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Volumn 173, Issue 2, 2006, Pages 527-539

Identification of novel mutations in ACT1 and SLA2 that suppress the actin-cable-overproducing phenotype caused by overexpression of a dominant active form of Bni1p in Saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN 1; AMINO ACID; MEMBRANE PROTEIN; METHENAMINE; MONOMER; MUTANT PROTEIN; PROFILIN; PROTEIN BNI1 DELTA; PROTEIN BNI1P; PROTEIN BUD6; PROTEIN SLA2; UNCLASSIFIED DRUG;

EID: 33745403827     PISSN: 00166731     EISSN: 00166731     Source Type: Journal    
DOI: 10.1534/genetics.105.055210     Document Type: Article
Times cited : (7)

References (60)
  • 1
    • 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
  • 2
    • 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., J. STRYKER, N. POKALA, M. SANDERS, P. CREWS et al., 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
  • 3
    • 0032494082 scopus 로고    scopus 로고
    • The yeast V159N actin mutant reveals roles for actin dynamics in vivo
    • BELMONT, L. D., and D. G DRUBIN, 1998 The yeast V159N actin mutant reveals roles for actin dynamics in vivo. J. Cell Biol. 142: 1289-1299.
    • (1998) J. Cell Biol. , vol.142 , pp. 1289-1299
    • Belmont, L.D.1    Drubin, D.G.2
  • 4
    • 0035736350 scopus 로고    scopus 로고
    • Large-scale identification of genes important for apical growth in Saccharomyces cerevisiae by directed allele replacement technology (DART) screening
    • BIDLINGMAIER, S., and M. SNYDER, 2002 Large-scale identification of genes important for apical growth in Saccharomyces cerevisiae by directed allele replacement technology (DART) screening. Funct. Integr. Genomics 1: 345-356.
    • (2002) Funct. Integr. Genomics , vol.1 , pp. 345-356
    • Bidlingmaier, S.1    Snyder, M.2
  • 5
    • 0033866402 scopus 로고    scopus 로고
    • The two proteins Pat1p (Mrt1p) and Spb8p interact in vivo, are required for mRNA decay, and are functionally linked to Pab1p
    • BONNEROT, C., R. BOECK and B. LAPEYRE, 2000 The two proteins Pat1p (Mrt1p) and Spb8p interact in vivo, are required for mRNA decay, and are functionally linked to Pab1p. Mol. Cell. Biol. 20: 5939-5946.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5939-5946
    • Bonnerot, C.1    Boeck, R.2    Lapeyre, B.3
  • 7
    • 0029966290 scopus 로고    scopus 로고
    • Movement of yeast cortical actin cytoskeleton visualized in vivo
    • USA
    • DOYLE, T., and D. BOTSTEIN, 1996 Movement of yeast cortical actin cytoskeleton visualized in vivo. Proc. Natl. Acad. Sci. USA 93: 3886-3891.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 3886-3891
    • Doyle, T.1    Botstein, D.2
  • 8
    • 0027765526 scopus 로고
    • Actin structure and function: Roles in mitochondrial organization and morphogenesis in budding yeast and identification of the phalloidin-binding site
    • DRUBIN, D. G., H. D. JONES and K. F. WERTMAN, 1993 Actin structure and function: roles in mitochondrial organization and morphogenesis in budding yeast and identification of the phalloidin-binding site. Mol. Biol. Cell 4: 1277-1294.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1277-1294
    • Drubin, D.G.1    Jones, H.D.2    Wertman, K.F.3
  • 9
    • 0025307598 scopus 로고
    • Null alleles of SAC7 suppress temperature-sensitive actin mutations in Saccharomyces cerevisiae
    • DUNN, T. M., and D. SHORTLE, 1990 Null alleles of SAC7 suppress temperature-sensitive actin mutations in Saccharomyces cerevisiae. Mol. Cell. Biol. 10: 2308-2314.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2308-2314
    • Dunn, T.M.1    Shortle, D.2
  • 10
    • 0026703547 scopus 로고
    • A simple and efficient procedure for transformation of yeasts
    • ELBLE, R., 1992 A simple and efficient procedure for transformation of yeasts. Biotechniques 13: 18-20.
