메뉴 건너뛰기




Volumn 288, Issue 41, 2013, Pages 29313-29322

More than just a cargo adapter, melanophilin prolongs and slows processive runs of myosin Va

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN-BINDING DOMAINS; ACTIVATION MECHANISMS; ADAPTER PROTEINS; DENDRITIC PERIPHERY; MOLECULAR MOTORS; POSITIVELY CHARGED; SINGLE MOLECULE LEVEL; TOTAL INTERNAL REFLECTION FLUORESCENCE MICROSCOPY;

EID: 84885671133     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.476929     Document Type: Article
Times cited : (35)

References (47)
  • 1
    • 73349109510 scopus 로고    scopus 로고
    • Actin and microtubule-based cytoskeletal cues direct polarized targeting of proteins in neurons
    • Arnold, D. B. (2009) Actin and microtubule-based cytoskeletal cues direct polarized targeting of proteins in neurons. Sci. Signal. 2, pe49
    • (2009) Sci. Signal , vol.2
    • Arnold, D.B.1
  • 2
    • 80053359163 scopus 로고    scopus 로고
    • Melanosomes on the move: A model to understand organelle dynamics
    • Hume, A. N., and Seabra, M. C. (2011) Melanosomes on the move: a model to understand organelle dynamics. Biochem. Soc. Trans. 39, 1191-1196
    • (2011) Biochem. Soc. Trans , vol.39 , pp. 1191-1196
    • Hume, A.N.1    Seabra, M.C.2
  • 3
    • 0032576622 scopus 로고    scopus 로고
    • Visualization of melanosome dynamics within wild-type and dilute melanocytes suggests a paradigm for myosin v function in vivo
    • Wu, X., Bowers, B., Rao, K., Wei, Q., and Hammer, J. A. (1998) 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) J. Cell Biol , vol.143 , pp. 1899-1918
    • Wu, X.1    Bowers, B.2    Rao, K.3    Wei, Q.4    Hammer, J.A.5
  • 4
    • 27544458296 scopus 로고    scopus 로고
    • Melanophilin and myosin Va track the microtubule plus end on EB1
    • Wu, X. S., Tsan, G. L., and Hammer, J. A. (2005) Melanophilin and myosin Va track the microtubule plus end on EB1. J. Cell Biol. 171, 201-207
    • (2005) J. Cell Biol , vol.171 , pp. 201-207
    • Wu, X.S.1    Tsan, G.L.2    Hammer, J.A.3
  • 5
    • 0035490904 scopus 로고    scopus 로고
    • The melanosome: Membrane dynamics in black and white
    • Marks, M. S., and Seabra, M. C. (2001) The melanosome: membrane dynamics in black and white. Nat. Rev. Mol. Cell Biol. 2, 738-748
    • (2001) Nat. Rev. Mol. Cell Biol , vol.2 , pp. 738-748
    • Marks, M.S.1    Seabra, M.C.2
  • 6
    • 0035073174 scopus 로고    scopus 로고
    • Rab27a enables myosin Va-dependent melanosome capture by recruiting the myosin to the organelle
    • Wu, X., Rao, K., Bowers, M. B., Copeland, N. G., Jenkins, N. A., and Hammer, J. A. (2001) Rab27a enables myosin Va-dependent melanosome capture by recruiting the myosin to the organelle. J. Cell Sci. 114, 1091-1100
    • (2001) J. Cell Sci , vol.114 , pp. 1091-1100
    • Wu, X.1    Rao, K.2    Bowers, M.B.3    Copeland, N.G.4    Jenkins, N.A.5    Hammer, J.A.6
  • 8
    • 43049183000 scopus 로고    scopus 로고
    • Myosin v from head to tail
    • Trybus, K. M. (2008) Myosin V from head to tail. Cell. Mol. Life Sci. 65, 1378-1389
    • (2008) Cell. Mol. Life Sci , vol.65 , pp. 1378-1389
    • Trybus, K.M.1
  • 11
    • 0025967015 scopus 로고
    • Novel myosin heavy-chain encoded by murine dilute coat color locus
    • Mercer, J. A., Seperack, P. K., Strobel, M. C., Copeland, N. G., and Jenkins, N. A. (1991) Novel myosin heavy-chain encoded by murine dilute coat color locus. Nature 349, 709-713
