메뉴 건너뛰기




Volumn 8, Issue 2, 1997, Pages 367-385

Evidence for physical and functional interactions among two Saccharomyces cerevisiae SH3 domain proteins, an adenylyl cyclase-associated protein and the actin cytoskeleton

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN FILAMENT; ARTICLE; CYTOSKELETON; FUNGAL GENETICS; GENE DISRUPTION; NONHUMAN; PLASMID; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; SACCHAROMYCES CEREVISIAE;

EID: 0031027546     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.8.2.367     Document Type: Article
Times cited : (148)

References (82)
  • 1
    • 0024584813 scopus 로고
    • A yeast actin-binding protein is encoded by SAC6, a gene found by suppression of an actin mutation
    • Adams, A.E., Botstein, D., and Drubin, D.G. (1989). A yeast actin-binding protein is encoded by SAC6, a gene found by suppression of an actin mutation. Science 243, 231-233.
    • (1989) Science , vol.243 , pp. 231-233
    • Adams, A.E.1    Botstein, D.2    Drubin, D.G.3
  • 3
    • 0028928199 scopus 로고
    • Defining protein interactions with yeast actin in vivo
    • Amberg, D., Basart, E., and Botstein, D. (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.1    Basart, E.2    Botstein, D.3
  • 4
    • 0028238878 scopus 로고
    • Actin-binding protein, drebrin, accumulates in submembranous regions in parallel with neuronal differentiation
    • Asada, H., Uyemura, K., and Shirao, T. (1994). Actin-binding protein, drebrin, accumulates in submembranous regions in parallel with neuronal differentiation. J. Neurosci. Res. 38, 149-159.
    • (1994) J. Neurosci. Res. , vol.38 , pp. 149-159
    • Asada, H.1    Uyemura, K.2    Shirao, T.3
  • 5
    • 0004270170 scopus 로고
    • Expression and purification of glutathione-S-transferase fusion proteins
    • ed. F. Ausubel, New York: Greene Publishing Associates and Wiley-Interscience
    • Ausubel, F. (1990). Expression and purification of glutathione-S-transferase fusion proteins. In: Current Protocols in Molecular Biology, ed. F. Ausubel, New York: Greene Publishing Associates and Wiley-Interscience.
    • (1990) Current Protocols in Molecular Biology
    • Ausubel, F.1
  • 6
    • 0029774184 scopus 로고    scopus 로고
    • Actin: General principles from studies in yeast
    • Ayscough, K.A., and Drubin, D.G. (1996). Actin: general principles from studies in yeast. Annu. Rev. Cell Dev. Biol. 12, 129-160.
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 129-160
    • Ayscough, K.A.1    Drubin, D.G.2
  • 7
    • 0027984898 scopus 로고
    • 1 cyclin expression by cyclic AMP in budding yeast
    • 1 cyclin expression by cyclic AMP in budding yeast. Nature 371, 339-342.
    • (1994) Nature , vol.371 , pp. 339-342
    • Baroni, M.1    Monti, P.2    Alberghina, L.3
  • 8
    • 0027237665 scopus 로고
    • A simple and efficient method for direct gene deletion in Saccharomyces cerevisiae
    • Baudin, A., Ozier, K.O., Denouel, A., Lacroute, F., and Cullin, C. (1993). A simple and efficient method for direct gene deletion in Saccharomyces cerevisiae. Nucleic Acids Res. 21, 3329-3330.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 3329-3330
    • Baudin, A.1    Ozier, K.O.2    Denouel, A.3    Lacroute, F.4    Cullin, C.5
  • 9
    • 0027219273 scopus 로고
    • Alteration of a yeast SH3 protein leads to conditional viability with defects in cytoskeletal and budding patterns
    • Bauer, F., Urdaci, M., Aigle, M., and Crouzet, M. (1993). Alteration of a yeast SH3 protein leads to conditional viability with 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
  • 10
    • 0028061489 scopus 로고
    • Cloning and mRNA expression of human unconventional myosin-IC. A homologue of amoeboid myosins-I with a single IQ motif and an SH3 domain
    • Bement, W.M., Wirth, J.A., and Mooseker, M.S. (1994). Cloning and mRNA expression of human unconventional myosin-IC. A homologue of amoeboid myosins-I with a single IQ motif and an SH3 domain. J. Mol. Biol. 243, 356-363.
