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Volumn 17, Issue 20, 2007, Pages 1721-1734

Zebrafish Melanophilin Facilitates Melanosome Dispersion by Regulating Dynein

Author keywords

CELLBIO

Indexed keywords

CARRIER PROTEIN; DYNEIN ADENOSINE TRIPHOSPHATASE; HYPOPHYSIS HORMONE; HYPOTHALAMUS HORMONE; INTERMEDIN; MELANIN; MELANIN CONCENTRATING HORMONE; MELANIN-CONCENTRATING HORMONE; PRIMER DNA; UNCLASSIFIED DRUG; ZEBRAFISH PROTEIN;

EID: 35348877498     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2007.09.028     Document Type: Article
Times cited : (67)

References (38)
  • 2
    • 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., and Borisy G.G. Functional coordination of microtubule-based and actin-based motility in melanophores. Curr. Biol. 8 (1998) 165-168
    • (1998) Curr. Biol. , vol.8 , pp. 165-168
    • Rodionov, V.I.1    Hope, A.J.2    Svitkina, T.M.3    Borisy, G.G.4
  • 4
    • 0032517764 scopus 로고    scopus 로고
    • Heterotrimeric kinesin II is the microtubule motor protein responsible for pigment dispersion in Xenopus melanophores
    • Tuma M.C., Zill A., Le Bot N., Vernos I., and Gelfand V. Heterotrimeric kinesin II is the microtubule motor protein responsible for pigment dispersion in Xenopus melanophores. J. Cell Biol. 143 (1998) 1547-1558
    • (1998) J. Cell Biol. , vol.143 , pp. 1547-1558
    • Tuma, M.C.1    Zill, A.2    Le Bot, N.3    Vernos, I.4    Gelfand, V.5
  • 5
    • 0032576778 scopus 로고    scopus 로고
    • Myosin cooperates with microtubule motors during organelle transport in melanophores
    • Rogers S.L., and Gelfand V.I. Myosin cooperates with microtubule motors during organelle transport in melanophores. Curr. Biol. 8 (1998) 161-164
    • (1998) Curr. Biol. , vol.8 , pp. 161-164
    • Rogers, S.L.1    Gelfand, V.I.2
  • 6
    • 0033588979 scopus 로고    scopus 로고
    • Regulation of melanosome movement in the cell cycle by reversible association with myosin V
    • Rogers S.L., Karcher R.L., Roland J.T., Minin A.A., Steffen W., and Gelfand V.I. Regulation of melanosome movement in the cell cycle by reversible association with myosin V. J. Cell Biol. 146 (1999) 1265-1276
    • (1999) J. Cell Biol. , vol.146 , pp. 1265-1276
    • Rogers, S.L.1    Karcher, R.L.2    Roland, J.T.3    Minin, A.A.4    Steffen, W.5    Gelfand, V.I.6
  • 8
    • 0030933293 scopus 로고    scopus 로고
    • Regulated bidirectional motility of melanophore pigment granules along microtubules in vitro
    • Rogers S.L., Tint I.S., Fanapour P.C., and Gelfand V.I. Regulated bidirectional motility of melanophore pigment granules along microtubules in vitro. Proc. Natl. Acad. Sci. USA 94 (1997) 3720-3725
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3720-3725
    • Rogers, S.L.1    Tint, I.S.2    Fanapour, P.C.3    Gelfand, V.I.4
  • 9
    • 0242318330 scopus 로고    scopus 로고
    • Switching between microtubule- and actin-based transport systems in melanophores is controlled by cAMP levels
    • Rodionov V., Yi J., Kashina A., Oladipo A., and Gross S.P. Switching between microtubule- and actin-based transport systems in melanophores is controlled by cAMP levels. Curr. Biol. 13 (2003) 1837-1847
    • (2003) Curr. Biol. , vol.13 , pp. 1837-1847
    • Rodionov, V.1    Yi, J.2    Kashina, A.3    Oladipo, A.4    Gross, S.P.5
  • 10
    • 0027324156 scopus 로고
    • Directional instability of kinetochore motility during chromosome congression and segregation in mitotic newt lung cells: A push-pull mechanism
    • Skibbens R.V., Skeen V.P., and Salmon E.D. Directional instability of kinetochore motility during chromosome congression and segregation in mitotic newt lung cells: A push-pull mechanism. J. Cell Biol. 122 (1993) 859-875
    • (1993) J. Cell Biol. , vol.122 , pp. 859-875
    • Skibbens, R.V.1    Skeen, V.P.2    Salmon, E.D.3
  • 11
    • 0842269058 scopus 로고    scopus 로고
    • Cargo-carrying motor vehicles on the neuronal highway: Transport pathways and neurodegenerative disease