    • (1991) Nature , vol.349 , pp. 709-713
    • Mercer, J.A.1    Seperack, P.K.2    Strobel, M.C.3    Copeland, N.G.4    Jenkins, N.A.5
  • 12
    • 33644548665 scopus 로고    scopus 로고
    • Structural basis for myosin v discrimination between distinct cargoes
    • Pashkova, N., Jin, Y., Ramaswamy, S., and Weisman, L. S. (2006) Structural basis for myosin V discrimination between distinct cargoes. EMBO J. 25, 693-700
    • (2006) EMBO J , vol.25 , pp. 693-700
    • Pashkova, N.1    Jin, Y.2    Ramaswamy, S.3    Weisman, L.S.4
  • 13
    • 0036000020 scopus 로고    scopus 로고
    • Rab27a is an essential component of melanosome receptor for myosin Va
    • Wu, X., Wang, F., Rao, K., Sellers, J. R., and Hammer, J. A., 3rd (2002) Rab27a is an essential component of melanosome receptor for myosin Va. Mol. Biol. Cell 13, 1735-1749
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1735-1749
    • Wu, X.1    Wang, F.2    Rao, K.3    Sellers, J.R.4    Hammer III, J.A.5
  • 14
    • 33746152398 scopus 로고    scopus 로고
    • The cargo binding domain regulates structure and activity of myosin 5
    • Thirumurugan, K., Sakamoto, T., Hammer, J. A., 3rd, Sellers, J. R., and Knight, P. J. (2006) The cargo binding domain regulates structure and activity of myosin 5. Nature 442, 212-215
    • (2006) Nature , vol.442 , pp. 212-215
    • Thirumurugan, K.1    Sakamoto, T.2    Hammer III, J.A.3    Sellers, J.R.4    Knight, P.J.5
  • 15
    • 33746129173 scopus 로고    scopus 로고
    • Three-dimensional structure of the myosin V-inhibited state by cryoelectron tomography
    • Liu, J., Taylor, D. W., Krementsova, E. B., Trybus, K. M., and Taylor, K. A. (2006) Three-dimensional structure of the myosin V-inhibited state by cryoelectron tomography. Nature 442, 208-211
    • (2006) Nature , vol.442 , pp. 208-211
    • Liu, J.1    Taylor, D.W.2    Krementsova, E.B.3    Trybus, K.M.4    Taylor, K.A.5
  • 16
    • 39549107553 scopus 로고    scopus 로고
    • The globular tail domain puts on the brake to stop the ATPase cycle of myosin Va
    • Li, X. D., Jung, H. S., Wang, Q., Ikebe, R., Craig, R., and Ikebe, M. (2008) The globular tail domain puts on the brake to stop the ATPase cycle of myosin Va. Proc. Natl. Acad. Sci. U.S.A. 105, 1140-1145
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 1140-1145
    • Li, X.D.1    Jung, H.S.2    Wang, Q.3    Ikebe, R.4    Craig, R.5    Ikebe, M.6
  • 17
    • 1642286846 scopus 로고    scopus 로고
    • Myosin V: Regulation by calcium, calmodulin, and the tail domain
    • Krementsov, D. N., Krementsova, E. B., and Trybus, K. M. (2004) Myosin V: regulation by calcium, calmodulin, and the tail domain. J. Cell Biol. 164, 877-886
    • (2004) J. Cell Biol , vol.164 , pp. 877-886
    • Krementsov, D.N.1    Krementsova, E.B.2    Trybus, K.M.3
  • 20
    • 0037165662 scopus 로고    scopus 로고
    • Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions
    • Nagashima, K., Torii, S., Yi, Z., Igarashi, M., Okamoto, K., Takeuchi, T., and Izumi, T. (2002) Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions. FEBS Lett. 517, 233-238
    • (2002) FEBS Lett , vol.517 , pp. 233-238
    • Nagashima, K.1    Torii, S.2    Yi, Z.3    Igarashi, M.4    Okamoto, K.5    Takeuchi, T.6    Izumi, T.7
  • 22