    • (1992) Biotechniques , vol.13 , pp. 18-20
    • Elble, R.1
  • 12
    • 0030932405 scopus 로고    scopus 로고
    • Bni1p, a yeast formin linking Cdc42p and the actin cytoskeleton during polarized morphogenesis
    • EVANGELISTA, M., K. BLUNDELL, M. S. LONGTINE, C. J. CHOW, N. ADAMES et al., 1997 Bni1p, a yeast formin linking Cdc42p and the actin cytoskeleton during polarized morphogenesis. Science 276: 118-122.
    • (1997) Science , vol.276 , pp. 118-122
    • Evangelista, M.1    Blundell, K.2    Longtine, M.S.3    Chow, C.J.4    Adames, N.5
  • 13
    • 0036514271 scopus 로고    scopus 로고
    • Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast
    • EVANGELISTA, M., D. PRUYNE, D. C. AMBERG, C. BOONE and A. BRETSCHER, 2002 Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast. Nat. Cell Biol. 4: 32-41.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 32-41
    • Evangelista, M.1    Pruyne, D.2    Amberg, D.C.3    Boone, C.4    Bretscher, A.5
  • 14
    • 0038445654 scopus 로고    scopus 로고
    • Formins: Signaling effectors for assembly and polarization of actin filaments
    • EVANGELISTA, M., S. ZIGMOND and C. BOONE, 2003 Formins: signaling effectors for assembly and polarization of actin filaments. J. Cell Sci. 116: 2603-2611.
    • (2003) J. Cell Sci. , vol.116 , pp. 2603-2611
    • Evangelista, M.1    Zigmond, S.2    Boone, C.3
  • 15
    • 2442659247 scopus 로고    scopus 로고
    • The deubiquitinating enzyme Doa4p protects cells from DNA topoisomerase I poisons
    • FIORANI, P., R. J. REID, A. SCHEPIS, H. R. JACQUIAU, H. GUO et al., 2004 The deubiquitinating enzyme Doa4p protects cells from DNA topoisomerase I poisons. J. Biol. Chem. 279: 21271-21281.
    • (2004) J. Biol. Chem. , vol.279 , pp. 21271-21281
    • Fiorani, P.1    Reid, R.J.2    Schepis, A.3    Jacquiau, H.R.4    Guo, H.5
  • 16
    • 0037125940 scopus 로고    scopus 로고
    • Drs2p-dependent formation of exocytic clathrin-coated vesicles in vivo
    • GALL, W. E., N. C. GEETHING, Z. HUA, M. F. INGRAM, K. LIU et al., 2002 Drs2p-dependent formation of exocytic clathrin-coated vesicles in vivo. Curr. Biol. 12: 1623-1627.
    • (2002) Curr. Biol. , vol.12 , pp. 1623-1627
    • Gall, W.E.1    Geething, N.C.2    Hua, Z.3    Ingram, M.F.4    Liu, K.5
  • 17
    • 0036270543 scopus 로고    scopus 로고
    • Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method
    • GIETZ, R. D., and R. A. WOODS, 2002 Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method. Methods Enzymol. 350: 87-96.
    • (2002) Methods Enzymol. , vol.350 , pp. 87-96
    • Gietz, R.D.1    Woods, R.A.2
  • 18
    • 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
  • 19
    • 0029018708 scopus 로고
    • Identification of a new family of tissue-specific basic helix-loop-helix proteins with a two-hybrid system
    • HOLLENBERG, S. M., R. STERNGLANZ, P. F. CHENG and H. WEINTRAUB, 1995 Identification of a new family of tissue-specific basic helix-loop-helix proteins with a two-hybrid system. Mol. Cell. Biol. 15: 3813-3822.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3813-3822
    • Hollenberg, S.M.1    Sternglanz, R.2    Cheng, P.F.3    Weintraub, H.4
  • 20
    • 0027244817 scopus 로고
    • Synthetic-lethal interactions identify two novel genes, SLA1 and SLA2, that control membrane cytoskeleton assembly in Saccharomyces cerevisiae
    • HOLTZMAN, D. A., S. YANG and D. G. DRUBIN, 1993 Synthetic-lethal interactions identify two novel genes, SLA1 and SLA2, that control membrane cytoskeleton assembly in Saccharomyces cerevisiae. J. Cell Biol. 122: 635-644.
    • (1993) J. Cell Biol. , vol.122 , pp. 635-644
    • Holtzman, D.A.1    Yang, S.2    Drubin, D.G.3
  • 21
    • 0030927327 scopus 로고    scopus 로고
    • Bni1p and Bnr1p: Downstream targets of the Rho family small G-proteins which interact with profilin and regulate actin cytoskeleton in Saccharomyces cerevisiae
    • IMAMURA, H., K. TANAKA, T. HIHARA, M. UMIKAWA, T. KAMEI et al., 1997 Bni1p and Bnr1p: downstream targets of the Rho family small G-proteins which interact with profilin and regulate actin cytoskeleton in Saccharomyces cerevisiae. EMBO J. 16: 2745-2755.
