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Volumn 13, Issue 9, 2003, Pages 715-724

The UCS domain protein She4p binds to myosin motor domains and is essential for class I and class V myosin function

Author keywords

[No Author keywords available]

Indexed keywords

SACCHAROMYCES; SACCHAROMYCES CEREVISIAE;

EID: 0037847544     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(03)00264-1     Document Type: Article
Times cited : (52)

References (33)
  • 1
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • Frydman, J. (2001). Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu. Rev. Biochem. 70, 603-647.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 603-647
    • Frydman, J.1
  • 2
    • 0030802287 scopus 로고    scopus 로고
    • Molecular chaperones and the cytoskeleton
    • Liang, P., and MacRae, T.H. (1997). Molecular chaperones and the cytoskeleton. J. Cell Sci. 110, 1431-1440.
    • (1997) J. Cell Sci. , vol.110 , pp. 1431-1440
    • Liang, P.1    MacRae, T.H.2
  • 4
    • 0037169028 scopus 로고    scopus 로고
    • Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin
    • Barral, J.M., Hutagalung, A.H., Brinker, A., Hartl, F.U., and Epstein, H.F. (2002). Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin. Science 295, 669-671.
    • (2002) Science , vol.295 , pp. 669-671
    • Barral, J.M.1    Hutagalung, A.H.2    Brinker, A.3    Hartl, F.U.4    Epstein, H.F.5
  • 5
    • 0016358187 scopus 로고
    • Temperature-sensitive mutation affecting myofilament assembly in Caenorhabditis elegans
    • Epstein, H.F., and Thomson, J.N. (1974). Temperature-sensitive mutation affecting myofilament assembly in Caenorhabditis elegans. Nature 250, 579-580.
    • (1974) Nature , vol.250 , pp. 579-580
    • Epstein, H.F.1    Thomson, J.N.2
  • 6
    • 0032583155 scopus 로고    scopus 로고
    • Unc-45 mutations in Caenorhabditis elegans implicate a CRO1/She4p-like domain in myosin assembly
    • Barral, J.M., Bauer, C.C., Ortiz, I., and Epstein, H.F. (1998). Unc-45 mutations in Caenorhabditis elegans implicate a CRO1/She4p-like domain in myosin assembly. J. Cell Biol. 143, 1215-1225.
    • (1998) J. Cell Biol. , vol.143 , pp. 1215-1225
    • Barral, J.M.1    Bauer, C.C.2    Ortiz, I.3    Epstein, H.F.4
  • 7
    • 0032473417 scopus 로고    scopus 로고
    • A homologue of the yeast SHE4 gene is essential for the transition between the syncytial and cellular stages during sexual reproduction of the fungus Podospora anserina
    • Berteuaux-Lecellier, V., Zickler, D., Debuchy, R., Panvier-Adoutte, A., Thompson-Coffe, C., and Picard, M. (1998). A homologue of the yeast SHE4 gene is essential for the transition between the syncytial and cellular stages during sexual reproduction of the fungus Podospora anserina. EMBO J. 17, 1248-1258.
    • (1998) EMBO J. , vol.17 , pp. 1248-1258
    • Berteuaux-Lecellier, V.1    Zickler, D.2    Debuchy, R.3    Panvier-Adoutte, A.4    Thompson-Coffe, C.5    Picard, M.6
  • 8
    • 0033886530 scopus 로고    scopus 로고
    • Fission yeast Rng3p: An UCS-domain protein that mediates myosin II assembly during cytokinesis
    • Wong, K.C., Naqvi, N.I., Iino, Y., Yamamoto, M., and Balasubramanian, M.K. (2000). Fission yeast Rng3p: an UCS-domain protein that mediates myosin II assembly during cytokinesis. J. Cell Sci. 113, 2421-2432.
    • (2000) J. Cell Sci. , vol.113 , pp. 2421-2432
    • Wong, K.C.1    Naqvi, N.I.2    Iino, Y.3    Yamamoto, M.4    Balasubramanian, M.K.5
