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Volumn 10, Issue 7, 1999, Pages 2265-2283

S1a2p is associated with the yeast cortical actin cytoskeleton via redundant localization signals

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; HUNTINGTIN; TALIN; CARRIER PROTEIN; DNA BINDING PROTEIN; FUNGAL PROTEIN; RECOMBINANT PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; SLA2 PROTEIN, S CEREVISIAE;

EID: 0032589216     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.10.7.2265     Document Type: Article
Times cited : (87)

References (41)
  • 1
    • 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. Struct. Biol. 2, 28-35.
    • (1995) Struct. Biol. , vol.2 , pp. 28-35
    • Amberg, D.1    Basart, E.2    Botstein, D.3
  • 2
    • 0004270170 scopus 로고
    • Expression and purification of glutathione-S-transferase fusion proteins
    • ed. F. Ausubel, New York: Greene Publishing Associates
    • 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, 16.7.
    • (1990) Current Protocols in Molecular Biology , pp. 167
    • Ausubel, F.1
  • 4
    • 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 latruculin-A
    • Ayscough, K.R., Stryker, J., Pokala, N., Sanders, M., Crews, P., and Drubin, D.G. (1997). High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latruculin-A. J. Cell Biol. 137, 399-416.
    • (1997) J. Cell Biol. , vol.137 , pp. 399-416
    • Ayscough, K.R.1    Stryker, J.2    Pokala, N.3    Sanders, M.4    Crews, P.5    Drubin, D.G.6
  • 5
    • 0032935690 scopus 로고    scopus 로고
    • GCS1, an Arf guanosine triphosphatase-activating protein in Saccharomyces cerevisiae, is required for normal actin cytoskeletal organization in vivo and stimulates actin polymerization in vitro
    • Blader, I.J., Cope, M.J.T.V., Jackson, T.R., Profit, A.A., Greenwood, A.F., Drubin, D.G., Prestwich, G.D., and Theibert, A.B. (1999). GCS1, an Arf guanosine triphosphatase-activating protein in Saccharomyces cerevisiae, is required for normal actin cytoskeletal organization in vivo and stimulates actin polymerization in vitro. Mol. Biol. Cell 10, 581-596.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 581-596
    • Blader, I.J.1    Cope, M.J.T.V.2    Jackson, T.R.3    Profit, A.A.4    Greenwood, A.F.5    Drubin, D.G.6    Prestwich, G.D.7    Theibert, A.B.8
  • 6
    • 0024325465 scopus 로고
    • Molecular analysis of the SNF4 gene of Saccharomyces cerevisiae: Evidence for physical association of the SNF4 protein with the SNF1 protein kinase
    • Celenza, J.L., Eng, F.J., and Carlson, M. (1989). Molecular analysis of the SNF4 gene of Saccharomyces cerevisiae: evidence for physical association of the SNF4 protein with the SNF1 protein kinase. Mol. Cell. Biol. 9, 5045-5054.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 5045-5054
    • Celenza, J.L.1    Eng, F.J.2    Carlson, M.3
  • 7
    • 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
  • 8
    • 0025022491 scopus 로고
    • Homology of a yeast actin-binding protein to signal transduction proteins and myosin-I
    • Drubin, D.G., Mulholland, J., Zhu, Z.M., 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    Zhu, Z.M.3    Botstein, D.4
  • 11
    • 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
  • 12
    • 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
  • 13
    • 0029121577 scopus 로고
    • Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site
    • Gary, R., and Bretscher, A. (1995). Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site. Mol. Biol. Cell 6, 1061-1075.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1061-1075
    • Gary, R.1    Bretscher, A.2
  • 14
    • 0029943112 scopus 로고    scopus 로고
    • Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4-5-bisphosphate
    • Gilmore, A.P., and Burridge, K. (1996). Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4-5-bisphosphate. Nature 381, 531-535.
    • (1996) Nature , vol.381 , pp. 531-535