    • (1997) EMBO J. , vol.16 , pp. 2745-2755
    • Imamura, H.1    Tanaka, K.2    Hihara, T.3    Umikawa, M.4    Kamei, T.5
  • 22
    • 9444257597 scopus 로고    scopus 로고
    • Septin ring assembly requires concerted action of polarisome components, a PAK kinase Cla4p, and the actin cytoskeleton in Saccharomyces cerevisiae
    • KADOTA, J., T. YAMAMOTO, S. YOSHIUCHI, E. BI and K. TANAKA, 2004 Septin ring assembly requires concerted action of polarisome components, a PAK kinase Cla4p, and the actin cytoskeleton in Saccharomyces cerevisiae. Mol. Biol. Cell 15: 5329-5345.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5329-5345
    • Kadota, J.1    Yamamoto, T.2    Yoshiuchi, S.3    Bi, E.4    Tanaka, K.5
  • 23
    • 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
  • 24
    • 0032561342 scopus 로고    scopus 로고
    • Interaction of Bnr1p with a novel Src homology 3 domain-containing Hof1p. Implication in cytokinesis in Saccharomyces cerevisiae
    • KAMEI, T., K. TANAKA, T. HIHARA, M. UMIKAWA, H. IMAMURA et al., 1998 Interaction of Bnr1p with a novel Src homology 3 domain-containing Hof1p. Implication in cytokinesis in Saccharomyces cerevisiae. J. Biol. Chem. 273: 28341-28345.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28341-28345
    • Kamei, T.1    Tanaka, K.2    Hihara, T.3    Umikawa, M.4    Imamura, H.5
  • 25
    • 0029591856 scopus 로고
    • Actin filaments in yeast are unstable in the absence of capping protein or fimbrin
    • KARPOVA, T. S., K. TATCHELL and J. A. COOPER, 1995 Actin filaments in yeast are unstable in the absence of capping protein or fimbrin. J. Cell Biol. 131: 1483-1493.
    • (1995) J. Cell Biol. , vol.131 , pp. 1483-1493
    • Karpova, T.S.1    Tatchell, K.2    Cooper, J.A.3
  • 26
    • 0034084906 scopus 로고    scopus 로고
    • Role of actin and Myo2p in polarized secretion and growth of Saccharomyces cerevisiae
    • KARPOVA, T. S., S. L. RECK-PETERSON, N. B. ELKIND, M. S. MOOSEKER, P. J. NOVICK et al., 2000 Role of actin and Myo2p in polarized secretion and growth of Saccharomyces cerevisiae. Mol. Biol. Cell 11: 1727-1737.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1727-1737
    • Karpova, T.S.1    Reck-Peterson, S.L.2    Elkind, N.B.3    Mooseker, M.S.4    Novick, P.J.5
  • 27
    • 0033556056 scopus 로고    scopus 로고
    • A positive selection for plasmid loss in Saccharomyces cerevisiae using galactose-inducible growth inhibitory sequences
    • KAWAHATA, M., S. AMARI, Y. NISHIZAWA and R. AKADA, 1999 A positive selection for plasmid loss in Saccharomyces cerevisiae using galactose-inducible growth inhibitory sequences. Yeast 15: 1-10.
    • (1999) Yeast , vol.15 , pp. 1-10
    • Kawahata, M.1    Amari, S.2    Nishizawa, Y.3    Akada, R.4
  • 28
    • 0033604447 scopus 로고    scopus 로고
    • An FH domain-containing Bnr1p is a multifunctional protein interacting with a variety of cytoskeletal proteins in Saccharomyces cerevisiae
    • KIKYO, M., K. TANAKA, T. KAMEI, K. OZAKI, T. FUJIWARA et al., 1999 An FH domain-containing Bnr1p is a multifunctional protein interacting with a variety of cytoskeletal proteins in Saccharomyces cerevisiae. Oncogene 18: 7046-7054.