  • 9
    • 0029981258 scopus 로고    scopus 로고
    • Mother cell-specific HO expression in budding yeast depends on the unconventional myosin Myo4p and other cytoplasmic proteins
    • Jansen, R.-P., Dowzer, C., Michaelis, C., Galova, M., and Nasmyth, K. (1996). Mother cell-specific HO expression in budding yeast depends on the unconventional myosin Myo4p and other cytoplasmic proteins. Cell 84, 687-697.
    • (1996) Cell , vol.84 , pp. 687-697
    • Jansen, R.-P.1    Dowzer, C.2    Michaelis, C.3    Galova, M.4    Nasmyth, K.5
  • 10
    • 1842833926 scopus 로고    scopus 로고
    • Two mammalian UNC-45 isoforms are related to distinct cytoskeletal and muscle-specific functions
    • Price, M.G., Landsverk, M.L., Barral, J.M., and Epstein, H.F. (2002). Two mammalian UNC-45 isoforms are related to distinct cytoskeletal and muscle-specific functions. J. Cell Sci. 115, 4013-4023.
    • (2002) J. Cell Sci. , vol.115 , pp. 4013-4023
    • Price, M.G.1    Landsverk, M.L.2    Barral, J.M.3    Epstein, H.F.4
  • 11
    • 0036022268 scopus 로고    scopus 로고
    • A zebrafish unc-45-related gene expressed during muscle development
    • Etheridge, L., Diiorio, P., and Sagerstrom, C.G. (2002). A zebrafish unc-45-related gene expressed during muscle development. Dev. Dyn. 224, 457-460.
    • (2002) Dev. Dyn. , vol.224 , pp. 457-460
    • Etheridge, L.1    Diiorio, P.2    Sagerstrom, C.G.3
  • 12
    • 12644263389 scopus 로고    scopus 로고
    • A novel fluorescence-activated cell sorter-based screen for yeast endocytosis mutants identifies a yeast homologue of mammalian eps15
    • Wendland, B., McCaffery, J.M., Xiao, Q., and Emr, S.D. (1996). A novel fluorescence-activated cell sorter-based screen for yeast endocytosis mutants identifies a yeast homologue of mammalian eps15. J. Cell Biol. 135, 1485-1500.
    • (1996) J. Cell Biol. , vol.135 , pp. 1485-1500
    • Wendland, B.1    McCaffery, J.M.2    Xiao, Q.3    Emr, S.D.4
  • 13
    • 0030875775 scopus 로고    scopus 로고
    • Mating type switching in yeast controlled by asymmetric localization of ASH1 mRNA
    • Long, R.M., Singer, R.H., Meng, X., Gonzalez, I., Nasmyth, K., and Jansen, R.-P. (1997). Mating type switching in yeast controlled by asymmetric localization of ASH1 mRNA. Science 277, 383-387.
    • (1997) Science , vol.277 , pp. 383-387
    • Long, R.M.1    Singer, R.H.2    Meng, X.3    Gonzalez, I.4    Nasmyth, K.5    Jansen, R.-P.6
  • 14
    • 0034644626 scopus 로고    scopus 로고
    • Plasma membrane compartmentalization in yeast by messenger RNA transport and a septin diffusion barrier
    • Takizawa, P.A., DeRisi, J.L., Wilhelm, J.E., and Vale, R.D. (2000). Plasma membrane compartmentalization in yeast by messenger RNA transport and a septin diffusion barrier. Science 290, 341-344.
    • (2000) Science , vol.290 , pp. 341-344
    • Takizawa, P.A.1    DeRisi, J.L.2    Wilhelm, J.E.3    Vale, R.D.4
  • 15
    • 0029923034 scopus 로고    scopus 로고
    • Role of type I myosins in receptor-mediated endocytosis in yeast
    • Geli, M.I., and Riezman, H. (1996). Role of type I myosins in receptor-mediated endocytosis in yeast. Science 272, 533-535.
    • (1996) Science , vol.272 , pp. 533-535
    • Geli, M.I.1    Riezman, H.2
  • 16
    • 0029984773 scopus 로고    scopus 로고
    • Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): Myosin I proteins are required for polarization of the actin cytoskeleton
