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Volumn 170, Issue 2, 2005, Pages 555-568

Interaction of the Saccharomyces cerevisiae cortical actin patch protein Rvs167p with proteins involved in ER to Golgi vesicle trafficking

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; AMPHIPHYSIN; CARRIER PROTEIN; CYTOSKELETON PROTEIN; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; PROTEIN GYP11P; PROTEIN GYP5P; PROTEIN RVS167P; PROTEIN YPT1P; RAB PROTEIN; UNCLASSIFIED DRUG;

EID: 22144471563     PISSN: 00166731     EISSN: None     Source Type: Journal    
DOI: 10.1534/genetics.104.040063     Document Type: Article
Times cited : (20)

References (76)
  • 1
    • 0033584946 scopus 로고    scopus 로고
    • Two new members of a family of Ypt/Rab GTPase activating proteins. Promiscuity of substrate recognition
    • ALBERT, S., and D. GALLWITZ, 1999 Two new members of a family of Ypt/Rab GTPase activating proteins. Promiscuity of substrate recognition. J. Biol. Chem. 274: 33186-33189.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33186-33189
    • Albert, S.1    Gallwitz, D.2
  • 2
    • 0033923318 scopus 로고    scopus 로고
    • Msb4p, a protein involved in Cdc42-dependent organization of the actin cytoskeleton, is a Ypt/ Rab-specific GAP
    • ALBERT, S., and D. GALLWITZ, 2000 Msb4p, a protein involved in Cdc42-dependent organization of the actin cytoskeleton, is a Ypt/ Rab-specific GAP. Biol. Chem. 381: 453-456.
    • (2000) Biol. Chem. , vol.381 , pp. 453-456
    • Albert, S.1    Gallwitz, D.2
  • 3
    • 0033214775 scopus 로고    scopus 로고
    • Identification of the catalytic domains and their functionally critical arginine residues of two yeast GTPase-activating proteins specific for Ypt/Rab transport GTPases
    • ALBERT, S., E. WILL and D. GALLWITZ, 1999 Identification of the catalytic domains and their functionally critical arginine residues of two yeast GTPase-activating proteins specific for Ypt/Rab transport GTPases. EMBO J. 18: 5216-5225.
    • (1999) EMBO J. , vol.18 , pp. 5216-5225
    • Albert, S.1    Will, E.2    Gallwitz, D.3
  • 4
    • 0028928199 scopus 로고
    • Defining protein interactions with yeast actin in vivo
    • AMBERG, D. C., E. BASART and D. BOTSTEIN, 1995 Defining protein interactions with yeast actin in vivo. Nat. Struct. Biol. 2: 28-35.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 28-35
    • Amberg, D.C.1    Basart, E.2    Botstein, D.3
  • 6
    • 0024438225 scopus 로고
    • The GTP-binding protein Ypt1 is required for transport in vitro: The Golgi apparatus is defective in ypt1 mutants
    • BACON, R. A., A. SALMINEN, H. RUOHOLA, P. NOVICK and S. FERRO-NOVICK, 1989 The GTP-binding protein Ypt1 is required for transport in vitro: the Golgi apparatus is defective in ypt1 mutants. J. Cell Biol. 109: 1015-1022.
    • (1989) J. Cell Biol. , vol.109 , pp. 1015-1022
    • Bacon, R.A.1    Salminen, A.2    Ruohola, H.3    Novick, P.4    Ferro-Novick, S.5
  • 7
    • 0032771075 scopus 로고    scopus 로고
    • Rvs167p, the budding yeast homolog of amphiphysin, colocalizes with actin patches
    • BALGUERIE, A., P. SIVADON, M. BONNEU and M. AIGLE, 1999 Rvs167p, the budding yeast homolog of amphiphysin, colocalizes with actin patches. J. Cell Sci. 112: 2529-2537.
    • (1999) J. Cell Sci. , vol.112 , pp. 2529-2537
    • Balguerie, A.1    Sivadon, P.2    Bonneu, M.3    Aigle, M.4
  • 8
    • 0027219273 scopus 로고
    • Alteration of a yeast SH3 protein leads to conditional viability and defects in cytoskeletal and budding patterns
    • BAUER, F., M. URDACI, M. AIGLE and M. CROUZET, 1993 Alteration of a yeast SH3 protein leads to conditional viability and defects in cytoskeletal and budding patterns. Mol. Cell. Biol. 13: 5070-5084.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5070-5084
    • Bauer, F.1    Urdaci, M.2    Aigle, M.3    Crouzet, M.4
  • 9
    • 0030758194 scopus 로고    scopus 로고
    • An Escherichia coli host strain useful for efficient overproduction of cloned gene products with NaCl as the inducer
    • BHANDARI, P., and J. GOWRISHANKAR, 1997 An Escherichia coli host strain useful for efficient overproduction of cloned gene products with NaCl as the inducer. J. Bacteriol. 179: 4403-4406.