    • (1999) Oncogene , vol.18 , pp. 7046-7054
    • Kikyo, M.1    Tanaka, K.2    Kamei, T.3    Ozaki, K.4    Fujiwara, T.5
  • 29
    • 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, III, 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 III, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5
  • 30
    • 0030908297 scopus 로고    scopus 로고
    • The I/LWEQ module: A conserved sequence that signifies F-actin binding in functionally diverse proteins from yeast to mammals
    • USA
    • MCCANN, R. O., and S. W. CRAIG, 1997 The I/LWEQ module: a conserved sequence that signifies F-actin binding in functionally diverse proteins from yeast to mammals. Proc. Natl. Acad. Sci. USA 94: 5679-5684.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 5679-5684
    • McCann, R.O.1    Craig, S.W.2
  • 31
    • 0036196880 scopus 로고    scopus 로고
    • The novel adaptor protein, Mti1p, and Vrp1p, a homolog of Wiskott-Aldrich syndrome protein-interacting protein (WIP), may antagonistically regulate type I myosins in Saccharomyces cerevisiae
    • MOCHIDA, J., T. YAMAMOTO, K. FUJIMURA-KAMADA and K. TANAKA, 2002 The novel adaptor protein, Mti1p, and Vrp1p, a homolog of Wiskott-Aldrich syndrome protein-interacting protein (WIP), may antagonistically regulate type I myosins in Saccharomyces cerevisiae. Genetics 160: 923-934.
    • (2002) Genetics , vol.160 , pp. 923-934
    • Mochida, J.1    Yamamoto, T.2    Fujimura-Kamada, K.3    Tanaka, K.4
  • 32
    • 0742305302 scopus 로고    scopus 로고
    • A conserved mechanism for Bni1- and mDia1-induced actin assembly and dual regulation of Bni1 by Bud6 and profilin
    • MOSELEY, J. B., I. SAGOT, A. L. MANNING, Y. XU, M. J. ECK et al., 2004 A conserved mechanism for Bni1- and mDia1-induced actin assembly and dual regulation of Bni1 by Bud6 and profilin. Mol. Biol. Cell 15: 896-907.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 896-907
    • Moseley, J.B.1    Sagot, I.2    Manning, A.L.3    Xu, Y.4    Eck, M.J.5
  • 33
    • 0028204439 scopus 로고
    • Ultrastructure of the yeast actin cytoskeleton and its association with the plasma membrane
    • MULHOLLAND, J., D. PREUSS, A. MOON, A. WONG, D. DRUBIN et al., 1994 Ultrastructure of the yeast actin cytoskeleton and its association with the plasma membrane. J. Cell Biol. 125: 381-391.
    • (1994) J. Cell Biol. , vol.125 , pp. 381-391
    • Mulholland, J.1    Preuss, D.2    Moon, A.3    Wong, A.4    Drubin, D.5
  • 34
    • 0030930123 scopus 로고    scopus 로고
    • Yeast actin cytoskeleton mutants accumulate a new class of Golgiderived secretary vesicle
    • MULHOLLAND, J., A. WESP, H. RIEZMAN and D. BOTSTEIN, 1997 Yeast actin cytoskeleton mutants accumulate a new class of Golgiderived 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
  • 35
    • 0028934931 scopus 로고
    • MOP2 (SLA2) affects the abundance of the plasma membrane H(+)-ATPase of Saccharomyces cerevisiae
    • NA, S., M. HINCAPIE, J. H. MCCUSKER and J. E. HABER, 1995 MOP2 (SLA2) affects the abundance of the plasma membrane H(+)-ATPase of Saccharomyces cerevisiae. J. Biol. Chem. 270: 6815-6823.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6815-6823
    • Na, S.1    Hincapie, M.2    McCusker, J.H.3    Haber, J.E.4
  • 36
    • 13444280218 scopus 로고    scopus 로고
    • Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain
    • OTOMO, T., D. R. TOMCHICK, C. OTOMO, S. C. PANCHAL, M. MACHIUS et al., 2005 Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain. Nature 433: 488-494.
    • (2005) Nature , vol.433 , pp. 488-494
    • Otomo, T.1    Tomchick, D.R.2    Otomo, C.3    Panchal, S.C.4    Machius, M.5
  • 37
    • 0029920783 scopus 로고    scopus 로고
    • Rom1p and Rom2p are GDP/GTP exchange proteins (GEPs) for the Rho1p small GTP binding protein in Saccharomyces cerevisiae
    • OZAKI, K., K. TANAKA, H. IMAMURA, T. HIHARA, T. KAMEYAMA et al., 1996 Rom1p and Rom2p are GDP/GTP exchange proteins (GEPs) for the Rho1p small GTP binding protein in Saccharomyces cerevisiae. EMBO J. 15: 2196-2207.
