (2009) Biophys. J. , vol.96 , pp. 4268-4275
    • Pierobon, P.1
  • 121
    • 78049255279 scopus 로고    scopus 로고
    • Dicing with dogma: de-branching the lamellipodium
    • Small, J. V. Dicing with dogma: de-branching the lamellipodium. Trends Cell Biol. 20, 628-633 (2010).
    • (2010) Trends Cell Biol , vol.20 , pp. 628-633
    • Small, J.V.1
  • 122
    • 76449102375 scopus 로고    scopus 로고
    • Versatile roles for myosin va in dense core vesicle biogenesis and function
    • Kogel, T., Bittins, C. M., Rudolf, R. & Gerdes, H. H. Versatile roles for myosin Va in dense core vesicle biogenesis and function. Biochem. Soc. Trans. 38, 199-204 (2010).
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 199-204
    • Kogel, T.1    Bittins, C.M.2    Rudolf, R.3    Gerdes, H.H.4
  • 123
    • 34547986066 scopus 로고    scopus 로고
    • 'Should I stay or should I go?': Myosin V function in organelle trafficking
    • DOI 10.1042/BC20070021
    • Desnos, C., Huet, S. & Darchen, F. 'Should I stay or should I go?': myosin V function in organelle trafficking. Biol. Cell 99, 411-423 (2007). (Pubitemid 47272224)
    • (2007) Biology of the Cell , vol.99 , Issue.8 , pp. 411-423
    • Desnos, C.1    Huet, S.2    Darchen, F.3
  • 124
    • 34248667614 scopus 로고    scopus 로고
    • Myosins in melanocytes: To move or not to move?
    • DOI 10.1111/j.1600-0749.2007.00376.x
    • Coudrier, E. Myosins in melanocytes: to move or not to move? Pigment Cell Res. 20, 153-160 (2007). (Pubitemid 46776378)
    • (2007) Pigment Cell Research , vol.20 , Issue.3 , pp. 153-160
    • Coudrier, E.1
  • 125
    • 52549110350 scopus 로고    scopus 로고
    • Myosins in the secretory pathway: Tethers or transporters?
    • Loubery, S. & Coudrier, E. Myosins in the secretory pathway: tethers or transporters? Cell. Mol. Life Sci. 65, 2790-2800 (2008).
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 2790-2800
    • Loubery, S.1    Coudrier, E.2
  • 126
    • 51649105426 scopus 로고    scopus 로고
    • Myosin-vb functions as a dynamic tether for peripheral endocytic compartments during transferrin trafficking
    • Provance, D. W. Jr et al. Myosin-Vb functions as a dynamic tether for peripheral endocytic compartments during transferrin trafficking. BMC. Cell Biol. 9, 44 (2008).
    • (2008) BMC. Cell Biol. , vol.9 , pp. 44
    • Provance Jr., D.W.1
  • 128
    • 2542470460 scopus 로고    scopus 로고
    • Slac2-a/melanophilin contains multiple PEST-like sequences that are highly sensitive to proteolysis
    • DOI 10.1074/jbc.401791200
    • Fukuda, M. & Itoh, T. Slac2-a/melanophilin contains multiple PEST-like sequences that are highly sensitive to proteolysis. J. Biol. Chem. 279, 22314-22321 (2004). (Pubitemid 38679428)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.21 , pp. 22314-22321
    • Fukuda, M.1    Itoh, T.2
  • 129
    • 53149101728 scopus 로고    scopus 로고
    • Rab3gep is the non-redundant guanine nucleotide exchange factor for rab27a in melanocytes
    • Figueiredo, A. C. et al. Rab3GEP is the non-redundant guanine nucleotide exchange factor for Rab27a in melanocytes. J. Biol. Chem. 283, 23209-23216 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 23209-23216
    • Figueiredo, A.C.1
  • 130
    • 33845307154 scopus 로고    scopus 로고
    • Identification of EPI64 as a GTPase-activating protein specific for Rab27A
    • DOI 10.1074/jbc.M603808200
    • Itoh, T. & Fukuda, M. Identification of EPI64 as a GTPase-activating protein specific for Rab27A. J. Biol. Chem. 281, 31823-31831 (2006). (Pubitemid 46041447)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.42 , pp. 31823-31831
    • Itoh, T.1    Fukuda, M.2
  • 131
    • 53049099181 scopus 로고    scopus 로고
    • Structural basis for the exclusive specificity of slac2-a/melanophilin for the rab27 gtpases
    • Kukimoto-Niino, M. et al. Structural basis for the exclusive specificity of Slac2-a/melanophilin for the Rab27 GTPases. Structure. 16, 1478-1490 (2008).