    • (1997) J. Bacteriol. , vol.179 , pp. 4403-4406
    • Bhandari, P.1    Gowrishankar, J.2
  • 10
    • 0034002308 scopus 로고    scopus 로고
    • Identification of novel, evolutionarily conserved Cdc42p-interacting proteins and of redundant pathways linking Cdc24p and Cdc42p to actin polarization in yeast
    • BI, E., J. B. CHIAVETTA, H. CHEN, G. C. CHEN, C. S. CHAN et al., 2000 Identification of novel, evolutionarily conserved Cdc42p-interacting proteins and of redundant pathways linking Cdc24p and Cdc42p to actin polarization in yeast. Mol. Biol. Cell 11: 773-793.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 773-793
    • Bi, E.1    Chiavetta, J.B.2    Chen, H.3    Chen, G.C.4    Chan, C.S.5
  • 11
    • 0034734849 scopus 로고    scopus 로고
    • A network of proteins around Rvs167p and Rvs161p, two proteins related to the yeast actin cytoskeleton
    • BON, E., P. RECORDON-NAVARRO, P. DURRENS, M. IWASE, A. Ton-E et al., 2000 A network of proteins around Rvs167p and Rvs161p, two proteins related to the yeast actin cytoskeleton. Yeast 13: 1229-1241.
    • (2000) Yeast , vol.13 , pp. 1229-1241
    • Bon, E.1    Recordon-Navarro, P.2    Durrens, P.3    Iwase, M.4    Ton-E, A.5
  • 12
    • 0842324801 scopus 로고    scopus 로고
    • The mechanisms of vesicle budding and fusion
    • BONIFACINO, J. S., and B. S. GLICK, 2004 The mechanisms of vesicle budding and fusion. Cell 116: 153-166.
    • (2004) Cell , vol.116 , pp. 153-166
    • Bonifacino, J.S.1    Glick, B.S.2
  • 13
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: A useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • BRACHMANN, C. B., A. DAVIES, G. J. COST, E. CAPUTO, J. LI et al., 1998 Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast 14: 115-132.
    • (1998) Yeast , vol.14 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5
  • 14
    • 0034887843 scopus 로고    scopus 로고
    • The yeast Rvs161 and Rvs167 proteins are involved in secretory vesicles targeting the plasma membrane and in cell integrity
    • BRETON, A. M., J. SCHAEFFER and M. AIGLE, 2001 The yeast Rvs161 and Rvs167 proteins are involved in secretory vesicles targeting the plasma membrane and in cell integrity. Yeast 18: 1053-1068.
    • (2001) Yeast , vol.18 , pp. 1053-1068
    • Breton, A.M.1    Schaeffer, J.2    Aigle, M.3
  • 15
    • 7244255991 scopus 로고    scopus 로고
    • Gyp5p and Gyl1p are involved in the control of polarized exocytosis in budding yeast
    • CHESNEAU, L., S. DUPRE, A. BURDINA, J. ROGER, S. LEPANSE et al., 2004 Gyp5p and Gyl1p are involved in the control of polarized exocytosis in budding yeast. J. Cell Sci. 117: 4757-4767.
    • (2004) J. Cell Sci. , vol.117 , pp. 4757-4767
    • Chesneau, L.1    Dupre, S.2    Burdina, A.3    Roger, J.4    Lepanse, S.5
  • 16
    • 0032798051 scopus 로고    scopus 로고
    • In vivo analysis of the domains of yeast Rvs167p suggests Rvs167p function is mediated through multiple protein interactions
    • COLWILL, K., D. FIELD, L. MOORE, J. FRIESEN and B. ANDREWS, 1999 In vivo analysis of the domains of yeast Rvs167p suggests Rvs167p function is mediated through multiple protein interactions. Genetics 152: 881-893.
    • (1999) Genetics , vol.152 , pp. 881-893
    • Colwill, K.1    Field, D.2    Moore, L.3    Friesen, J.4    Andrews, B.5
  • 17
    • 0034663597 scopus 로고    scopus 로고
    • Application of multiple sequence alignment profiles to improve protein secondary structure prediction
    • CUFF,J. A., and G.J. BARTON, 2000 Application of multiple sequence alignment profiles to improve protein secondary structure prediction. Proteins 40: 502-511.