    • Gilmore, A.P.1    Burridge, K.2
  • 15
    • 0001828191 scopus 로고
    • Immunizations
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Harlow, E., and Lane, D. (1988). Immunizations. In: Antibodies-A Laboratory Manual, Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, 53-138.
    • (1988) Antibodies-A Laboratory Manual , pp. 53-138
    • Harlow, E.1    Lane, D.2
  • 17
    • 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
  • 18
    • 0028318397 scopus 로고
    • An intramolecular association between the head and tail domains of vinculin modulates talin binding
    • Johnson, R.P., and Craig, S.W. (1994). An intramolecular association between the head and tail domains of vinculin modulates talin binding. J. Biol. Chem. 269, 12611-12619.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12611-12619
    • Johnson, R.P.1    Craig, S.W.2
  • 19
    • 0028836195 scopus 로고
    • F-actin binding site masked by the intramolecular association of vinculin head and tail domains
    • Johnson, R.P., and Craig, S.W. (1995). F-actin binding site masked by the intramolecular association of vinculin head and tail domains. Nature 373, 261-264.
    • (1995) Nature , vol.373 , pp. 261-264
    • Johnson, R.P.1    Craig, S.W.2
  • 20
    • 0030986659 scopus 로고    scopus 로고
    • HIP1, a human homologue of S. cerevisiae Sla2p, interacts with membrane associated huntingtin in the brain
    • Kalchman, M.A., et al. (1997). HIP1, a human homologue of S. cerevisiae Sla2p, interacts with membrane associated huntingtin in the brain. Nat. Genet. 16, 44-53.
    • (1997) Nat. Genet. , vol.16 , pp. 44-53
    • Kalchman, M.A.1
  • 21
    • 0031878090 scopus 로고    scopus 로고
    • The ADF homology (ADF-H) domain: A highly exploited actin-binding module
    • Lappalainen, P., Kessels, M.K., Cope, M.J.T.V., and Drubin, D.G. (1998). The ADF homology (ADF-H) domain: a highly exploited actin-binding module. Mol. Biol. Cell 9, 1951-1959.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1951-1959
    • Lappalainen, P.1    Kessels, M.K.2    Cope, M.J.T.V.3    Drubin, D.G.4
  • 22
    • 0021919105 scopus 로고
    • Specific interaction between phosphatidylinositol 4,5-bisphosphate and profilactin
    • Lassing, I., and Lindberg, U. (1985). Specific interaction between phosphatidylinositol 4,5-bisphosphate and profilactin. Nature 314, 472-474.
    • (1985) Nature , vol.314 , pp. 472-474
    • Lassing, I.1    Lindberg, U.2
  • 23
    • 0028871169 scopus 로고
    • Regulation of cortical actin cytoskeleton assembly during polarized cell growth in budding yeast
    • Li, R., Zheng, Y., and Drubin, D.G. (1995). Regulation of cortical actin cytoskeleton assembly during polarized cell growth in budding yeast. J. Cell Biol. 128, 599-615.
    • (1995) J. Cell Biol. , vol.128 , pp. 599-615
    • Li, R.1    Zheng, Y.2    Drubin, D.G.3
  • 24
    • 0031027546 scopus 로고    scopus 로고
    • Evidence for physical and functional interactions among two Saccharomyces cerevisiae SH3 domain proteins, an adenylyl cyclase-associated protein an the actin cytoskeleton
    • Lila, T., and Drubin, D.G. (1997). Evidence for physical and functional interactions among two Saccharomyces cerevisiae SH3 domain proteins, an adenylyl cyclase-associated protein an the actin cytoskeleton. Mol. Biol. Cell 8, 367-385.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 367-385
    • Lila, T.1    Drubin, D.G.2
  • 25
    • 0029042961 scopus 로고
    • Gene disruption with PCR products in Saccharomyces cerevisiae
    • Lorenz, M.C., Muir, R.S., Lim, E., McElver, J., Weber, S.C., and Heitman, J. (1995). Gene disruption with PCR products in Saccharomyces cerevisiae. Gene 158, 113-117.
    • (1995) Gene , vol.158 , pp. 113-117
    • Lorenz, M.C.1    Muir, R.S.2    Lim, E.3    McElver, J.4    Weber, S.C.5    Heitman, J.6
  • 26
    • 0026356891 scopus 로고
    • Predicting coiled-coils from protein sequences