    • (1994) J. Mol. Biol. , vol.243 , pp. 356-363
    • Bement, W.M.1    Wirth, J.A.2    Mooseker, M.S.3
  • 11
    • 15844384186 scopus 로고    scopus 로고
    • Associations among PH and SH3 domain-containing proteins and Rho-type GTPases in yeast
    • Bender, L., Lo, H., Lee, H., Kokojan, V., Peterson, J., and Bender, A. (1996). Associations among PH and SH3 domain-containing proteins and Rho-type GTPases in yeast. J. Cell Biol. 133, 879-894.
    • (1996) J. Cell Biol. , vol.133 , pp. 879-894
    • Bender, L.1    Lo, H.2    Lee, H.3    Kokojan, V.4    Peterson, J.5    Bender, A.6
  • 12
    • 0023484186 scopus 로고
    • 5-Fluoro-orotic acid as a selective agent in yeast molecular genetics
    • Boeke, J.D., Trueheart, J., Natsoulis, G., and Fink, G.R. (1987). 5-Fluoro-orotic acid as a selective agent in yeast molecular genetics. Methods Enzymol. 154, 164-175.
    • (1987) Methods Enzymol. , vol.154 , pp. 164-175
    • Boeke, J.D.1    Trueheart, J.2    Natsoulis, G.3    Fink, G.R.4
  • 13
    • 0026235967 scopus 로고
    • Ras-related signaling processes in Saccharomyces cerevisiae
    • Broach, J.R. (1991). Ras-related signaling processes in Saccharomyces cerevisiae. Curr. Opin. Gen. Dev. 1, 370-377.
    • (1991) Curr. Opin. Gen. Dev. , vol.1 , pp. 370-377
    • Broach, J.R.1
  • 14
    • 0025253769 scopus 로고
    • The function of Ras genes in Saccharomyces cerevisiae
    • Broach, J.R., and Deschenes, R.J. (1990). The function of Ras genes in Saccharomyces cerevisiae. Adv. Cancer Res. 54, 79-139.
    • (1990) Adv. Cancer Res. , vol.54 , pp. 79-139
    • Broach, J.R.1    Deschenes, R.J.2
  • 15
    • 0026586631 scopus 로고
    • A yeast gene (BEM1) necessary for cell polarization whose product contains two SH3 domains
    • Chenevert, J., Corrado, K., Bender, A., Pringle, J., and Herskowitz, I. (1992). A yeast gene (BEM1) necessary for cell polarization whose product contains two SH3 domains. Nature 356, 77-79.
    • (1992) Nature , vol.356 , pp. 77-79
    • Chenevert, J.1    Corrado, K.2    Bender, A.3    Pringle, J.4    Herskowitz, I.5
  • 16
    • 0026743906 scopus 로고
    • Identification of a protein that binds to the SH3 region of Ab1 and is similar to Bcr and GAP-rho
    • Cicchetti, P., Mayer, B.J., Thiel, G., and Baltimore, D. (1992). Identification of a protein that binds to the SH3 region of Ab1 and is similar to Bcr and GAP-rho. Science 257, 803-806.
    • (1992) Science , vol.257 , pp. 803-806
    • Cicchetti, P.1    Mayer, B.J.2    Thiel, G.3    Baltimore, D.4
  • 17
    • 0030060326 scopus 로고    scopus 로고
    • A role of amphiphysin in synaptic vesicle endocytosis is suggested by its binding to dynamin in nerve terminals
    • David, C., McPherson, P., Mundigl, O., and De Camilli, P. (1996). A role of amphiphysin in synaptic vesicle endocytosis is suggested by its binding to dynamin in nerve terminals. Proc. Natl. Acad. Sci. USA 93, 331-335.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 331-335
    • David, C.1    McPherson, P.2    Mundigl, O.3    De Camilli, P.4
  • 18
    • 0028169904 scopus 로고
    • Autoimmunity in Stiff-man syndrome with breast cancer is targeted to the C-terminal region of human amphiphysin, a protein similar to the yeast proteins, Rvs167 and Rvs161
    • David, C., Solimena, M., and De Camilli, P. (1994). Autoimmunity in Stiff-man syndrome with breast cancer is targeted to the C-terminal region of human amphiphysin, a protein similar to the yeast proteins, Rvs167 and Rvs161. FEBS Lett. 351, 73-79.
