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Volumn 160, Issue 6, 2003, Pages 887-897

Identification of an organelle-specific myosin V receptor

Author keywords

Membrane transport; Myo2p; Vac17p; Vacuole; Yeast

Indexed keywords

AMINO ACID; MYOSIN V; MYOSIN V RECEPTOR; PROTEIN MYO2P; PROTEIN VAC17P; UNCLASSIFIED DRUG;

EID: 0037451122     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200210139     Document Type: Article
Times cited : (92)

References (34)
  • 1
    • 0034735942 scopus 로고    scopus 로고
    • The role of the proteins Kar9 and Myo2 in orienting the mitotic spindle of budding yeast
    • Beach, D.L., J. Thibodeaux, P. Maddox, E. Yeh, and K. Bloom. 2000. The role of the proteins Kar9 and Myo2 in orienting the mitotic spindle of budding yeast. Curr. Biol. 10:1497-1506.
    • (2000) Curr. Biol. , vol.10 , pp. 1497-1506
    • Beach, D.L.1    Thibodeaux, J.2    Maddox, P.3    Yeh, E.4    Bloom, K.5
  • 2
    • 0030692711 scopus 로고    scopus 로고
    • Vac7p, a novel vacuolar protein, is required for normal vacuole inheritance and morphology
    • Bonangelino, C.J., N.L. Catlett, and L.S. Weisman. 1997. Vac7p, a novel vacuolar protein, is required for normal vacuole inheritance and morphology. Mol. Cell Biol. 17:6847-6858.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 6847-6858
    • Bonangelino, C.J.1    Catlett, N.L.2    Weisman, L.S.3
  • 3
    • 13444256902 scopus 로고    scopus 로고
    • Role of a yeast myosin-V in movement of the vacuole and other cargoes
    • University of Iowa, Iowa City
    • Catlett, N.L. 2000. Role of a yeast myosin-V in movement of the vacuole and other cargoes. In Department of Biochemistry. University of Iowa, Iowa City. 135.
    • (2000) Department of Biochemistry , pp. 135
    • Catlett, N.L.1
  • 4
    • 0032426664 scopus 로고    scopus 로고
    • The terminal tail region of a yeast myosin-V mediates its attachment to vacuole membranes and sites of polarized growth
    • Catlett, N.L., and L.S. Weisman. 1998. The terminal tail region of a yeast myosin-V mediates its attachment to vacuole membranes and sites of polarized growth. Proc. Natl. Acad. Sci. USA. 95:14799-14804.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14799-14804
    • Catlett, N.L.1    Weisman, L.S.2
  • 5
    • 0034618049 scopus 로고    scopus 로고
    • Two distinct regions in a yeast myosin-V tail domain are required for the movement of different cargoes
    • Catlett, N.L., J.E. Duex, F. Tang, and L.S. Weisman. 2000. Two distinct regions in a yeast myosin-V tail domain are required for the movement of different cargoes. J. Cell Biol. 150:513-526.
    • (2000) J. Cell Biol. , vol.150 , pp. 513-526
    • Catlett, N.L.1    Duex, J.E.2    Tang, F.3    Weisman, L.S.4
  • 6
    • 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 T.S. Kuroda. 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
  • 7
    • 0029908193 scopus 로고    scopus 로고
    • Characterization of new vacuolar segregation mutants, isolated by screening for loss of proteinase B self-activation
    • Gomes de Mesquita, D.S., H.B. van den Hazel, J. Bouwman, and C.L. Woldringh. 1996. Characterization of new vacuolar segregation mutants, isolated by screening for loss of proteinase B self-activation. Eur. J. Cell Biol. 71:237-247.
    • (1996) Eur. J. Cell Biol. , vol.71 , pp. 237-247
    • Gomes de Mesquita, D.S.1    Van den Hazel, H.B.2    Bouwman, J.3    Woldringh, C.L.4
  • 8
    • 0028902506 scopus 로고
    • The role of Myo2, a yeast class V myosin, in vesicular transport
    • Govindan, B., R. Bowser, and P. Novick. 1995. The role of Myo2, a yeast class V myosin, in vesicular transport. J. Cell Biol. 128:1055-1068.
    • (1995) J. Cell Biol. , vol.128 , pp. 1055-1068
    • Govindan, B.1    Bowser, R.2    Novick, P.3
  • 9
    • 0030470182 scopus 로고    scopus 로고
    • Actin and myosin function in directed vacuole movement during cell division in Saccharomyces cerevisiae
    • Hill, K.L., N.L. Catlett, and L.S. Weisman. 1996. Actin and myosin function in directed vacuole movement during cell division in Saccharomyces cerevisiae. J. Cell Biol. 135:1535-1549.
    • (1996) J. Cell Biol. , vol.135 , pp. 1535-1549