    • Gunawardena S., and Goldstein L.S. Cargo-carrying motor vehicles on the neuronal highway: Transport pathways and neurodegenerative disease. J. Neurobiol. 58 (2004) 258-271
    • (2004) J. Neurobiol. , vol.58 , pp. 258-271
    • Gunawardena, S.1    Goldstein, L.S.2
  • 13
    • 0023057728 scopus 로고
    • Bidirectional pigment granule movements of melanophores are regulated by protein phosphorylation and dephosphorylation
    • Rozdzial M.M., and Haimo L.T. Bidirectional pigment granule movements of melanophores are regulated by protein phosphorylation and dephosphorylation. Cell 47 (1986) 1061-1070
    • (1986) Cell , vol.47 , pp. 1061-1070
    • Rozdzial, M.M.1    Haimo, L.T.2
  • 14
    • 0026549077 scopus 로고
    • Intracellular cyclic AMP not calcium, determines the direction of vesicle movement in melanophores: Direct measurement by fluorescence ratio imaging
    • Sammak P.J., Adams S.R., Harootunian A.T., Schliwa M., and Tsien R.Y. Intracellular cyclic AMP not calcium, determines the direction of vesicle movement in melanophores: Direct measurement by fluorescence ratio imaging. J. Cell Biol. 117 (1992) 57-72
    • (1992) J. Cell Biol. , vol.117 , pp. 57-72
    • Sammak, P.J.1    Adams, S.R.2    Harootunian, A.T.3    Schliwa, M.4    Tsien, R.Y.5
  • 15
    • 33644548583 scopus 로고    scopus 로고
    • Organelle transport along microtubules in Xenopus melanophores: Evidence for cooperation between multiple motors
    • Levi V., Serpinskaya A.S., Gratton E., and Gelfand V. Organelle transport along microtubules in Xenopus melanophores: Evidence for cooperation between multiple motors. Biophys. J. 90 (2006) 318-327
    • (2006) Biophys. J. , vol.90 , pp. 318-327
    • Levi, V.1    Serpinskaya, A.S.2    Gratton, E.3    Gelfand, V.4
  • 16
    • 0025647064 scopus 로고
    • Delayed start-up of kinesin-driven microtubule gliding following inhibition by adenosine 5′-[beta,gamma-imido]triphosphate
    • Schnapp B.J., Crise B., Sheetz M.P., Reese T.S., and Khan S. Delayed start-up of kinesin-driven microtubule gliding following inhibition by adenosine 5′-[beta,gamma-imido]triphosphate. Proc. Natl. Acad. Sci. USA 87 (1990) 10053-10057
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 10053-10057
    • Schnapp, B.J.1    Crise, B.2    Sheetz, M.P.3    Reese, T.S.4    Khan, S.5
  • 17
    • 0034611001 scopus 로고    scopus 로고
    • Dynein-mediated cargo transport in vivo. A switch controls travel distance
    • Gross S.P., Welte M.A., Block S.M., and Wieschaus E.F. Dynein-mediated cargo transport in vivo. A switch controls travel distance. J. Cell Biol. 148 (2000) 945-956
    • (2000) J. Cell Biol. , vol.148 , pp. 945-956
    • Gross, S.P.1    Welte, M.A.2    Block, S.M.3    Wieschaus, E.F.4
  • 19
    • 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
    • Fukuda M., Kuroda T.S., and 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 (2002) 12432-12436
    • (2002) J. Biol. Chem. , vol.277 , pp. 12432-12436
    • Fukuda, M.1    Kuroda, T.S.2    Mikoshiba, K.3
  • 21
    • 0001329015 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay
    • Maquat L.E. Nonsense-mediated mRNA decay. Curr. Biol. 12 (2002) R196-R197
    • (2002) Curr. Biol. , vol.12
    • Maquat, L.E.1
  • 22
    • 0032824044 scopus 로고    scopus 로고
    • nacre encodes a zebrafish microphthalmia-related protein that regulates neural-crest-derived pigment cell fate
    • Lister J.A., Robertson C.P., Lepage T., Johnson S.L., and Raible D.W. nacre encodes a zebrafish microphthalmia-related protein that regulates neural-crest-derived pigment cell fate. Development 126 (1999) 3757-3767
    • (1999) Development , vol.126 , pp. 3757-3767
    • Lister, J.A.1    Robertson, C.P.2    Lepage, T.3    Johnson, S.L.4    Raible, D.W.5
  • 25
    • 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. A coiled-coil domain of melanophilin is essential for myosin Va recruitment and melanosome transport in melanocytes. Mol. Biol. Cell 17 (2006) 720-735