    • (2000) Proteins , vol.40 , pp. 502-511
    • Cuff, J.A.1    Barton, G.J.2
  • 18
    • 0037175026 scopus 로고    scopus 로고
    • Significance of GTP hydrolysis in Ypt1p-regulated endoplasmic reticulum to Golgi transport revealed by the analysis of two novel Ypt1-GAPs
    • DE ANTONI, A., J. SCHMITZOVA, H. H. TREPTE, D. GALLWITZ and S. ALBERT, 2002 Significance of GTP hydrolysis in Ypt1p-regulated endoplasmic reticulum to Golgi transport revealed by the analysis of two novel Ypt1-GAPs. J. Biol. Chem. 277: 41023-41031.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41023-41031
    • De Antoni, A.1    Schmitzova, J.2    Trepte, H.H.3    Gallwitz, D.4    Albert, S.5
  • 20
    • 0032488901 scopus 로고    scopus 로고
    • Identification of a Sec4p GTPase-activating protein (GAP) as a novel member of a Rab GAP family
    • DU, L.-L., R. N. COLLINS and P. J. NOVICK, 1998 Identification of a Sec4p GTPase-activating protein (GAP) as a novel member of a Rab GAP family. J. Biol. Chem. 273: 3253-3256.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3253-3256
    • Du, L.-L.1    Collins, R.N.2    Novick, P.J.3
  • 22
    • 0034854464 scopus 로고    scopus 로고
    • Mass spectrometry for the study of protein-protein interactions
    • FIGEYS, D., L. D. MCBROOM and M. F. MORAN, 2001 Mass spectrometry for the study of protein-protein interactions. Methods 24: 230-239.
    • (2001) Methods , vol.24 , pp. 230-239
    • Figeys, D.1    Mcbroom, L.D.2    Moran, M.F.3
  • 23
    • 0038783734 scopus 로고    scopus 로고
    • Regulation of the yeast amphiphysin homologue Rvsl67p by phosphorylation
    • FRIESEN, H., K. MURPHY, A. BREITKREUTZ, M. TYERS and B. ANDREWS, 2003 Regulation of the yeast amphiphysin homologue Rvsl67p by phosphorylation. Mol. Biol. Cell 7: 3027-3040.
    • (2003) Mol. Biol. Cell , vol.7 , pp. 3027-3040
    • Friesen, H.1    Murphy, K.2    Breitkreutz, A.3    Tyers, M.4    Andrews, B.5
  • 24
    • 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., B. L. ANDERSON, H. M. WARRICK, L. A. Pox and J. A. SPUDICH, 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    Pox, L.A.4    Spudich, J.A.5
  • 25
    • 0031026823 scopus 로고    scopus 로고
    • The nuclear receptor homologue Ftz-F1 and the homeodomain protein Ftz are mutually dependent cofactors
    • GUICHET, A., J. W. R. COPELAND, M. ERDELYI, D. HLOUSEK, P. ZAVORSKY et al., 1997 The nuclear receptor homologue Ftz-F1 and the homeodomain protein Ftz are mutually dependent cofactors. Nature 385: 548-552.
    • (1997) Nature , vol.385 , pp. 548-552
    • Guichet, A.1    Copeland, J.W.R.2    Erdelyi, M.3    Hlousek, D.4    Zavorsky, P.5
  • 26
    • 0031036674 scopus 로고    scopus 로고
    • Role of the casein kinase I isoform, HRR25, and the cell cycle regulatory transcription factor, SBF, in the transcriptional response to DNA damage in Saccharomyces cerevisiae
    • HO, Y., S. MASON, R. KOBAYASHI, M. HOEKSTRA and B. ANDREWS, 1997 Role of the casein kinase I isoform, HRR25, and the cell cycle regulatory transcription factor, SBF, in the transcriptional response to DNA damage in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 94: 581-586.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 581-586
    • Ho, Y.1    Mason, S.2    Kobayashi, R.3    Hoekstra, M.4    Andrews, B.5
  • 27
    • 0037050004 scopus 로고    scopus 로고
    • Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectometry
    • Ho, Y., A. GRUHLER, A. HEILBUT, G. D. BADER, L. MOORE et al., 2002 Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectometry. Nature 415: 180-183.