    • (2008) Structure , vol.16 , pp. 1478-1490
    • Kukimoto-Niino, M.1
  • 132
    • 1242329406 scopus 로고    scopus 로고
    • Missense mutations in the globular tail of myosin-Va in dilute mice partially impair binding of Slac2-a/melanophilin
    • DOI 10.1242/jcs.00891
    • Fukuda, M. & Kuroda, T. S. Missense mutations in the globular tail of myosin-Va in dilute mice partially impair binding of Slac2-a/melanophilin. J. Cell Sci. 1 1 7, 583-591 (2004). (Pubitemid 38240199)
    • (2004) Journal of Cell Science , vol.117 , Issue.4 , pp. 583-591
    • Fukuda, M.1    Kuroda, T.S.2
  • 134
    • 0043093725 scopus 로고    scopus 로고
    • The actin-binding domain of Slac2-a/melanophilin is required for melanosome distribution in melanocytes
    • DOI 10.1128/MCB.23.15.5245-5255.2003
    • Kuroda, T. S., Ariga, H. & Fukuda, M. The actin-binding domain of Slac2-a/melanophilin is required for melanosome distribution in melanocytes. Mol. Cell. Biol. 23, 5245-5255 (2003). (Pubitemid 36950880)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.15 , pp. 5245-5255
    • Kuroda, T.S.1    Ariga, H.2    Fukuda, M.3
  • 135
    • 27544458296 scopus 로고    scopus 로고
    • Melanophilin and myosin Va track the microtubule plus end on EB1
    • DOI 10.1083/jcb.200503028
    • Wu, X. S., Tsan, G. L. & Hammer, J. A. III. Melanophilin and myosin Va track the microtubule plus end on EB1. J. Cell Biol. 171, 201-207 (2005). (Pubitemid 41540013)
    • (2005) Journal of Cell Biology , vol.171 , Issue.2 , pp. 201-207
    • Wu, X.S.1    Tsan, G.L.2    Hammer III, J.A.3
  • 136
    • 34948826453 scopus 로고    scopus 로고
    • Rab27a and MyoVa are the primary Mlph interactors regulating melanosome transport in melanocytes
    • DOI 10.1242/jcs.010207
    • Hume, A. N., Ushakov, D. S., Tarafder, A. K., Ferenczi, M. A. & Seabra, M. C. Rab27a and MyoVa are the primary Mlph interactors regulating melanosome transport in melanocytes. J. Cell Sci. 120, 3111-3122 (2007). (Pubitemid 47517093)
    • (2007) Journal of Cell Science , vol.120 , Issue.17 , pp. 3111-3122
    • Hume, A.N.1    Ushakov, D.S.2    Tarafder, A.K.3    Ferenczi, M.A.4    Seabra, M.C.5
  • 137
    • 33750520133 scopus 로고    scopus 로고
    • A coiled-coil domain of melanophilin is essential for Myosin Va recruitment and melanosome transport in melanocytes
    • DOI 10.1091/mbc.E06-05-0457
    • Hume, A. N., Tarafder, A. K., Ramalho, J. S., Sviderskaya, E. V. & Seabra, M. C. A coiled-coil domain of melanophilin is essential for myosin Va recruitment and melanosome transport in melanocytes. Mol. Biol. Cell 17, 4720-4735 (2006). (Pubitemid 44665742)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.11 , pp. 4720-4735
    • Hume, A.N.1    Tarafder, A.K.2    Ramalho, J.S.3    Sviderskaya, E.V.4    Seabra, M.C.5
  • 138
    • 1642286846 scopus 로고    scopus 로고
    • Myosin V: Regulation by calcium, calmodulin, and the tail domain
    • DOI 10.1083/jcb.200310065
    • Krementsov, D. N., Krementsova, E. B. & Trybus, K. M. Myosin V: regulation by calcium, calmodulin, and the tail domain. J. Cell Biol. 164, 877-886 (2004). (Pubitemid 38366899)
    • (2004) Journal of Cell Biology , vol.164 , Issue.6 , pp. 877-886
    • Krementsov, D.N.1    Krementsova, E.B.2    Trybus, K.M.3
  • 139
    • 1242317813 scopus 로고    scopus 로고
    • 2+-induced activation of ATPase activity of myosin Va is accompanied with a large conformational change
    • DOI 10.1016/j.bbrc.2004.01.084