    • (2006) Mol. Biol. Cell , vol.17 , pp. 720-735
    • Hume, A.N.1    Tarafder, A.K.2    Ramalho, J.S.3    Sviderskaya, E.V.4    Seabra, M.C.5
  • 26
    • 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. Activation of myosin Va function by melanophilin, a specific docking partner of myosin Va. J. Biol. Chem. 280 (2005) 17815-17822
    • (2005) J. Biol. Chem. , vol.280 , pp. 17815-17822
    • Li, X.D.1    Ikebe, R.2    Ikebe, M.3
  • 27
    • 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 III J.A. Rab27a is an essential component of melanosome receptor for myosin Va. Mol. Biol. Cell 13 (2002) 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
  • 28
    • 32344449132 scopus 로고    scopus 로고
    • Functional analysis of slac2-a/melanophilin as a linker protein between Rab27A and myosin Va in melanosome transport
    • Kuroda T.S., Itoh T., and Fukuda M. Functional analysis of slac2-a/melanophilin as a linker protein between Rab27A and myosin Va in melanosome transport. Methods Enzymol. 403 (2005) 419-431
    • (2005) Methods Enzymol. , vol.403 , pp. 419-431
    • Kuroda, T.S.1    Itoh, T.2    Fukuda, M.3
  • 29
    • 0025158107 scopus 로고
    • Protein kinase recognition sequence motifs
    • Kemp B.E., and Pearson R.B. Protein kinase recognition sequence motifs. Trends Biochem. Sci. 15 (1990) 342-346
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 342-346
    • Kemp, B.E.1    Pearson, R.B.2
  • 30
    • 0042622251 scopus 로고    scopus 로고
    • Scansite 2.0: Proteome-wide prediction of cell signaling interactions using short sequence motifs
    • Obenauer J.C., Cantley L.C., and Yaffe M.B. Scansite 2.0: Proteome-wide prediction of cell signaling interactions using short sequence motifs. Nucleic Acids Res. 31 (2003) 3635-3641
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3635-3641
    • Obenauer, J.C.1    Cantley, L.C.2    Yaffe, M.B.3
  • 31
    • 0033853883 scopus 로고    scopus 로고
    • Making sense of melanosome dynamics in mouse melanocytes
    • Wu X., and Hammer III J.A. Making sense of melanosome dynamics in mouse melanocytes. Pigment Cell Res. 13 (2000) 241-247
    • (2000) Pigment Cell Res. , vol.13 , pp. 241-247
    • Wu, X.1    Hammer III, J.A.2
  • 32
    • 23044506137 scopus 로고    scopus 로고
    • Functional analysis of Slac2-c/MyRIP as a linker protein between melanosomes and myosin VIIa
    • Kuroda T.S., and Fukuda M. Functional analysis of Slac2-c/MyRIP as a linker protein between melanosomes and myosin VIIa. J. Biol. Chem. 280 (2005) 28015-28022
    • (2005) J. Biol. Chem. , vol.280 , pp. 28015-28022
    • Kuroda, T.S.1    Fukuda, M.2
  • 33
    • 1842581761 scopus 로고    scopus 로고
    • Rabphilin and Noc2 are recruited to dense-core vesicles through specific interaction with Rab27A in PC12 cells
    • Fukuda M., Kanno E., and Yamamoto A. Rabphilin and Noc2 are recruited to dense-core vesicles through specific interaction with Rab27A in PC12 cells. J. Biol. Chem. 279 (2004) 13065-13075
    • (2004) J. Biol. Chem. , vol.279 , pp. 13065-13075
    • Fukuda, M.1    Kanno, E.2    Yamamoto, A.3
  • 34
    • 28244484879 scopus 로고    scopus 로고
    • The C2B domain of rabphilin directly interacts with SNAP-25 and regulates the docking step of dense core vesicle exocytosis in PC12 cells
    • Tsuboi T., and Fukuda M. The C2B domain of rabphilin directly interacts with SNAP-25 and regulates the docking step of dense core vesicle exocytosis in PC12 cells. J. Biol. Chem. 280 (2005) 39253-39259
    • (2005) J. Biol. Chem. , vol.280 , pp. 39253-39259
    • Tsuboi, T.1    Fukuda, M.2
  • 38
    • 0026690741 scopus 로고
    • Control of organelle transport in melanophores: Regulation of Ca2+ and cAMP levels
    • Thaler C.D., and Haimo L.T. Control of organelle transport in melanophores: Regulation of Ca2+ and cAMP levels. Cell Motil. Cytoskeleton 22 (1992) 175-184
    • (1992) Cell Motil. Cytoskeleton , vol.22 , pp. 175-184
    • Thaler, C.D.1    Haimo, L.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.