    • (1996) EMBO J. , vol.15 , pp. 2196-2207
    • Ozaki, K.1    Tanaka, K.2    Imamura, H.3    Hihara, T.4    Kameyama, T.5
  • 39
    • 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
  • 40
    • 0032576569 scopus 로고    scopus 로고
    • Tropomyosin-containing actin cables direct the Myo2p-dependent polarized delivery of secretory vesicles in budding yeast
    • PRUYNE, D.W., D. H. SCHOTT and A. BRETSCHER, 1998 Tropomyosin-containing actin cables direct the Myo2p-dependent polarized delivery of secretory vesicles in budding yeast. J. Cell Biol. 143: 1931-1945.
    • (1998) J. Cell Biol. , vol.143 , pp. 1931-1945
    • Pruyne, D.W.1    Schott, D.H.2    Bretscher, A.3
  • 41
    • 0037178706 scopus 로고    scopus 로고
    • Role of formins in actin assembly: Nucleation and barbed-end association
    • PRUYNE, D., M. EVANGELISTA, C. YANG, E. BI, S. ZIGMOND et al., 2002 Role of formins in actin assembly: nucleation and barbed-end association. Science 297: 612-615.
    • (2002) Science , vol.297 , pp. 612-615
    • Pruyne, D.1    Evangelista, M.2    Yang, C.3    Bi, E.4    Zigmond, S.5
  • 42
    • 0027455339 scopus 로고
    • end3 and end4: Two mutants defective in receptor-mediated and fluid-phase endocytosis in Saccharomyces cerevisiae
    • RATHS, S., J. ROHRER, F. CRAUSAZ and H. RIEZMAN, 1993 end3 and end4: two mutants defective in receptor-mediated and fluid-phase endocytosis in Saccharomyces cerevisiae. J. Cell Biol. 120: 55-65.
    • (1993) J. Cell Biol. , vol.120 , pp. 55-65
    • Raths, S.1    Rohrer, J.2    Crausaz, F.3    Riezman, H.4
  • 43
    • 0037599264 scopus 로고    scopus 로고
    • Negative regulation of yeast WASp by two SH3 domain-containing proteins
    • RODAL, A. A., A. L. MANNING, B. L. GOODE and D. G. DRUBIN, 2003 Negative regulation of yeast WASp by two SH3 domain-containing proteins. Curr. Biol. 13: 1000-1008.
    • (2003) Curr. Biol. , vol.13 , pp. 1000-1008
    • Rodal, A.A.1    Manning, A.L.2    Goode, B.L.3    Drubin, D.G.4
  • 44
    • 7044224754 scopus 로고    scopus 로고
    • Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis
    • ROMERO, S., C. LE CLAINCHE, D. DIDRY, C. EGILE, D. PANTALONI et al., 2004 Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis. Cell 119: 419-429.
    • (2004) Cell , vol.119 , pp. 419-429
    • Romero, S.1    Le Clainche, C.2    Didry, D.3    Egile, C.4    Pantaloni, D.5
  • 45
    • 0036141585 scopus 로고    scopus 로고
    • Yeast formins regulate cell polarity by controlling the assembly of actin cables
    • SAGOT, I., S. K. KLEE and D. PELLMAN, 2002a Yeast formins regulate cell polarity by controlling the assembly of actin cables. Nat. Cell Biol. 4: 42-50.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 42-50
    • Sagot, I.1    Klee, S.K.2    Pellman, D.3
  • 47
    • 0036275447 scopus 로고    scopus 로고
    • Getting started with yeast
    • SHERMAN, F., 2002 Getting started with yeast. Methods Enzymol. 350: 3-41.