    • Goodson, H.V., Anderson, B.L., Warrick, H.M., Pon, L.A., and Spudich, J.A. (1996). Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): myosin I proteins are required for polarization of the actin cytoskeleton. J. Cell Biol. 133, 1277-1291.
    • (1996) J. Cell Biol. , vol.133 , pp. 1277-1291
    • Goodson, H.V.1    Anderson, B.L.2    Warrick, H.M.3    Pon, L.A.4    Spudich, J.A.5
  • 17
    • 0034002965 scopus 로고    scopus 로고
    • Polarization of cell growth in yeast: I. Establishment and maintenance of polarity states
    • Pruyne, D., and Bretscher, A. (2000). Polarization of cell growth in yeast: I. Establishment and maintenance of polarity states. J. Cell Sci. 113, 365-375.
    • (2000) J. Cell Sci. , vol.113 , pp. 365-375
    • Pruyne, D.1    Bretscher, A.2
  • 18
    • 0037013903 scopus 로고    scopus 로고
    • Crystal structure of the motor domain of a class-I myosin
    • Kollmar, M., Durrwang, U., Kliche, W., Manstein, D.J., and Kull, F.J. (2002). Crystal structure of the motor domain of a class-I myosin. EMBO J. 21, 2517-2525.
    • (2002) EMBO J. , vol.21 , pp. 2517-2525
    • Kollmar, M.1    Durrwang, U.2    Kliche, W.3    Manstein, D.J.4    Kull, F.J.5
  • 20
    • 0034663930 scopus 로고    scopus 로고
    • An intact SH3 domain is required for myosin I-induced actin polymerization
    • Geli, M.I., Lombardi, R., Schmelzl, B., and Riezman, H. (2000). An intact SH3 domain is required for myosin I-induced actin polymerization. EMBO J. 19, 4281-4291.
    • (2000) EMBO J. , vol.19 , pp. 4281-4291
    • Geli, M.I.1    Lombardi, R.2    Schmelzl, B.3    Riezman, H.4
  • 21
    • 0028352176 scopus 로고
    • Immunofluorescence localization of the unconventional myosin, Myo2p, and the putative kinesin-related protein, Smy1p, to the same regions of polarized growth in Saccharomyces cerevisiae
    • Lillie, S.H., and Brown, S.S. (1994). Immunofluorescence localization of the unconventional myosin, Myo2p, and the putative kinesin-related protein, Smy1p, to the same regions of polarized growth in Saccharomyces cerevisiae. J. Cell Biol. 125, 825-842.
    • (1994) J. Cell Biol. , vol.125 , pp. 825-842
    • Lillie, S.H.1    Brown, S.S.2
  • 23
    • 0030978526 scopus 로고    scopus 로고
    • High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A
    • Ayscough, K.R., Stryker, J., Pokala, N., Sanders, M., Crews, P., and Drubin, D.G. (1997). High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A. J. Cell Biol. 137, 399-416.
    • (1997) J. Cell Biol. , vol.137 , pp. 399-416
    • Ayscough, K.R.1    Stryker, J.2    Pokala, N.3    Sanders, M.4    Crews, P.5    Drubin, D.G.6
  • 24
    • 0032526679 scopus 로고    scopus 로고
    • The Src homology domain 3 (SH3) of a yeast type I myosin, Myo5p, binds to verprolin and is required for targeting to sites of actin polarization
    • Anderson, B.L., Boldogh, I., Evangelista, M., Boone, C., Greene, L.A., and Pon, L.A. (1998). The Src homology domain 3 (SH3) of a yeast type I myosin, Myo5p, binds to verprolin and is required for targeting to sites of actin polarization. J. Cell Biol. 141, 1357-1370.
    • (1998) J. Cell Biol. , vol.141 , pp. 1357-1370
    • Anderson, B.L.1    Boldogh, I.2    Evangelista, M.3    Boone, C.4    Greene, L.A.5    Pon, L.A.6
  • 25
    • 0033732904 scopus 로고    scopus 로고
    • In vivo function of class I myosins
    • Osherov, N., and May, G.S. (2000). In vivo function of class I myosins. Cell Motil. Cytoskeleton 47, 163-173.