    • (1994) FEBS Lett. , vol.351 , pp. 73-79
    • David, C.1    Solimena, M.2    De Camilli, P.3
  • 19
  • 20
    • 0027417421 scopus 로고
    • Yeast mutants affected in viability upon starvation have a modified phospholipid composition
    • Desfarges, L., Durrens, P., Juguelin, H., Cassagne, C., Bonneu, M., and Aigle, M. (1993). Yeast mutants affected in viability upon starvation have a modified phospholipid composition. Yeast 9, 267-277.
    • (1993) Yeast , vol.9 , pp. 267-277
    • Desfarges, L.1    Durrens, P.2    Juguelin, H.3    Cassagne, C.4    Bonneu, M.5    Aigle, M.6
  • 21
    • 0024192883 scopus 로고
    • Yeast actin-binding proteins: Evidence for a role in morphogenesis
    • Drubin, D.G., Miller, K.G., and Botstein, D. (1988). Yeast actin-binding proteins: evidence for a role in morphogenesis. J. Cell Biol. 107, 2551-2561.
    • (1988) J. Cell Biol. , vol.107 , pp. 2551-2561
    • Drubin, D.G.1    Miller, K.G.2    Botstein, D.3
  • 22
    • 0025022491 scopus 로고
    • Homology of a yeast actin-binding protein to signal transduction proteins and myosin-I
    • Drubin, D.G., Mulholland, J., Zhimin, Z., and Botstein, D. (1990). Homology of a yeast actin-binding protein to signal transduction proteins and myosin-I. Nature 343, 288-290.
    • (1990) Nature , vol.343 , pp. 288-290
    • Drubin, D.G.1    Mulholland, J.2    Zhimin, Z.3    Botstein, D.4
  • 23
    • 0030045345 scopus 로고    scopus 로고
    • Origins of cell polarity
    • Drubin, D.G., and Nelson, W.J. (1996). Origins of cell polarity. Cell 84, 335-344.
    • (1996) Cell , vol.84 , pp. 335-344
    • Drubin, D.G.1    Nelson, W.J.2
  • 24
    • 0025361043 scopus 로고
    • SRV2, a gene required for RAS activation of adenylate cyclase in yeast
    • Fedor-Chaiken, M., Deschenes, R.J., and Broach, J.R. (1990). SRV2, a gene required for RAS activation of adenylate cyclase in yeast. Cell 61, 329-340.
    • (1990) Cell , vol.61 , pp. 329-340
    • Fedor-Chaiken, M.1    Deschenes, R.J.2    Broach, J.R.3
  • 25
    • 0025304792 scopus 로고
    • Cloning and characterization of CAP, the S. cerevisiae gene encoding the 70 kd adenylyl cyclase-associated protein
    • Field, J., et al. (1990). Cloning and characterization of CAP, the S. cerevisiae gene encoding the 70 kd adenylyl cyclase-associated protein. Cell 61, 319-327.
    • (1990) Cell , vol.61 , pp. 319-327
    • Field, J.1
  • 26
    • 0027359378 scopus 로고
    • Identification and sequence analysis of cDNAs encoding a 110-kilodalton actin filament-associated pp60src substrate
    • Flynn, D.C., Leu, T.H., Reynolds, A.B., and Parsons, J.T. (1993). Identification and sequence analysis of cDNAs encoding a 110-kilodalton actin filament-associated pp60src substrate. Mol. Cell. Biol. 13, 7892-7900.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7892-7900
    • Flynn, D.C.1    Leu, T.H.2    Reynolds, A.B.3    Parsons, J.T.4
  • 27
    • 0028920045 scopus 로고
    • An actin monomer binding activity localizes to the carboxyl-terminal half of the Saccharomyces cerevisiae cyclase-associated protein
    • Freeman, N.L., Chen, Z., Horenstein, J., Weber, A., and Field, J. (1995). An actin monomer binding activity localizes to the carboxyl-terminal half of the Saccharomyces cerevisiae cyclase-associated protein. J. Biol. Chem. 270, 5680-5685.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5680-5685
    • Freeman, N.L.1    Chen, Z.2    Horenstein, J.3    Weber, A.4    Field, J.5
  • 28
    • 0030048768 scopus 로고    scopus 로고
    • A conserved proline-rich region of the Saccharomyces cerevisiae cyclase-associated protein binds SH3 domains and modulates cytoskeletal localization
    • Freeman, N.L., Lila, T., Mintzer, K.A., Chen, Z., Pahk, A.J., Ren, R., Drubin, D.G., and Field, J. (1996). A conserved proline-rich region of the Saccharomyces cerevisiae cyclase-associated protein binds SH3 domains and modulates cytoskeletal localization. Mol. Cell. Biol. 16, 548-556.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 548-556
    • Freeman, N.L.1    Lila, T.2    Mintzer, K.A.3    Chen, Z.4    Pahk, A.J.5    Ren, R.6    Drubin, D.G.7    Field, J.8
  • 29
    • 0029082226 scopus 로고
    • DNM1, a dynamin-related gene, participates in endosomal trafficking in yeast
    • Gammie, A.E., Kurihara, L.J., Vallee, R.B., and Rose, M.D. (1995). DNM1, a dynamin-related gene, participates in endosomal trafficking in yeast. J. Cell Biol. 130, 553-566.