    • (2002) Methods Enzymol. , vol.350 , pp. 3-41
    • Sherman, F.1
  • 48
    • 0031835436 scopus 로고    scopus 로고
    • Spa2p interacts with cell polarity proteins and signaling components involved in yeast cell morphogenesis
    • SHEU, Y. J., B. SANTOS, N. FORTIN, C. COSTIGAN and M. SNYDER, 1998 Spa2p interacts with cell polarity proteins and signaling components involved in yeast cell morphogenesis. Mol. Cell. Biol. 18: 4053-4069.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4053-4069
    • Sheu, Y.J.1    Santos, B.2    Fortin, N.3    Costigan, C.4    Snyder, M.5
  • 49
    • 0033919372 scopus 로고    scopus 로고
    • Polarized growth controls cell shape and bipolar bud site selection in Saccharomyces cerevisiae
    • SHEU, Y. J., Y. BARRAL and M. SNYDER, 2000 Polarized growth controls cell shape and bipolar bud site selection in Saccharomyces cerevisiae. Mol. Cell. Biol. 20: 5235-5247.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5235-5247
    • Sheu, Y.J.1    Barral, Y.2    Snyder, M.3
  • 50
    • 0021269292 scopus 로고
    • Construction and genetic characterization of temperature-sensitive mutant alleles of the yeast actin gene
    • USA
    • SHORTLE, D., P. NOVICK and D. BOTSTEIN, 1984 Construction and genetic characterization of temperature-sensitive mutant alleles of the yeast actin gene. Proc. Natl. Acad. Sci. USA 81: 4889-4893.
    • (1984) Proc. Natl. Acad. Sci. , vol.81 , pp. 4889-4893
    • Shortle, D.1    Novick, P.2    Botstein, D.3
  • 51
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • SIKORSKI, R. S., and P. HIETER, 1989 A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122: 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 52
    • 0035023988 scopus 로고    scopus 로고
    • The life cycle of actin patches in mating yeast
    • SMITH, M. G., S. R. SWAMY and L. A. PON, 2001 The life cycle of actin patches in mating yeast. J. Cell Sci. 114: 1505-1513.
    • (2001) J. Cell Sci. , vol.114 , pp. 1505-1513
    • Smith, M.G.1    Swamy, S.R.2    Pon, L.A.3
  • 54
    • 0035861532 scopus 로고    scopus 로고
    • Systematic genetic analysis with ordered arrays of yeast deletion mutants
    • TONG, A. H., 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.1    Evangelista, M.2    Parsons, A.B.3    Xu, H.4    Bader, G.D.5
  • 55
    • 0031416482 scopus 로고    scopus 로고
    • Actin-binding verprolin is a polarity development protein required for the morphogenesis and function of the yeast actin cytoskeleton
    • VADUVA, G., N. C. MARTIN and A. K. HOPPER, 1997 Actin-binding verprolin is a polarity development protein required for the morphogenesis and function of the yeast actin cytoskeleton. J. Cell Biol. 139: 1821-1833.
    • (1997) J. Cell Biol. , vol.139 , pp. 1821-1833
    • Vaduva, G.1    Martin, N.C.2    Hopper, A.K.3
  • 56
    • 0027250250 scopus 로고
    • Mammalian Ras interacts directly with the serine/threonine kinase Raf
    • VOJTEK, A. B., S. M. HOLLENBERG and J. A. COOPER, 1993 Mammalian Ras interacts directly with the serine/threonine kinase Raf. Cell 74: 205-214.
    • (1993) Cell , vol.74 , pp. 205-214
    • Vojtek, A.B.1    Hollenberg, S.M.2    Cooper, J.A.3
  • 58
    • 0026737363 scopus 로고
    • Systematic mutational analysis of the yeast ACT1 gene
    • WERTMAN, K. F., D. G. DRUBIN and D. BOTSTEIN, 1992 Systematic mutational analysis of the yeast ACT1 gene. Genetics 132: 337-350.
    • (1992) Genetics , vol.132 , pp. 337-350
    • Wertman, K.F.1    Drubin, D.G.2    Botstein, D.3
  • 59
    • 0032589216 scopus 로고    scopus 로고
    • Sla2p is associated with the yeast cortical actin cytoskeleton via redundant localization signals
    • YANG, S., M. J. COPE and D. G. DRUBIN, 1999 Sla2p is associated with the yeast cortical actin cytoskeleton via redundant localization signals. Mol. Biol. Cell 10: 2265-2283.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2265-2283
    • Yang, S.1    Cope, M.J.2    Drubin, D.G.3
  • 60
    • 0032832577 scopus 로고    scopus 로고
    • Temperature-sensitive mutations in the Saccharomyces cerevisiae MRT4, GRC5, SLA2 and THS1 genes result in defects in mRNA turnover
    • ZUK, D., J. P. BELK and A. JACOBSON, 1999 Temperature-sensitive mutations in the Saccharomyces cerevisiae MRT4, GRC5, SLA2 and THS1 genes result in defects in mRNA turnover. Genetics 153: 35-47.
    • (1999) Genetics , vol.153 , pp. 35-47
    • Zuk, D.1    Belk, J.P.2    Jacobson, A.3


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