    • 34547126025 scopus 로고    scopus 로고
    • Identification of a minimal myosin Va binding site within an intrinsically unstructured domain of melanophilin
    • Geething, N. C., and Spudich, J. A. (2007) Identification of a minimal myosin Va binding site within an intrinsically unstructured domain of melanophilin. J. Biol. Chem. 282, 21518-21528
    • (2007) J. Biol. Chem , vol.282 , pp. 21518-21528
    • Geething, N.C.1    Spudich, J.A.2
  • 23
    • 1242329406 scopus 로고    scopus 로고
    • Missense mutations in the globular tail of myosin-Va in dilute mice partially impair binding of Slac2-a/melanophilin
    • Fukuda, M., and Kuroda, T. S. (2004) Missense mutations in the globular tail of myosin-Va in dilute mice partially impair binding of Slac2-a/melanophilin. J. Cell Sci. 117, 583-591
    • (2004) J. Cell Sci , vol.117 , pp. 583-591
    • Fukuda, M.1    Kuroda, T.S.2
  • 24
    • 33750520133 scopus 로고    scopus 로고
    • A coiled-coil domain of melanophilin is essential for myosin Va recruitment and melanosome transport in melanocytes
    • Hume, A. N., Tarafder, A. K., Ramalho, J. S., Sviderskaya, E. V., and Seabra, M. C. (2006) A coiled-coil domain of melanophilin is essential for myosin Va recruitment and melanosome transport in melanocytes. Mol. Biol. Cell 17, 4720-4735
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4720-4735
    • Hume, A.N.1    Tarafder, A.K.2    Ramalho, J.S.3    Sviderskaya, E.V.4    Seabra, M.C.5
  • 25
    • 0037044819 scopus 로고    scopus 로고
    • Slac2-c (synaptotagmin-like protein homologue lacking C2 domains-c), a novel linker protein that interacts with Rab27, myosin Va/VIIa, and actin
    • Fukuda, M., and Kuroda, T. S. (2002) Slac2-c (synaptotagmin-like protein homologue lacking C2 domains-c), a novel linker protein that interacts with Rab27, myosin Va/VIIa, and actin. J. Biol. Chem. 277, 43096-43103
    • (2002) J. Biol. Chem , vol.277 , pp. 43096-43103
    • Fukuda, M.1    Kuroda, T.S.2
  • 26
    • 0043093725 scopus 로고    scopus 로고
    • The actin binding domain of Slac2 - A/melanophilin is required for melanosome distribution in melanocytes
    • Kuroda, T. S., Ariga, H., and Fukuda, M. (2003) The actin binding domain of Slac2-a/melanophilin is required for melanosome distribution in melanocytes. Mol. Cell. Biol. 23, 5245-5255
    • (2003) Mol. Cell. Biol , vol.23 , pp. 5245-5255
    • Kuroda, T.S.1    Ariga, H.2    Fukuda, M.3
  • 27
    • 84859582076 scopus 로고    scopus 로고
    • Posttranslational modifications of Rab GTPases help their insertion into membranes
    • Pylypenko, O., and Goud, B. (2012) Posttranslational modifications of Rab GTPases help their insertion into membranes. Proc. Natl. Acad. Sci. U.S.A. 109, 5555-5556
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 5555-5556
    • Pylypenko, O.1    Goud, B.2
  • 28
    • 33750054102 scopus 로고    scopus 로고
    • In vitro reconstitution of a transport complex containing Rab27a, melanophilin and myosin Va
    • Wu, X., Sakamoto, T., Zhang, F., Sellers, J. R., and Hammer, J. A., 3rd (2006) In vitro reconstitution of a transport complex containing Rab27a, melanophilin and myosin Va. FEBS Lett. 580, 5863-5868
    • (2006) FEBS Lett , vol.580 , pp. 5863-5868
    • Wu, X.1    Sakamoto, T.2    Zhang, F.3    Sellers, J.R.4    Hammer III, J.A.5
  • 29
    • 0034654352 scopus 로고    scopus 로고