    • (2002) Nature , vol.415 , pp. 180-183
    • Ho, Y.1    Gruhler, A.2    Heilbut, A.3    Bader, G.D.4    Moore, L.5
  • 28
    • 0142184341 scopus 로고    scopus 로고
    • Global analysis of protein localization in budding yeast
    • HUH, W. K., J. V. FALVO, L. C. GERKE, A. S. CARROLL, R. W. HOWSON et al., 2003 Global analysis of protein localization in budding yeast. Nature 425: 686-691.
    • (2003) Nature , vol.425 , pp. 686-691
    • Huh, W.K.1    Falvo, J.V.2    Gerke, L.C.3    Carroll, A.S.4    Howson, R.W.5
  • 29
    • 0035836765 scopus 로고    scopus 로고
    • A comprehensive two-hybrid analysis to explore the yeast protein interactome
    • ITO, T., T. CHIBA, R. OZAWA, M. YOSHIDA, M. HATTORI et al., 2001 A comprehensive two-hybrid analysis to explore the yeast protein interactome. Proc. Natl. Acad. Sci. USA 98: 4569-4574.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4569-4574
    • Ito, T.1    Chiba, T.2    Ozawa, R.3    Yoshida, M.4    Hattori, M.5
  • 30
    • 0344827286 scopus 로고    scopus 로고
    • A pathway for association of receptors, adaptors, and actin during endocytic internalization
    • KAKSONEN, M., Y. SUN and D. G. DRUBIN, 2003 A pathway for association of receptors, adaptors, and actin during endocytic internalization. Cell 115: 475-487.
    • (2003) Cell , vol.115 , pp. 475-487
    • Kaksonen, M.1    Sun, Y.2    Drubin, D.G.3
  • 31
    • 0025259313 scopus 로고
    • Methods for assessing the statistical significance of molecular sequence features by using general scoring schemes
    • KARLIN, S., and S. F. ALTSCHUL, 1990 Methods for assessing the statistical significance of molecular sequence features by using general scoring schemes. Proc. Natl. Acad. Sci. USA 87: 2264-2268.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2264-2268
    • Karlin, S.1    Altschul, S.F.2
  • 32
    • 0027175241 scopus 로고
    • Applications and statistics for multiple high-scoring segments in molecular sequences
    • KARLIN, S., and S. F. ALTSCHUL, 1993 Applications and statistics for multiple high-scoring segments in molecular sequences. Proc. Natl. Acad. Sci. USA 90: 5873-5877.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5873-5877
    • Karlin, S.1    Altschul, S.F.2
  • 33
    • 1942452749 scopus 로고    scopus 로고
    • Proof and evolutionary analysis of ancient genome duplication in the yeast Saccharomyces cerevisiae
    • KELLIS, M., B. W. BIRREN and E. S. LANDER, 2004 Proof and evolutionary analysis of ancient genome duplication in the yeast Saccharomyces cerevisiae. Nature 428: 617-624.
    • (2004) Nature , vol.428 , pp. 617-624
    • Kellis, M.1    Birren, B.W.2    Lander, E.S.3
  • 34
    • 0032882140 scopus 로고    scopus 로고
    • High-copy suppressor analysis reveals a physical interaction between Sec34p and Sec35p, a protein implicated in vesicle docking
    • KIM, D. W., M. SACHER, A. SCARPA, A. M. QUINN and S. FERRO-NOVICK, 1999 High-copy suppressor analysis reveals a physical interaction between Sec34p and Sec35p, a protein implicated in vesicle docking. Mol. Biol. Cell 10: 3317-3329.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3317-3329
    • Kim, D.W.1    Sacher, M.2    Scarpa, A.3    Quinn, A.M.4    Ferro-Novick, S.5
  • 35
    • 0030609041 scopus 로고    scopus 로고
    • Vesicular transport: How many Ypt/Rab GTPases make a eukaryotic cell?
    • LAZAR, T., M. GOTTE and D. GALLWITZ, 1997 Vesicular transport: How many Ypt/Rab GTPases make a eukaryotic cell? Trends Biochem. Sci. 22: 468-472.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 468-472
    • Lazar, T.1    Gotte, M.2    Gallwitz, D.3
  • 36
    • 0032481122 scopus 로고    scopus 로고
    • Interaction of yeast Rvs167 and Pho85 cyclin-dependent kinase complexes may link the cell cycle to the actin cytoskeleton
    • LEE, J., K. COLWILL, V. ANELIUNAS, C. TENNYSON, L. MOORE et al., 1998 Interaction of yeast Rvs167 and Pho85 cyclin-dependent kinase complexes may link the cell cycle to the actin cytoskeleton. Curr. Biol. 8: 1310-1321.