    • (1995) J. Cell Biol. , vol.130 , pp. 553-566
    • Gammie, A.E.1    Kurihara, L.J.2    Vallee, R.B.3    Rose, M.D.4
  • 30
    • 0026081344 scopus 로고
    • CAP is a bifunctional component of the Saccharomyces cerevisiae adenylyl cyclase complex
    • Gerst, J., Fergusen, K., Vojtek, A., Wigler, M., and Field, J. (1991). CAP is a bifunctional component of the Saccharomyces cerevisiae adenylyl cyclase complex. Mol. Cell. Biol. 11, 1248-1257.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1248-1257
    • Gerst, J.1    Fergusen, K.2    Vojtek, A.3    Wigler, M.4    Field, J.5
  • 31
    • 0026556288 scopus 로고
    • SNC1, a yeast homolog of the synaptic vesicle-associated membrane protein/synaptobrevin gene family: Genetic interactions with the RAS and CAP genes
    • Gerst, J.E., Rodgers, L., Riggs, M., and Wigler, M. (1992). SNC1, a yeast homolog of the synaptic vesicle-associated membrane protein/synaptobrevin gene family: genetic interactions with the RAS and CAP genes. Proc. Natl. Acad. Sci. USA 89, 4338-4342.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4338-4342
    • Gerst, J.E.1    Rodgers, L.2    Riggs, M.3    Wigler, M.4
  • 32
    • 0026543510 scopus 로고
    • ASP-56, a new actin sequestering protein from pig platelets with homology to CAP, an adenylate cyclase-associated protein from yeast
    • Gieselmann, R., and Mann, K. (1992). ASP-56, a new actin sequestering protein from pig platelets with homology to CAP, an adenylate cyclase-associated protein from yeast. FEBS Lett. 298, 149-153.
    • (1992) FEBS Lett. , vol.298 , pp. 149-153
    • Gieselmann, R.1    Mann, K.2
  • 33
    • 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
  • 34
    • 0030063258 scopus 로고    scopus 로고
    • Identification of a cyclase-associated protein (CAP) homologue in Dictyostelium discoideum and characterization of its interaction with actin
    • Gottwald, U., Brokamp, R., Karakesisoglou, I., Schleicher, M., and Noegel, A.A. (1996). Identification of a cyclase-associated protein (CAP) homologue in Dictyostelium discoideum and characterization of its interaction with actin. Mol. Biol. Cell 7, 261-272.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 261-272
    • Gottwald, U.1    Brokamp, R.2    Karakesisoglou, I.3    Schleicher, M.4    Noegel, A.A.5
  • 35
    • 0027402975 scopus 로고
    • Synaptic vesicle phosphoproteins and regulation of synaptic function
    • Greengard, P., Valtorta, F., Czernik, A.J., and Benfenati, F. (1993). Synaptic vesicle phosphoproteins and regulation of synaptic function. Science 259, 780-785.
    • (1993) Science , vol.259 , pp. 780-785
    • Greengard, P.1    Valtorta, F.2    Czernik, A.J.3    Benfenati, F.4
  • 36
    • 0030056968 scopus 로고    scopus 로고
    • Cell adhesion: The molecular basis of tissue architecture and morphogenesis
    • Gumbiner, B.M. (1996). Cell adhesion: the molecular basis of tissue architecture and morphogenesis. Cell 84, 345-357.