    • Hill, K.L.1    Catlett, N.L.2    Weisman, L.S.3
  • 10
    • 0035842904 scopus 로고    scopus 로고
    • A role for Vps1p, actin, and the Myo2p motor in peroxisome abundance and inheritance in Saccharomyces cerevisiae
    • Hoepfner, D., M. van den Berg, P. Philippsen, H.F. Tabak, and E.H. Hettema. 2001. A role for Vps1p, actin, and the Myo2p motor in peroxisome abundance and inheritance in Saccharomyces cerevisiae. J. Cell Biol. 155:979-990.
    • (2001) J. Cell Biol. , vol.155 , pp. 979-990
    • Hoepfner, D.1    Van den Berg, M.2    Philippsen, P.3    Tabak, H.F.4    Hettema, E.H.5
  • 12
    • 0030455820 scopus 로고    scopus 로고
    • Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast
    • James, P., J. Halladay, and E.A. Craig. 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
  • 13
    • 0025801365 scopus 로고
    • The Saccharomyces cerevisiae MYO2 gene encodes an essential myosin for vectorial transport of vesicles
    • Johnston, G.C., J.A. Prendergast, and R.A. Singer. 1991. The Saccharomyces cerevisiae MYO2 gene encodes an essential myosin for vectorial transport of vesicles. J. Cell Biol. 113:539-551.
    • (1991) J. Cell Biol. , vol.113 , pp. 539-551
    • Johnston, G.C.1    Prendergast, J.A.2    Singer, R.A.3
  • 16
    • 0033525077 scopus 로고    scopus 로고
    • Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts. Many raft proteins are acylated, while few are prenylated
    • Melkonian, K.A., A.G. Ostermeyer, J.Z. Chen, M.G. Roth, and D.A. Brown. 1999. Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts. Many raft proteins are acylated, while few are prenylated. J. Biol. Chem. 274:3910-3917.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3910-3917
    • Melkonian, K.A.1    Ostermeyer, A.G.2    Chen, J.Z.3    Roth, M.G.4    Brown, D.A.5
  • 17
    • 0037165662 scopus 로고    scopus 로고
    • Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions
    • Nagashima, K., S. Torii, Z. Yi, M. Igarashi, K. Okamoto, T. Takeuchi, and T. Izumi. 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
  • 18
    • 0031046165 scopus 로고    scopus 로고
    • Isolation of early meiotic recombination genes analogous to S. cerevisiae REC104 from the yeasts S. paradoxus and S. pastorianus
    • Nau, J.J., K.R. Summers, A.M. Galbraith, S.A. Bullard, and R.E. Malone. 1997. Isolation of early meiotic recombination genes analogous to S. cerevisiae REC104 from the yeasts S. paradoxus and S. pastorianus. Curr. Genet. 31:7-14.
    • (1997) Curr. Genet. , vol.31 , pp. 7-14
    • Nau, J.J.1    Summers, K.R.2    Galbraith, A.M.3    Bullard, S.A.4    Malone, R.E.5
  • 19
    • 0037054540 scopus 로고    scopus 로고
    • Ypt32 recruits the Sec4p guanine nucleotide exchange factor, Sec2p, to secretory vesicles; evidence for a Rab cascade in yeast
    • Ortiz, D., M. Medkova, C. Walch-Solimena, and P. Novick. 2002. Ypt32 recruits the Sec4p guanine nucleotide exchange factor, Sec2p, to secretory vesicles; evidence for a Rab cascade in yeast. J. Cell Biol. 157:1005-1015.
    • (2002) J. Cell Biol. , vol.157 , pp. 1005-1015
    • Ortiz, D.1    Medkova, M.2    Walch-Solimena, C.3    Novick, P.4
  • 20
    • 0036107354 scopus 로고    scopus 로고
    • Melanophilin, the product of the leaden locus, is required for targeting of myosin-Va to melanosomes
    • Provance, D.W., T.L. James, and J.A. Mercer. 2002. Melanophilin, the product of the leaden locus, is required for targeting of myosin-Va to melanosomes. Traffic. 3:124-132.
    • (2002) Traffic , vol.3 , pp. 124-132
    • Provance, D.W.1    James, T.L.2    Mercer, J.A.3
  • 21
    • 0032915418 scopus 로고    scopus 로고
    • The tail of a yeast class V myosin, Myo2p, functions as a localization domain
    • Reck-Peterson, S.L., P.J. Novick, and M.S. Mooseker. 1999. The tail of a yeast class V myosin, Myo2p, functions as a localization domain. Mol. Biol. Cell. 10:1001-1017.
    • (1999) Mol. Biol. Cell. , vol.10 , pp. 1001-1017
    • Reck-Peterson, S.L.1    Novick, P.J.2    Mooseker, M.S.3
  • 23
    • 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., J. Ho, D. Pruyne, and A. Bretscher. 1999. The COOH-terminal domain of Myo2p, a yeast myosin V, has a direct role in secretory vesicle targeting. J. Cell Biol. 147:791-808.