    • (1998) Curr. Biol. , vol.8 , pp. 1310-1321
    • Lee, J.1    Colwill, K.2    Aneliunas, V.3    Tennyson, C.4    Moore, L.5
  • 39
    • 0027241227 scopus 로고
    • Bos1p, an integral membrane protein of the endoplasmic reticulum to Golgi transport vesicles, is required for their fusion competence
    • LIAN, J. P., and S. FERRO-NOVICK, 1993 Bos1p, an integral membrane protein of the endoplasmic reticulum to Golgi transport vesicles, is required for their fusion competence. Cell 73: 735-745.
    • (1993) Cell , vol.73 , pp. 735-745
    • Lian, J.P.1    Ferro-Novick, S.2
  • 40
    • 0031027546 scopus 로고    scopus 로고
    • Evidence for physical and functional interactions among two Saccharomyces cerevisiae SH3 domain proteins, an adenylyl cyclase-associated protein and the actin cytoskeleton
    • LILA, T., and D. DRUBIN, 1997 Evidence for physical and functional interactions among two Saccharomyces cerevisiae SH3 domain proteins, an adenylyl cyclase-associated protein and the actin cytoskeleton. Mol. Biol. Cell 8: 367-385.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 367-385
    • Lila, T.1    Drubin, D.2
  • 41
    • 0035937188 scopus 로고    scopus 로고
    • Rvs161p and Rvs167p, the two yeast amphiphysin homologs, function together in vivo
    • LOMBARDI, R., and H. RIEZMAN, 2001 Rvs161p and Rvs167p, the two yeast amphiphysin homologs, function together in vivo. J. Biol. Chem. 276: 6016-6022.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6016-6022
    • Lombardi, R.1    Riezman, H.2
  • 42
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • LONGTINE, M. S., A. MCKENZIE, D. J. DEMARINI, N. G. SHAH, A. WACH et al., 1998 Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14: 953-961.
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    Mckenzie, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5
  • 43
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • LUPAS, A., M. VAN DYKE and J. STOCK, 1991 Predicting coiled coils from protein sequences. Science 252: 1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 44
    • 0032542018 scopus 로고    scopus 로고
    • Mutagenesis of a buried polar interaction in an SH3 domain: Sequence conservation provides the best prediction of stability effects
    • MAXWELL, K. L., and A. R. DAVIDSON, 1998 Mutagenesis of a buried polar interaction in an SH3 domain: sequence conservation provides the best prediction of stability effects. Biochemistry 37: 16172-16182.
    • (1998) Biochemistry , vol.37 , pp. 16172-16182
    • Maxwell, K.L.1    Davidson, A.R.2
  • 45
    • 0035030510 scopus 로고    scopus 로고
    • SH3 domains: Complexity in moderation
    • MAYER, B. J., 2001 SH3 domains: complexity in moderation. J. Cell Sci. 114: 1253-1263.
    • (2001) J. Cell Sci. , vol.114 , pp. 1253-1263
    • Mayer, B.J.1
  • 46
    • 0028589197 scopus 로고
    • The PCL2 (ORFD)-PHO85 cyclin-dependent kinase complex: A cell cycle regulator in yeast
    • MEASDAY, V., L. MOORE, J. OGAS, M. TYERS and B. ANDREWS, 1994 The PCL2 (ORFD)-PHO85 cyclin-dependent kinase complex: a cell cycle regulator in yeast. Science 266: 1391-1395.
    • (1994) Science , vol.266 , pp. 1391-1395
    • Measday, V.1    Moore, L.2    Ogas, J.3    Tyers, M.4    Andrews, B.5
  • 47
    • 0031017530 scopus 로고    scopus 로고
    • A family of cyclin-like proteins that interact with the cyclin-dependent kinase, Pho85
    • MEASDAY, V., L. MOORE, R. RETNAKARAN, J. LEE, M. DONOVIEL et al., 1997 A family of cyclin-like proteins that interact with the cyclin-dependent kinase, Pho85. Mol. Cell. Biol. 17: 1212-1223.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1212-1223
    • Measday, V.1    Moore, L.2    Retnakaran, R.3    Lee, J.4    Donoviel, M.5
  • 48
    • 0030930123 scopus 로고    scopus 로고
    • Yeast actin cytoskeleton mutants accumulate a new class of Golgi-derived secretary vesicle
    • MULHOLLAND, J., A. WESP, H. RIEZMAN and D. BOTSTEIN, 1997 Yeast actin cytoskeleton mutants accumulate a new class of Golgi-derived secretary vesicle. Mol. Biol. Cell 8: 1481-1499.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1481-1499
    • Mulholland, J.1    Wesp, A.2    Riezman, H.3    Botstein, D.4
  • 49
    • 0035952983 scopus 로고    scopus 로고
    • Molecular requirements for the internalisation step of endocytosis: Insights from yeast
    • MUNN, A., 2001 Molecular requirements for the internalisation step of endocytosis: insights from yeast. Biochim. Biophys. Acta 1535: 236-257.