    • (1996) Cell , vol.84 , pp. 345-357
    • Gumbiner, B.M.1
  • 37
    • 0002547043 scopus 로고
    • Immunoaffinity purification
    • ed. H.J. Cuddihy. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Harlow, E., and Lane, D. (1988a). Immunoaffinity purification. In: Antibodies - A Laboratory Manual, ed. H.J. Cuddihy. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, 511-552.
    • (1988) Antibodies - A Laboratory Manual , pp. 511-552
    • Harlow, E.1    Lane, D.2
  • 38
    • 0001798502 scopus 로고
    • Immunoblotting
    • H.J. Cuddihy. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Harlow, E., and Lane, D. (1988b). Immunoblotting. In: Antibodies - A Laboratory Manual, H.J. Cuddihy. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, 471-504.
    • (1988) Antibodies - A Laboratory Manual , pp. 471-504
    • Harlow, E.1    Lane, D.2
  • 39
    • 0029955660 scopus 로고    scopus 로고
    • An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase
    • Hildebrand, J.D., Taylor, J.M., and Parsons, J.T. (1996). An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase. Mol. Cell. Biol. 16, 3169-3178.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3169-3178
    • Hildebrand, J.D.1    Taylor, J.M.2    Parsons, J.T.3
  • 40
    • 0027244817 scopus 로고
    • Synthetic-lethal interactions identify two novel genes, SLA1 and SLA2, that control membrane cytoskeleton assembly in Saccharomyces cerevisiae
    • Holtzman, D.A., Yang, S., and Drubin, D.G. (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
  • 42
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Fukuda, Y., Murata, K., and Kimura, A. (1983). Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153, 163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 43
    • 0027260748 scopus 로고
    • Actin and fimbrin are required for the internalization step of endocytosis in yeast
    • Kubler, E., and Riezman, H. (1993). Actin and fimbrin are required for the internalization step of endocytosis in yeast. EMBO J. 12, 2855-2862.
    • (1993) EMBO J. , vol.12 , pp. 2855-2862
    • Kubler, E.1    Riezman, H.2
  • 44
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: A physically integrated molecular process
    • Lauffenburger, D.A., and Horwitz, A. (1996). Cell migration: a physically integrated molecular process. Cell 84, 359-369.
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.2
  • 45
    • 0027414941 scopus 로고
    • Morphogenesis in the yeast cell cycle: Regulation by Cdc28 and cyclins
    • Lew, D.J., and Reed, S.I. (1993). Morphogenesis in the yeast cell cycle: regulation by Cdc28 and cyclins. J. Cell Biol. 120, 1305-1320.
    • (1993) J. Cell Biol. , vol.120 , pp. 1305-1320
    • Lew, D.J.1    Reed, S.I.2
  • 46
    • 0028915943 scopus 로고
    • A cell cycle checkpoint monitors cell morphogenesis in budding yeast
    • Lew, D.J., and Reed, S.I. (1995). A cell cycle checkpoint monitors cell morphogenesis in budding yeast. J. Cell Biol. 129, 739-749.
    • (1995) J. Cell Biol. , vol.129 , pp. 739-749
    • Lew, D.J.1    Reed, S.I.2
  • 47
    • 0029898291 scopus 로고    scopus 로고
    • Yeast src homology region 3 domain-binding proteins involved in bud formation
    • Matsui, Y., Matsui, R., Akada, R., and Toh-e, A. (1996). Yeast src homology region 3 domain-binding proteins involved in bud formation. J. Cell Biol. 133, 865-878.
    • (1996) J. Cell Biol. , vol.133 , pp. 865-878
    • Matsui, Y.1    Matsui, R.2    Akada, R.3    Toh-e, A.4
  • 48
    • 0029281993 scopus 로고
    • Minding your p's and q's
    • Mayer, B.J., and Eck, M.J. (1995). Minding your p's and q's. Curr. Biol. 5, 364-367.
    • (1995) Curr. Biol. , vol.5 , pp. 364-367
    • Mayer, B.J.1    Eck, M.J.2
  • 50
    • 0027222202 scopus 로고
    • Binding of the alpha-fodrin SH3 domain to the leading lamellae of locomoting chicken fibroblasts
    • Merilainen, J., Palovuori, R., Sormunen, R., Wasenius, V.M., and Lehto, V.P. (1993). Binding of the alpha-fodrin SH3 domain to the leading lamellae of locomoting chicken fibroblasts. J. Cell Sci. 105, 647-654.