    • A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions
    • Philo, J. S. (2000) A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions. Anal. Biochem. 279, 151-163
    • (2000) Anal. Biochem , vol.279 , pp. 151-163
    • Philo, J.S.1
  • 30
    • 26444477373 scopus 로고    scopus 로고
    • Automatic tracking of individual fluorescence particles: Application to the study of chromosome dynamics
    • Sage, D., Neumann, F. R., Hediger, F., Gasser, S. M., and Unser, M. (2005) Automatic tracking of individual fluorescence particles: application to the study of chromosome dynamics. IEEE Trans. Image Process. 14, 1372-1383
    • (2005) IEEE Trans. Image Process , vol.14 , pp. 1372-1383
    • Sage, D.1    Neumann, F.R.2    Hediger, F.3    Gasser, S.M.4    Unser, M.5
  • 31
    • 33845382806 scopus 로고
    • Nonparametric estimation from incomplete observations
    • Kaplan, E. L., and Meier, P. (1958) Nonparametric estimation from incomplete observations. J. Am. Stat. Assoc. 53, 457-481
    • (1958) J. Am. Stat. Assoc , vol.53 , pp. 457-481
    • Kaplan, E.L.1    Meier, P.2
  • 33
    • 0020021878 scopus 로고
    • Purification of muscle actin
    • Pardee, J. D., and Spudich, J. A. (1982) Purification of muscle actin. Methods Enzymol. 85, 164-181
    • (1982) Methods Enzymol , vol.85 , pp. 164-181
    • Pardee, J.D.1    Spudich, J.A.2
  • 35
    • 4444384544 scopus 로고    scopus 로고
    • Nanometer localization of single green fluorescent proteins: Evidence that myosinVwalks hand-over-hand via telemark configuration
    • Snyder, G. E., Sakamoto, T., Hammer, J. A., 3rd, Sellers, J. R., and Selvin, P. R. (2004) Nanometer localization of single green fluorescent proteins: evidence that myosinVwalks hand-over-hand via telemark configuration. Biophys. J. 87, 1776-1783
    • (2004) Biophys. J , vol.87 , pp. 1776-1783
    • Snyder, G.E.1    Sakamoto, T.2    Hammer III, J.A.3    Sellers, J.R.4    Selvin, P.R.5
  • 36
    • 28944449570 scopus 로고    scopus 로고
    • Step-size is determined by neck length in myosin v
    • Sakamoto, T., Yildez, A., Selvin, P. R., and Sellers, J. R. (2005) Step-size is determined by neck length in myosin V. Biochemistry 44, 16203-16210
    • (2005) Biochemistry , vol.44 , pp. 16203-16210
    • Sakamoto, T.1    Yildez, A.2    Selvin, P.R.3    Sellers, J.R.4
  • 37
    • 17844385071 scopus 로고    scopus 로고
    • Differential labeling of myosin v heads with quantum dots allows direct visualization of hand-over-hand processivity
    • Warshaw, D. M., Kennedy, G. G., Work, S. S., Krementsova, E. B., Beck, S., and Trybus, K. M. (2005) Differential labeling of myosin V heads with quantum dots allows direct visualization of hand-over-hand processivity. Biophys. J. 88, L30-32
    • (2005) Biophys. J , vol.88
    • Warshaw, D.M.1    Kennedy, G.G.2    Work, S.S.3    Krementsova, E.B.4    Beck, S.5    Trybus, K.M.6
  • 38
    • 70349973366 scopus 로고    scopus 로고
    • Anomalous dynamics of melanosomes driven by myosin-V in Xenopus laevis melanophores
    • Brunstein, M., Bruno, L., Desposito, M., and Levi, V. (2009) Anomalous dynamics of melanosomes driven by myosin-V in Xenopus laevis melanophores. Biophys. J. 97, 1548-1557
    • (2009) Biophys. J , vol.97 , pp. 1548-1557
    • Brunstein, M.1    Bruno, L.2    Desposito, M.3    Levi, V.4
  • 39