    • (2001) Biochim. Biophys. Acta , vol.1535 , pp. 236-257
    • Munn, A.1
  • 50
    • 0031555306 scopus 로고    scopus 로고
    • Protein-protein interaction between the RVS161 and RVS167 gene products of Saccharomyces cerevisiae
    • NAVARRO, P., P. DURRENS and M. AIGLE, 1997 Protein-protein interaction between the RVS161 and RVS167 gene products of Saccharomyces cerevisiae. Biochim. Biophys. Acta 1343: 187-192.
    • (1997) Biochim. Biophys. Acta , vol.1343 , pp. 187-192
    • Navarro, P.1    Durrens, P.2    Aigle, M.3
  • 51
    • 0030758036 scopus 로고    scopus 로고
    • A shared domain between a spindle assembly checkpoint protein and Ypt/Rab-specific GTPase activators
    • NEUWALD, A. F., 1997 A shared domain between a spindle assembly checkpoint protein and Ypt/Rab-specific GTPase activators. Trends Biochem. Sci. 22: 22-23.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 22-23
    • Neuwald, A.F.1
  • 52
    • 0021906692 scopus 로고
    • Phenotypic analysis of temperature-sensitive yeast actin mutants
    • NOVICK, P., and D. BOTSTEIN, 1985 Phenotypic analysis of temperature-sensitive yeast actin mutants. Cell 40: 405-416.
    • (1985) Cell , vol.40 , pp. 405-416
    • Novick, P.1    Botstein, D.2
  • 53
    • 0034648797 scopus 로고    scopus 로고
    • Topological restriction of SNARE-dependent membrane fusion
    • PARLATI, F. J. A. MCNEW, R. FUKUDA, R. MILLER, T. H. SOLLNER et al., 2000 Topological restriction of SNARE-dependent membrane fusion. Nature 407: 194-198.
    • (2000) Nature , vol.407 , pp. 194-198
    • Parlati, F.1    Mcnew, J.A.2    Fukuda, R.3    Miller, R.4    Sollner, T.H.5
  • 54
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • PAWSON, T., and J. D. SCOTT, 1997 Signaling through scaffold, anchoring, and adaptor proteins. Science 278: 2075-2080.
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 55
    • 1442317538 scopus 로고    scopus 로고
    • BAR domains as sensors of membrane curvature: The amphiphysin BAR structure
    • PETER, B. J., H. KENT, I. G. MILLS, Y. VALLIS, P. J. BUTLER et al., 2004 BAR domains as sensors of membrane curvature: the amphiphysin BAR structure. Science 303: 495-499.
    • (2004) Science , vol.303 , pp. 495-499
    • Peter, B.J.1    Kent, H.2    Mills, I.G.3    Vallis, Y.4    Butler, P.J.5
  • 56
    • 0036260725 scopus 로고    scopus 로고
    • Ordering of compartments in the yeast endocytic pathway
    • PRESCIANOTTO-BASCHONG, C., and H. RIEZMAN, 2002 Ordering of compartments in the yeast endocytic pathway. Traffic 3: 37-49.
    • (2002) Traffic , vol.3 , pp. 37-49
    • Prescianotto-Baschong, C.1    Riezman, H.2
  • 57
    • 0027056183 scopus 로고
    • Characterization of the Saccharomyces Golgi complex through the cell cycle by immunoelectron microscopy
    • PREUSS, D., J. MULHOLLAND, A. FRANZUSOFF, N. SEGEV and D. BOTSTEIN, 1992 Characterization of the Saccharomyces Golgi complex through the cell cycle by immunoelectron microscopy. Mol. Biol. Cell 3: 789-803.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 789-803
    • Preuss, D.1    Mulholland, J.2    Franzusoff, A.3    Segev, N.4    Botstein, D.5
  • 58
    • 0034056057 scopus 로고    scopus 로고
    • Polarization of cell growth in yeast. II. The role of the cortical actin cytoskeleton
    • PRUYNE, D., and A. BRETSCHER, 2000 Polarization of cell growth in yeast. II. The role of the cortical actin cytoskeleton. J. Cell Sci. 113: 571-585.