    • (1993) J. Cell Sci. , vol.105 , pp. 647-654
    • Merilainen, J.1    Palovuori, R.2    Sormunen, R.3    Wasenius, V.M.4    Lehto, V.P.5
  • 51
    • 0028035235 scopus 로고
    • Interactions between adenylyl cyclase, CAP and RAS from Saccharomyces cerevisiae
    • Mintzer, K.A., and Field, J. (1994). Interactions between adenylyl cyclase, CAP and RAS from Saccharomyces cerevisiae. Cell Signal 6, 681-694.
    • (1994) Cell Signal , vol.6 , pp. 681-694
    • Mintzer, K.A.1    Field, J.2
  • 52
    • 0030049170 scopus 로고    scopus 로고
    • Actin-based cell motility and cell locomotion
    • Mitchison, T.J., and Cramer, L.P. (1996). Actin-based cell motility and cell locomotion. Cell 84, 371-379.
    • (1996) Cell , vol.84 , pp. 371-379
    • Mitchison, T.J.1    Cramer, L.P.2
  • 53
    • 0028839660 scopus 로고
    • The ADF/cofilin proteins: Stimulus-responsive modulators of actin dynamics
    • Moon, A., and Drubin, D.G. (1995). The ADF/cofilin proteins: stimulus-responsive modulators of actin dynamics. Mol. Biol. Cell 6, 1423-1431.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1423-1431
    • Moon, A.1    Drubin, D.G.2
  • 54
    • 0028856410 scopus 로고
    • End5, end6, and end7: Mutations that cause actin delocalization and block the internalization step of endocytosis in Saccharomyces cerevisiae
    • Munn, A.L., Stevenson, B.J., Geh, M.I., and Riezman, H. (1995).end5, end6, and end7: mutations that cause actin delocalization and block the internalization step of endocytosis in Saccharomyces cerevisiae. Mol. Biol. Cell 6, 1721-1742.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1721-1742
    • Munn, A.L.1    Stevenson, B.J.2    Geh, M.I.3    Riezman, H.4
  • 55
    • 0027245080 scopus 로고
    • Crystal structure of the SH3 domain in human Fyn; comparison of the three-dimensional structures of SH3 domains in tyrosine kinases and spectrin
    • Noble, M., Musacchio, A., Saraste, M., Courtneidge, S., and Wierenga, R. (1993). Crystal structure of the SH3 domain in human Fyn; comparison of the three-dimensional structures of SH3 domains in tyrosine kinases and spectrin. EMBO J. 12, 2617-2624.
    • (1993) EMBO J. , vol.12 , pp. 2617-2624
    • Noble, M.1    Musacchio, A.2    Saraste, M.3    Courtneidge, S.4    Wierenga, R.5
  • 56
    • 0029565191 scopus 로고
    • The Dictyostelium cytoskeleton
    • Noegel, A.A., and Luna, J.E. (1995). The Dictyostelium cytoskeleton. Experientia, 51, 1135-1143.
    • (1995) Experientia , vol.51 , pp. 1135-1143
    • Noegel, A.A.1    Luna, J.E.2
  • 57
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson, W.R., and Lipman, D.J. (1988). Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA 85, 2444-2448.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 58
    • 0022555884 scopus 로고
    • Actin and actin binding proteins. A critical evaluation of mechanisms and functions
    • Pollard, T.D., and Cooper, J.A. (1986). Actin and actin binding proteins. A critical evaluation of mechanisms and functions. Annu. Rev. Biochem. 55, 987-1035.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 987-1035
    • Pollard, T.D.1    Cooper, J.A.2
  • 61
    • 0027090325 scopus 로고
    • Actin- and tubulin-dependent functions during Saccharomyces cerevisiae mating projection formation
    • Read, E.B., Okamura, H.H., and Drubin, D.G. (1992). Actin- and tubulin-dependent functions during Saccharomyces cerevisiae mating projection formation. Mol. Biol. Cell 3, 429-444.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 429-444
    • Read, E.B.1    Okamura, H.H.2    Drubin, D.G.3
  • 62
    • 0023545322 scopus 로고
    • A Saccharomyces cerevisine genomic plasmid bank based on a centromere-containing shuttle vector
    • Rose, M.D., Novick, P., Thomas, J.H., Botstein, D., and Fink, G.R. (1987). A Saccharomyces cerevisine genomic plasmid bank based on a centromere-containing shuttle vector. Gene 60, 237-243.