    • (2000) Cell Motil. Cytoskeleton , vol.47 , pp. 163-173
    • Osherov, N.1    May, G.S.2
  • 26
    • 0033571411 scopus 로고    scopus 로고
    • The COOH-terminal domain of Myo2p, a yeast myosin V, has a direct role in secretory vesicle targeting
    • Schott, D., Ho, J., Pruyne, D., and Bretscher, A. (1999). The COOH-terminal domain of Myo2p, a yeast myosin V, has a direct role in secretory vesicle targeting. J. Cell Biol. 147, 791-807.
    • (1999) J. Cell Biol. , vol.147 , pp. 791-807
    • Schott, D.1    Ho, J.2    Pruyne, D.3    Bretscher, A.4
  • 27
    • 0034707661 scopus 로고    scopus 로고
    • Caenorhabditis elegans UNC-45 is a component of muscle thick filaments and colocalizes with myosin heavy chain B, but not myosin heavy chain A
    • Ao, W., and Pilgrim, D. (2000). Caenorhabditis elegans UNC-45 is a component of muscle thick filaments and colocalizes with myosin heavy chain B, but not myosin heavy chain A. J. Cell Biol. 148, 375-384.
    • (2000) J. Cell Biol. , vol.148 , pp. 375-384
    • Ao, W.1    Pilgrim, D.2
  • 28
    • 0030840519 scopus 로고    scopus 로고
    • Heterologous HIS3 marker and GFP reporter modules for PCR-targetting in Saccharomyces cerevisiae
    • Wach, A., Brachat, A., Alberti-Segui, C., Rebischung, C., and Philiippsen, P. (1997). Heterologous HIS3 marker and GFP reporter modules for PCR-targetting in Saccharomyces cerevisiae. Yeast 13, 1065-1075.
    • (1997) Yeast , vol.13 , pp. 1065-1075
    • Wach, A.1    Brachat, A.2    Alberti-Segui, C.3    Rebischung, C.4    Philiippsen, P.5
  • 29
    • 0032775010 scopus 로고    scopus 로고
    • Epitope tagging of yeast genes using a PCR-based strategy: More tags and improved practical routines
    • Knop, M., Siegers, K., Pereira, G., Zachariae, W., Winsor, B., Nasmyth, K., and Schiebel, E. (1999). Epitope tagging of yeast genes using a PCR-based strategy: more tags and improved practical routines. Yeast 15, 963-972.
    • (1999) Yeast , vol.15 , pp. 963-972
    • Knop, M.1    Siegers, K.2    Pereira, G.3    Zachariae, W.4    Winsor, B.5    Nasmyth, K.6    Schiebel, E.7
  • 30
    • 0030455820 scopus 로고    scopus 로고
    • Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast
    • James, P., Halladay, J., and Craig, E.A. (1996). Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast. Genetics 144, 1425-1436.
    • (1996) Genetics , vol.144 , pp. 1425-1436
    • James, P.1    Halladay, J.2    Craig, E.A.3
  • 31
    • 0038128252 scopus 로고    scopus 로고
    • She4p/Dim1p interacts with the motor domain of unconventional myosins in the budding yeast Saccharomyces cerevisiae
    • in press Published online February 6, 2003, 10.1091/mbc.E02-09-0616
    • Toi, H., Fujimura-Kamada, K., Irie, K., Takai, Y., Todo, S., and Tanaka, K. (2003). She4p/Dim1p interacts with the motor domain of unconventional myosins in the budding yeast Saccharomyces cerevisiae. Mol. Biol. Cell, in press Published online February 6, 2003, 10.1091/mbc.E02-09-0616.
    • (2003) Mol. Biol. Cell
    • Toi, H.1    Fujimura-Kamada, K.2    Irie, K.3    Takai, Y.4    Todo, S.5    Tanaka, K.6
  • 32
    • 0037138403 scopus 로고    scopus 로고
    • Calmodulin signaling via the IQ motif
    • Bähler, M., and Rhoads, A. (2002). Calmodulin signaling via the IQ motif. FEBS Lett. 513, 107-113.
    • (2002) FEBS Lett. , vol.513 , pp. 107-113
    • Bähler, M.1    Rhoads, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.