    • (2000) J. Cell Sci. , vol.113 , pp. 571-585
    • Pruyne, D.1    Bretscher, A.2
  • 59
    • 0034596986 scopus 로고    scopus 로고
    • Crystal structure of the GAP domain of Gyp1p: First insights into interaction with Ypt/Rab proteins
    • RAK, A., R. FEDOROV, K. ALEXANDROV, S. ALBERT, R. S. GOODY et al., 2000 Crystal structure of the GAP domain of Gyp1p: first insights into interaction with Ypt/Rab proteins. EMBO J. 19: 5105-5113.
    • (2000) EMBO J. , vol.19 , pp. 5105-5113
    • Rak, A.1    Fedorov, R.2    Alexandrov, K.3    Albert, S.4    Goody, R.S.5
  • 60
    • 0030838041 scopus 로고    scopus 로고
    • Use of conditional promoters for expression of heterologous proteins in Saccharomyces cerevisiae
    • RONTCKE, V., W. GRAULICH, D. MUMBERG, R. MULLER and M. FUNK, 1997 Use of conditional promoters for expression of heterologous proteins in Saccharomyces cerevisiae. Methods Enzymol. 283: 313-322.
    • (1997) Methods Enzymol. , vol.283 , pp. 313-322
    • Rontcke, V.1    Graulich, W.2    Mumberg, D.3    Muller, R.4    Funk, M.5
  • 61
    • 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., C. A. REINKE, B. J. BEVIS, A. T. HAMMOND, I. B. SEARS el al., 2001 A role for actin, Cdc1p, and Myo2p in the inheritance of late Golgi elements in Saccharomyces cerevisiae. J. Cell. Biol. 153: 47-62.
    • (2001) J. Cell. Biol. , vol.153 , pp. 47-62
    • Rossanese, O.W.1    Reinke, C.A.2    Bevis, B.J.3    Hammond, A.T.4    Sears, I.B.5
  • 62
    • 0242268461 scopus 로고    scopus 로고
    • Predicting protein functions from redundancies in large-scale protein interaction networks
    • SAMANTA, M. P., and S. LIANG, 2003 Predicting protein functions from redundancies in large-scale protein interaction networks. Proc. Natl. Acad. Sci. USA 100: 12579-12583.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12579-12583
    • Samanta, M.P.1    Liang, S.2
  • 63
    • 0025770571 scopus 로고
    • Mediation of the attachment or fusion step in vesicular transport by the GTP-binding Ypt1 protein
    • SEGEV, N., 1991 Mediation of the attachment or fusion step in vesicular transport by the GTP-binding Ypt1 protein. Science 252:1553-1556.
    • (1991) Science , vol.252 , pp. 1553-1556
    • Segev, N.1
  • 64
    • 0035425411 scopus 로고    scopus 로고
    • Ypt and Rab GTPases: Insight into functions through novel interactions
    • SEGEV, N., 2001 Ypt and Rab GTPases: insight into functions through novel interactions. Curr. Opin. Cell Biol. 13: 500-511.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 500-511
    • Segev, N.1
  • 65
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • SHEVCHENKO, A., M. WILM, O. VORM and M. MANN, 1996 Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68: 850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 66
    • 1842338743 scopus 로고    scopus 로고
    • Use of a synthetic lethal screen to identify yeast mutants impaired in endocytosis, vacuolar protein sorting and the organization of the cytoskeleton
    • SINGER-KRUGER, B., and S. FERRO-NOVICK, 1997 Use of a synthetic lethal screen to identify yeast mutants impaired in endocytosis, vacuolar protein sorting and the organization of the cytoskeleton. Eur. J. Cell Biol. 74: 365-375.
    • (1997) Eur. J. Cell Biol. , vol.74 , pp. 365-375
    • Singer-Kruger, B.1    Ferro-Novick, S.2
  • 67
    • 0030697988 scopus 로고    scopus 로고
    • Functional assessment of the yeast Rvs161 and Rvs167 protein domains
    • SIVADON, P., M. CROUZET and M. AIGLE, 1997 Functional assessment of the yeast Rvs161 and Rvs167 protein domains. FEBS Lett. 417: 21-27.