    • 0032576778 scopus 로고    scopus 로고
    • Myosin cooperates with microtubule motors during organelle transport in melanophores
    • Rogers, S. L., and Gelfand, V. I. (1998) Myosin cooperates with microtubule motors during organelle transport in melanophores. Curr. Biol. 8, 161-164
    • (1998) Curr. Biol , vol.8 , pp. 161-164
    • Rogers, S.L.1    Gelfand, V.I.2
  • 40
    • 24044519039 scopus 로고    scopus 로고
    • Activation of myosin Va function by melanophilin, a specific docking partner of myosin Va
    • Li, X. D., Ikebe, R., and Ikebe, M. (2005) Activation of myosin Va function by melanophilin, a specific docking partner of myosin Va. J. Biol. Chem. 280, 17815-17822
    • (2005) J. Biol. Chem , vol.280 , pp. 17815-17822
    • Li, X.D.1    Ikebe, R.2    Ikebe, M.3
  • 42
    • 78650651853 scopus 로고    scopus 로고
    • Simultaneous observation of tail and head movements of myosin v during processive motion
    • Lu, H., Kennedy, G. G., Warshaw, D. M., and Trybus, K. M. (2010) Simultaneous observation of tail and head movements of myosin V during processive motion. J. Biol. Chem. 285, 42068-42074
    • (2010) J. Biol. Chem , vol.285 , pp. 42068-42074
    • Lu, H.1    Kennedy, G.G.2    Warshaw, D.M.3    Trybus, K.M.4
  • 43
    • 47749142424 scopus 로고    scopus 로고
    • Load and Pi control flux through the branched kinetic cycle of myosin v
    • Kad, N. M., Trybus, K. M., and Warshaw, D. M. (2008) Load and Pi control flux through the branched kinetic cycle of myosin V. J. Biol. Chem. 283, 17477-17484
    • (2008) J. Biol. Chem , vol.283 , pp. 17477-17484
    • Kad, N.M.1    Trybus, K.M.2    Warshaw, D.M.3
  • 44
    • 84857074367 scopus 로고    scopus 로고
    • Myrip couples the capture of secretory granules by the actin-rich cell cortex and their attachment to the plasma membrane
    • Huet, S., Fanget, I., Jouannot, O., Meireles, P., Zeiske, T., Larochette, N., Darchen, F., and Desnos, C. (2012) Myrip couples the capture of secretory granules by the actin-rich cell cortex and their attachment to the plasma membrane. J. Neurosci. 32, 2564-2577
    • (2012) J. Neurosci , vol.32 , pp. 2564-2577
    • Huet, S.1    Fanget, I.2    Jouannot, O.3    Meireles, P.4    Zeiske, T.5    Larochette, N.6    Darchen, F.7    Desnos, C.8
  • 45
    • 34247384044 scopus 로고    scopus 로고
    • The ternary Rab27a-myrip-myosin VIIa complex regulates melanosome motility in the retinal pigment epithelium
    • Lopes, V. S., Ramalho, J. S., Owen, D. M., Karl, M. O., Strauss, O., Futter, C. E., and Seabra, M. C. (2007) The ternary Rab27a-myrip-myosin VIIa complex regulates melanosome motility in the retinal pigment epithelium. Traffic 8, 486-499
    • (2007) Traffic , vol.8 , pp. 486-499
    • Lopes, V.S.1    Ramalho, J.S.2    Owen, D.M.3    Karl, M.O.4    Strauss, O.5    Futter, C.E.6    Seabra, M.C.7
  • 46
    • 0033214974 scopus 로고    scopus 로고
    • Novel rabphilin- 3-like protein associates with insulin-containing granules in pancreatic beta cells
    • Wang, J., Takeuchi, T., Yokota, H., and Izumi, T. (1999) Novel rabphilin- 3-like protein associates with insulin-containing granules in pancreatic beta cells. J. Biol. Chem. 274, 28542-28548
    • (1999) J. Biol. Chem , vol.274 , pp. 28542-28548
    • Wang, J.1    Takeuchi, T.2    Yokota, H.3    Izumi, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.