    • 2+-induced activation of ATPase activity of myosin Va is accompanied with a large conformational change. Biochem. Biophys. Res. Commun. 31 5, 538-545 (2004). (Pubitemid 38229377)
    • (2004) Biochemical and Biophysical Research Communications , vol.315 , Issue.3 , pp. 538-545
    • Li, X.-D.1    Mabuchi, K.2    Ikebe, R.3    Ikebe, M.4
  • 140
    • 0030969912 scopus 로고    scopus 로고
    • Two new Ypt GTPases are required for exit from the yeast trans-Golgi compartment
    • DOI 10.1083/jcb.137.3.563
    • Jedd, G., Mulholland, J. & Segev, N. Two new Ypt GTPases are required for exit from the yeast trans-Golgi compartment. J. Cell Biol. 137, 563-580 (1997). (Pubitemid 27200661)
    • (1997) Journal of Cell Biology , vol.137 , Issue.3 , pp. 563-580
    • Jedd, G.1    Mulholland, J.2    Segev, N.3
  • 141
    • 0028820010 scopus 로고
    • The ypt1 gtpase is essential for the first two steps of the yeast secretory pathway
    • Jedd, G., Richardson, C., Litt, R. & Segev, N. The Ypt1 GTPase is essential for the first two steps of the yeast secretory pathway. J. Cell Biol. 131, 583-590 (1995).
    • (1995) J. Cell Biol. , vol.131 , pp. 583-590
    • Jedd, G.1    Richardson, C.2    Litt, R.3    Segev, N.4
  • 142
    • 33644548665 scopus 로고    scopus 로고
    • Structural basis for myosin V discrimination between distinct cargoes
    • DOI 10.1038/sj.emboj.7600965, PII 7600965
    • Pashkova, N., Jin, Y., Ramaswamy, S. & Weisman, L. S. Structural basis for myosin V discrimination between distinct cargoes. EMBO J. 25, 693-700 (2006). (Pubitemid 43292432)
    • (2006) EMBO Journal , vol.25 , Issue.4 , pp. 693-700
    • Pashkova, N.1    Jin, Y.2    Ramaswamy, S.3    Weisman, L.S.4
  • 143
    • 9244232349 scopus 로고    scopus 로고
    • Molecular motors: Strategies to get along
    • DOI 10.1016/j.cub.2004.10.046, PII S0960982204008516
    • Mallik, R. & Gross, S. P. Molecular motors: strategies to get along. Curr. Biol. 14, R971-R982 (2004). (Pubitemid 39547951)
    • (2004) Current Biology , vol.14 , Issue.22
    • Mallik, R.1    Gross, S.P.2
  • 144
    • 77952334420 scopus 로고    scopus 로고
    • Actin in dendritic spines: Connecting dynamics to function
    • Hotulainen, P. & Hoogenraad, C. C. Actin in dendritic spines: connecting dynamics to function. J. Cell Biol. 189, 619-629 (2010).
    • (2010) J. Cell Biol. , vol.189 , pp. 619-629
    • Hotulainen, P.1    Hoogenraad, C.C.2
  • 145
    • 75649108232 scopus 로고    scopus 로고
    • Molecular architecture of synaptic actin cytoskeleton in hippocampal neurons reveals a mechanism of dendritic spine morphogenesis
    • Korobova, F. & Svitkina, T. Molecular architecture of synaptic actin cytoskeleton in hippocampal neurons reveals a mechanism of dendritic spine morphogenesis. Mol. Biol. Cell 21, 165-176 (2010).
    • (2010) Mol. Biol. Cell , vol.21 , pp. 165-176
    • Korobova, F.1    Svitkina, T.2
  • 146
    • 77957018107 scopus 로고    scopus 로고
    • A network of networks: Cytoskeletal control of compartmentalized function within dendritic spines
    • Frost, N. A., Kerr, J. M., Lu, H. E. & Blanpied, T. A. A network of networks: cytoskeletal control of compartmentalized function within dendritic spines. Curr. Opin. Neurobiol. 20, 578-587 (2010).
    • (2010) Curr. Opin. Neurobiol. , vol.20 , pp. 578-587
    • Frost, N.A.1    Kerr, J.M.2    Lu, H.E.3    Blanpied, T.A.4


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