    • (1999) J. Cell Biol. , vol.147 , pp. 791-808
    • Schott, D.1    Ho, J.2    Pruyne, D.3    Bretscher, A.4
  • 24
    • 0003529274 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Sherman, F., G.R. Fink, and J.B. Hicks. 1986. Methods in Yeast Genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. 153 pp.
    • (1986) Methods in Yeast Genetics , vol.153
    • Sherman, F.1    Fink, G.R.2    Hicks, J.B.3
  • 25
    • 0033790210 scopus 로고    scopus 로고
    • Suppressors of mdm20 in yeast identify new alleles of ACT1 and TPM1 predicted to enhance actin-tropomyosin interactions
    • Singer, J.M., G.J. Hermann, and J.M. Shaw. 2000. Suppressors of mdm20 in yeast identify new alleles of ACT1 and TPM1 predicted to enhance actin-tropomyosin interactions. Genetics. 156:523-534.
    • (2000) Genetics , vol.156 , pp. 523-534
    • Singer, J.M.1    Hermann, G.J.2    Shaw, J.M.3
  • 26
    • 0037422115 scopus 로고    scopus 로고
    • Regulated degradation of a class V myosin receptor directs movement of the yeast vacuole
    • 10.1038/nature01453
    • Tang, F., E.J. Kauffman, J.L. Novak, J.J. Nau, N.L. Catlett, and L.S. Weisman. 2003. Regulated degradation of a class V myosin receptor directs movement of the yeast vacuole. Nature. 10.1038/nature01453.
    • (2003) Nature
    • Tang, F.1    Kauffman, E.J.2    Novak, J.L.3    Nau, J.J.4    Catlett, N.L.5    Weisman, L.S.6
  • 27
    • 0022461695 scopus 로고
    • A gene required for the separation of chromosomes on the spindle apparatus in yeast
    • Thomas, J.H., and D. Botstein. 1986. A gene required for the separation of chromosomes on the spindle apparatus in yeast. Cell. 44:65-76.
    • (1986) Cell , vol.44 , pp. 65-76
    • Thomas, J.H.1    Botstein, D.2
  • 28
    • 0025640941 scopus 로고
    • In vitro reconstitution of intercompartmental protein transport to the yeast vacuole
    • Vida, T.A., T.R. Graham, and S.D. Emr. 1990. In vitro reconstitution of intercompartmental protein transport to the yeast vacuole. J. Cell Biol. 111: 2871-2884.
    • (1990) J. Cell Biol. , vol.111 , pp. 2871-2884
    • Vida, T.A.1    Graham, T.R.2    Emr, S.D.3
  • 29
    • 0035860689 scopus 로고    scopus 로고
    • Fusion of docked membranes requires the armadillo repeat protein Vac8p
    • Wang, Y.X., E.J. Kauffman, J.E. Duex, and L.S. Weisman. 2001. Fusion of docked membranes requires the armadillo repeat protein Vac8p. J. Biol. Chem. 276: 35133-35140.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35133-35140
    • Wang, Y.X.1    Kauffman, E.J.2    Duex, J.E.3    Weisman, L.S.4
  • 30
    • 0002529177 scopus 로고
    • Mutagenesis of yeast cell
    • F.M. Ausubel, R. Brent, R.E. Kingston, D.D. Moore, J.A. Smith, J.G. Seidman, and K. Struhl, editors. Greene Publishing Associates and Wiley-Interscience, New York
    • Winston, F. 1990. Mutagenesis of yeast cell. In Current Protocols in Molecular Biology. F.M. Ausubel, R. Brent, R.E. Kingston, D.D. Moore, J.A. Smith, J.G. Seidman, and K. Struhl, editors. Greene Publishing Associates and Wiley-Interscience, New York. 13.3.1-13.3.4.
    • (1990) Current Protocols in Molecular Biology , pp. 1331-1334
    • Winston, F.1
  • 31
    • 0036000020 scopus 로고    scopus 로고
    • Rab27a is an essential component of melanosome receptor for Myosin va
    • Wu, X., F. Wang, K. Rao, J.R. Sellers, and J.A. Hammer III. 2002a. 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 J.A. III5
  • 33
    • 0034739004 scopus 로고    scopus 로고
    • Myosin V orientates the mirotic spindle in yeast
    • Yin, H., D. Pruyne, T.C. Huffaker, and A. Bretscher. 2000. Myosin V orientates the mirotic spindle in yeast. Nature. 406:1013-1015.
    • (2000) Nature , vol.406 , pp. 1013-1015
    • Yin, H.1    Pruyne, D.2    Huffaker, T.C.3    Bretscher, A.4
  • 34
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias, D.A., J.D. Violin, A.C. Newton, and R.Y. Tsien. 2002. Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science. 296:913-916.
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4


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