    • (1987) Gene , vol.60 , pp. 237-243
    • Rose, M.D.1    Novick, P.2    Thomas, J.H.3    Botstein, D.4    Fink, G.R.5
  • 65
    • 0026512294 scopus 로고
    • Cloning of drebrin A and induction of neurite-like processes in drebrin-transfected cells
    • published erratum appears in Neuroreport 3, 1992, following 285
    • Shirao, T., Kojima, N., and Obata, K. (1992). Cloning of drebrin A and induction of neurite-like processes in drebrin-transfected cells (published erratum appears in Neuroreport 3, 1992, following 285). Neuroreport 3, 109-112.
    • (1992) Neuroreport , vol.3 , pp. 109-112
    • Shirao, T.1    Kojima, N.2    Obata, K.3
  • 66
    • 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 Hieter, P. (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
  • 67
    • 0028910268 scopus 로고
    • Actin cytoskeleton and budding pattern are altered in the yeast rvs161 mutant: The Rvs161 protein shares common domains with the brain protein amphiphysin
    • Sivadon, P., Bauer, F., Aigle, M., and Crouzet, M. (1995). Actin cytoskeleton and budding pattern are altered in the yeast rvs161 mutant: the Rvs161 protein shares common domains with the brain protein amphiphysin. Mol. Gen. Genet. 246, 485-495.
    • (1995) Mol. Gen. Genet. , vol.246 , pp. 485-495
    • Sivadon, P.1    Bauer, F.2    Aigle, M.3    Crouzet, M.4
  • 68
    • 0028930161 scopus 로고
    • A novel mammalian myosin I from rat with an SH3 domain localizes to Con A-inducible, F-actin-rich structures at cell-cell contacts
    • Stoffler, H.E., Ruppert, C., Reinhard, J., and Bahler, M. (1995). A novel mammalian myosin I from rat with an SH3 domain localizes to Con A-inducible, F-actin-rich structures at cell-cell contacts. J. Cell Biol. 129, 819-830.
    • (1995) J. Cell Biol. , vol.129 , pp. 819-830
    • Stoffler, H.E.1    Ruppert, C.2    Reinhard, J.3    Bahler, M.4
  • 69
    • 3543024026 scopus 로고
    • Nonmuscle actin binding proteins
    • Stossel, T.P., et al. (1985). Nonmuscle actin binding proteins. Annu. Rev. Cell Biol. 1, 353-402.
    • (1985) Annu. Rev. Cell Biol. , vol.1 , pp. 353-402
    • Stossel, T.P.1
  • 70
    • 0028938790 scopus 로고
    • The cytoskeleton and morphogenesis of the early Drosophila embryo
    • Sullivan, W., and Therkauf, W.E. (1995). The cytoskeleton and morphogenesis of the early Drosophila embryo. Curr. Opin. Cell Biol. 7, 18-22.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 18-22
    • Sullivan, W.1    Therkauf, W.E.2
  • 73
    • 0028289562 scopus 로고
    • Primary sequence of paxillin contains putative SH2 and SH3 domain binding motifs and multiple LIM domains: Identification of a vinculin and pp125Fak-binding region
    • Turner, C.E., and Miller, J.T. (1994). Primary sequence of paxillin contains putative SH2 and SH3 domain binding motifs and multiple LIM domains: identification of a vinculin and pp125Fak-binding region. J. Cell Sci. 107, 1583-1591.
    • (1994) J. Cell Sci. , vol.107 , pp. 1583-1591
    • Turner, C.E.1    Miller, J.T.2
  • 74
    • 0027329134 scopus 로고
    • Identification and characterization of a cDNA encoding mouse CAP: A homolog of the yeast adenylyl cyclase associated protein
    • Vojtek, A.B., and Cooper, J.A. (1993). Identification and characterization of a cDNA encoding mouse CAP: a homolog of the yeast adenylyl cyclase associated protein. J. Cell Sci. 105, 777-785.