    • (1997) FEBS Lett. , vol.417 , pp. 21-27
    • Sivadon, P.1    Crouzet, M.2    Aigle, M.3
  • 68
    • 22144460177 scopus 로고    scopus 로고
    • A novel link between a Rab GTPase and Rvs proteins: The yeast amphiphysin homologues
    • in press
    • TALAREK, N., A. BALGUERIE, M. AIGLE and P. DURRENS, 2005 A novel link between a Rab GTPase and Rvs proteins: the yeast amphiphysin homologues. Cell Biochem. Funct. 23 (in press).
    • (2005) Cell Biochem. Funct. , vol.23
    • Talarek, N.1    Balguerie, A.2    Aigle, M.3    Durrens, P.4
  • 69
    • 0035204230 scopus 로고    scopus 로고
    • Assembly and regulation of the cytokinetic apparatus in budding yeast
    • TOLLIDAY, N., N. BOUQUIN and R. LI, 2001 Assembly and regulation of the cytokinetic apparatus in budding yeast. Curr. Opin. Microbiol. 4:690-695.
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 690-695
    • Tolliday, N.1    Bouquin, N.2    Li, R.3
  • 70
    • 10744230485 scopus 로고    scopus 로고
    • Global mapping of the yeast genetic interaction network
    • TONG, A. H., G. LESAGE, G. D. BADER, H. DING, H. XU et al., 2004 Global mapping of the yeast genetic interaction network. Science 303: 808-813.
    • (2004) Science , vol.303 , pp. 808-813
    • Tong, A.H.1    Lesage, G.2    Bader, G.D.3    Ding, H.4    Xu, H.5
  • 71
    • 0035861532 scopus 로고    scopus 로고
    • Systematic genetic analysis with ordered arrays of yeast deletion mutants
    • TONG, A. H. Y., M. EVANGELISTA, A. B. PARSONS, H. XU, G. D. BADER et al., 2001 Systematic genetic analysis with ordered arrays of yeast deletion mutants. Science 294: 2364-2368.
    • (2001) Science , vol.294 , pp. 2364-2368
    • Tong, A.H.Y.1    Evangelista, M.2    Parsons, A.B.3    Xu, H.4    Bader, G.D.5
  • 72
    • 0037059461 scopus 로고    scopus 로고
    • A combined experimental and computational strategy to define protein interaction networks for peptide recognition modules
    • TONG, A. H. Y, B. DREES, G. NARDELLI, G. D. BADER, B. BRANNETTI el al., 2002 A combined experimental and computational strategy to define protein interaction networks for peptide recognition modules. Science 295: 321-324.
    • (2002) Science , vol.295 , pp. 321-324
    • Tong, A.H.Y.1    Drees, B.2    Nardelli, G.3    Bader, G.D.4    Brannetti, B.5
  • 73
    • 0034628508 scopus 로고    scopus 로고
    • A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae
    • UETZ, P., L. GIOT, G. CAGNEY, T. MANSFIELD, R. S. JUDSON et al., 2000 A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature 403: 623-627.
    • (2000) Nature , vol.403 , pp. 623-627
    • Uetz, P.1    Giot, L.2    Cagney, G.3    Mansfield, T.4    Judson, R.S.5
  • 74
    • 0033529707 scopus 로고    scopus 로고
    • Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis
    • WINZELER, E., D. D. SHOEMAKER, A. ASTROMOFF, H. LIANG, K. ANDERSON et al., 1999 Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis. Science 285: 901-906.
    • (1999) Science , vol.285 , pp. 901-906
    • Winzeler, E.1    Shoemaker, D.D.2    Astromoff, A.3    Liang, H.4    Anderson, K.5
  • 75
    • 0030947344 scopus 로고    scopus 로고
    • Molecular evidence for an ancient duplication of the entire yeast genome
    • WOLFE, K. H., and D. C. SHIELDS, 1997 Molecular evidence for an ancient duplication of the entire yeast genome. Nature 387: 708-713.
    • (1997) Nature , vol.387 , pp. 708-713
    • Wolfe, K.H.1    Shields, D.C.2
  • 76
    • 0036651754 scopus 로고    scopus 로고
    • Amphiphysins: Raising the BAR for synaptic vesicle recycling and membrane dynamics. Bin-Amphiphysin-Rvsp
    • ZHANG, B., and A. C. ZELHOF, 2002 Amphiphysins: raising the BAR for synaptic vesicle recycling and membrane dynamics. Bin-Amphiphysin-Rvsp. Traffic 3: 452-460.
    • (2002) Traffic , vol.3 , pp. 452-460
    • Zhang, B.1    Zelhof, A.C.2


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