    • Lupas, A., Van Dyke, M., and Stock, J. (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
  • 27
    • 0023615620 scopus 로고
    • Plasmid construction by homologous recombination in yeast
    • Ma, H., Kunes, S., Schatz, P.J., and Botstein, D. (1987). Plasmid construction by homologous recombination in yeast. Gene 58, 201-216.
    • (1987) Gene , vol.58 , pp. 201-216
    • Ma, H.1    Kunes, S.2    Schatz, P.J.3    Botstein, D.4
  • 29
    • 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
    • McCann, R.O., and Craig, S.W. (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. USA , vol.94 , pp. 5679-5684
    • McCann, R.O.1    Craig, S.W.2
  • 30
    • 0027446345 scopus 로고
    • Cofilin is an essential component of the yeast cortical cytoskeleton
    • Moon, A.L., Janmey, P.A., Louie, K.A., and Drubin, D.G. (1993). Cofilin is an essential component of the yeast cortical cytoskeleton. J. Cell Biol. 120, 421-435.
    • (1993) J. Cell Biol. , vol.120 , pp. 421-435
    • Moon, A.L.1    Janmey, P.A.2    Louie, K.A.3    Drubin, D.G.4
  • 31
    • 0028204439 scopus 로고
    • Ultrastructure of the yeast actin cytoskeleton and its association with the plasma membrane
    • Mulholland, J., Preuss, D., Moon, A., Wong, A., Drubin, D., and Botstein, D. (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    Botstein, D.6
  • 32
    • 0030930123 scopus 로고    scopus 로고
    • Yeast actin cytoskeleton mutants accumulate a new class of Golgi-derived secretory vesicle
    • Mulholland, J., Wesp, A., Riezman, H., and Botstein, D. (1997). Yeast actin cytoskeleton mutants accumulate a new class of Golgi-derived secretory 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
  • 33
    • 0028934931 scopus 로고
    • MOP2 (SLA2) affects the abundance of the plasma membrane H(+)-AT-Pase of Saccharomyces cerevisiae
    • Na, S., Hincapie, M., McCusker, J.H., and Haber, J.E. (1995). MOP2 (SLA2) affects the abundance of the plasma membrane H(+)-AT-Pase 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
  • 35
    • 0027455339 scopus 로고
    • end3 and end4: Two mutants defective in receptor-mediated and fluid-phase endocytosis in Saccharomyces cerevisiae
    • Raths, S., Rohrer, J., Crausaz, F., and Riezman, H. (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
  • 37
    • 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
  • 38
    • 0030872948 scopus 로고    scopus 로고
    • PSTPIP: A tyrosine phosphorylated cleavage furrow-associated protein that is a substrate for a PEST tyrosine phosphatase
    • Spencer, S., Dowbenko, D., Cheng, J., Li, W., Brush, J., Utzig, S., Simanis, V., and Lasky, L.A. (1997). PSTPIP: a tyrosine phosphorylated cleavage furrow-associated protein that is a substrate for a PEST tyrosine phosphatase. J. Cell Biol. 138, 845-860.
    • (1997) J. Cell Biol. , vol.138 , pp. 845-860
    • Spencer, S.1    Dowbenko, D.2    Cheng, J.3    Li, W.4    Brush, J.5    Utzig, S.6    Simanis, V.7    Lasky, L.A.8
  • 40
    • 0030785341 scopus 로고    scopus 로고
    • End4p-Sla2p interacts with actin-associated proteins for endocytosis in Saccharomyces cerevisiae
    • Wesp, A., Hicke, L., Palecek, J., Lombardi, R., Aust, T., Munn, A.L., and Riezman, H. (1997). End4p-Sla2p interacts with actin-associated proteins for endocytosis in Saccharomyces cerevisiae. Mol. Biol. Cell 8, 2291-2306.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2291-2306
    • Wesp, A.1    Hicke, L.2    Palecek, J.3    Lombardi, R.4    Aust, T.5    Munn, A.L.6    Riezman, H.7
  • 41
    • 0031012576 scopus 로고    scopus 로고
    • A role for the actin cytoskeleton of Saccharomyces cerevisiae in bipolar bud-site selection
    • Yang, S., Ayscough, K.R., and Drubin, D.G. (1997). A role for the actin cytoskeleton of Saccharomyces cerevisiae in bipolar bud-site selection. J. Cell Biol. 136, 111-123.
    • (1997) J. Cell Biol. , vol.136 , pp. 111-123
    • Yang, S.1    Ayscough, K.R.2    Drubin, D.G.3


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