    • (1993) J. Cell Sci. , vol.105 , pp. 777-785
    • Vojtek, A.B.1    Cooper, J.A.2
  • 75
    • 0026693870 scopus 로고
    • The 70-kilodalton adenylyl cyclase-associated protein is not essential for interaction of Saccharomyces cerevisiae adenylyl cyclase with RAS proteins
    • Wang, J., Suzuki, N., and Kataoka, T. (1992). The 70-kilodalton adenylyl cyclase-associated protein is not essential for interaction of Saccharomyces cerevisiae adenylyl cyclase with RAS proteins. Mol. Cell. Biol. 12, 4937-4945.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 4937-4945
    • Wang, J.1    Suzuki, N.2    Kataoka, T.3
  • 76
    • 0027190847 scopus 로고
    • Analysis of the function of the 70-kilodalton cyclase-associated protein (CAP) by using mutants of yeast adenylyl cyclase defective in CAP binding
    • Wang, J., Suzuki, N., Nishida, Y., and Kataoka, T. (1993). Analysis of the function of the 70-kilodalton cyclase-associated protein (CAP) by using mutants of yeast adenylyl cyclase defective in CAP binding. Mol. Cell. Biol. 13, 4087-4097.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4087-4097
    • Wang, J.1    Suzuki, N.2    Nishida, Y.3    Kataoka, T.4
  • 77
    • 0030039635 scopus 로고    scopus 로고
    • Human skeletal muscle nebulin sequence encodes a blueprint for thin filament architecture. Sequence motifs and affinity profiles of tandem repeats and terminal SH3
    • Wang, K., Knipfer, M., Huang, Q.Q., van Heerden, A., Hsu, L.C., Gutierrez, G., Quian, X.L., and Stedman, H. (1996). Human skeletal muscle nebulin sequence encodes a blueprint for thin filament architecture. Sequence motifs and affinity profiles of tandem repeats and terminal SH3. J. Biol. Chem. 271, 4304-4314.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4304-4314
    • Wang, K.1    Knipfer, M.2    Huang, Q.Q.3    Van Heerden, A.4    Hsu, L.C.5    Gutierrez, G.6    Quian, X.L.7    Stedman, H.8
  • 79
    • 0027419589 scopus 로고
    • Cortactin, an 80/85-kilodalton Pp 60src substrate, is a filamentous actin-binding protein enriched in the cell cortex
    • Wu, H., and Parsons, J.T. (1993). Cortactin, an 80/85-kilodalton Pp 60src substrate, is a filamentous actin-binding protein enriched in the cell cortex. J. Cell Biol. 120, 1417-1426.
    • (1993) J. Cell Biol. , vol.120 , pp. 1417-1426
    • Wu, H.1    Parsons, J.T.2
  • 80
    • 0026031717 scopus 로고
    • A dynamin-like protein encoded by the yeast sporulation gene SPO15
    • Yeh, E., Driscoll, R., Coltrera, M., Olins, A., and Bloom, K. (1991). A dynamin-like protein encoded by the yeast sporulation gene SPO15. Nature 349, 713-715.
    • (1991) Nature , vol.349 , pp. 713-715
    • Yeh, E.1    Driscoll, R.2    Coltrera, M.3    Olins, A.4    Bloom, K.5
  • 81
    • 0013484134 scopus 로고
    • Structural basis for the binding of proline-rich peptides to SH3 domains
    • Yu, H., Chen, J., Feng, S., Dalgarno, D., Brauer, A., and Schreiber, S. (1994). Structural basis for the binding of proline-rich peptides to SH3 domains. Cell 76, 933-945.
    • (1994) Cell , vol.76 , pp. 933-945
    • Yu, H.1    Chen, J.2    Feng, S.3    Dalgarno, D.4    Brauer, A.5    Schreiber, S.6
  • 82
    • 0029912384 scopus 로고    scopus 로고
    • Genetic analysis of the bipolar pattern of bud site selection in the yeast Saccharomyces cerevisiae
    • Zahner, J.E., Harkins, H., and Pringle, J.R. (1996). Genetic analysis of the bipolar pattern of bud site selection in the yeast Saccharomyces cerevisiae. Mol. Cell. Biol. 16, 1857-1870.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1857-1870
    • Zahner, J.E.1    Harkins, H.2    Pringle, J.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.