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Volumn 112, Issue 15, 1999, Pages 2529-2537

Rvs167p, the budding yeast homolog of amphiphysin, colocalizes with actin patches

Author keywords

Actin cytoskeleton; Amphiphysin; GFP; RVS167; Saccharomyces cerevisiae

Indexed keywords

ACTIN; FUNGAL PROTEIN;

EID: 0032771075     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (60)

References (47)
  • 1
    • 0021355377 scopus 로고
    • Relationship of actin and tubulin distribution to bud growth in wild-type and morphogenetic-mutant Saccharomyces cerevisiae
    • Adams, A. E. M. and Pringle, J. R. (1984). Relationship of actin and tubulin distribution to bud growth in wild-type and morphogenetic-mutant Saccharomyces cerevisiae. J. Cell Biol. 98, 934-945.
    • (1984) J. Cell Biol. , vol.98 , pp. 934-945
    • Adams, A.E.M.1    Pringle, J.R.2
  • 2
    • 0028928199 scopus 로고
    • Defining protein interactions with yeast actin in vivo
    • Amberg, D. C., Basart, E. and Botstein, D. (1995). Defining protein interactions with yeast actin in vivo. Nature Struct. Biol. 2, 28-35.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 28-35
    • Amberg, D.C.1    Basart, E.2    Botstein, D.3
  • 3
    • 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., Stryker, J., Pokala, N., Sanders, M., Crews, P. and Drubin, D. (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    Drubin, D.6
  • 4
    • 0031604152 scopus 로고    scopus 로고
    • Use of latrunculin-A, an actin monomer-binding drug
    • Ayscough, K. R. (1998). Use of latrunculin-A, an actin monomer-binding drug. Methods Enzymol. 298, 18-25.
    • (1998) Methods Enzymol. , vol.298 , pp. 18-25
    • Ayscough, K.R.1
  • 5
    • 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
  • 6
    • 0025785410 scopus 로고
    • A family of low and high copy replicative, integrative and single-stranded S. cerevisiae/E. coli shuttle vectors
    • Bonneaud, N., Ozier-Kalogeropoulos, O., Li, G. Y., Labouesse, M., Minvielle-Sebastia, L. and Lacroute, F. (1991). A family of low and high copy replicative, integrative and single-stranded S. cerevisiae/E. coli shuttle vectors. Yeast 7, 609-615.
    • (1991) Yeast , vol.7 , pp. 609-615
    • Bonneaud, N.1    Ozier-Kalogeropoulos, O.2    Li, G.Y.3    Labouesse, M.4    Minvielle-Sebastia, L.5    Lacroute, F.6
  • 8
    • 0031726759 scopus 로고    scopus 로고
    • Genetic and functional relationship between Rvsp, myosin and actin in Saccharomyces cerevisiae
    • Breton, A. M. and Aigle, M. (1998). Genetic and functional relationship between Rvsp, myosin and actin in Saccharomyces cerevisiae. Curr. Genet. 34, 280-286.
    • (1998) Curr. Genet. , vol.34 , pp. 280-286
    • Breton, A.M.1    Aigle, M.2
  • 9
    • 0032482228 scopus 로고    scopus 로고
    • Rvs161p interacts with Fus2p to promote cell fusion in Saccharomyces cerevisiae
    • Brizzio, V., Gammie, A. E. and Rose, M. (1998). Rvs161p interacts with Fus2p to promote cell fusion in Saccharomyces cerevisiae. J. Cell Biol. 141, 567-584.
    • (1998) J. Cell Biol. , vol.141 , pp. 567-584
    • Brizzio, V.1    Gammie, A.E.2    Rose, M.3
  • 10
    • 0030905586 scopus 로고    scopus 로고
    • Amphiphysin II (SH3P9;BIN1), a member of the amphiphysin/Rvs family, is concentrated in the cortical cytomatrix of axon initial segments and nodes of ranvier in brain and around T tubules skeletal muscle
    • Butler, M. H., David, C., Ochoa, G.-C., Freyberg, Z., Daniell, L., Grabs, D., Cremona, O. and De Camilli, P. (1997). Amphiphysin II (SH3P9;BIN1), a member of the amphiphysin/Rvs family, is concentrated in the cortical cytomatrix of axon initial segments and nodes of Ranvier in brain and around T tubules skeletal muscle. J. Cell Biol. 137, 1355-1367.
    • (1997) J. Cell Biol. , vol.137 , pp. 1355-1367
    • Butler, M.H.1    David, C.2    Ochoa, G.-C.3    Freyberg, Z.4    Daniell, L.5    Grabs, D.6    Cremona, O.7    De Camilli, P.8
  • 11
    • 0026599048 scopus 로고
    • One-step transformation of yeast in stationary phase
    • Chen, D. C., Yang, B. C. and Kuo, T. T. (1992). One-step transformation of yeast in stationary phase. Curr. Genet. 21, 83-84.
    • (1992) Curr. Genet. , vol.21 , pp. 83-84
    • Chen, D.C.1    Yang, B.C.2    Kuo, T.T.3
  • 12
    • 0031050445 scopus 로고    scopus 로고
    • Yeast-enhanced green fluorescent protein (yEGFP): A reporter of gene expression in Candida albicans
    • Cormack, B. P., Bertram, G., Egerton, M., Gow, N. A. R., Falkow, S. and Brown, A. J. P. (1997). Yeast-enhanced green fluorescent protein (yEGFP): a reporter of gene expression in Candida albicans. Microbiol. 143, 303-311.
    • (1997) Microbiol. , vol.143 , pp. 303-311
    • Cormack, B.P.1    Bertram, G.2    Egerton, M.3    Gow, N.A.R.4    Falkow, S.5    Brown, A.J.P.6
  • 13
    • 0025989149 scopus 로고
    • Yeast mutant affected for viability upon nutrient starvation: Characterization and cloning of the RVS161 gene
    • Crouzet, M., Urdaci, M., Dulau, L. and Aigle, M. (1991). Yeast mutant affected for viability upon nutrient starvation: characterization and cloning of the RVS161 gene. Yeast 7, 727-743.
    • (1991) Yeast , vol.7 , pp. 727-743
    • Crouzet, M.1    Urdaci, M.2    Dulau, L.3    Aigle, M.4
  • 14
    • 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, Rvs161 and Rvs167
    • 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, Rvs161 and Rvs167. FEBS Lett. 351, 73-79.
    • (1994) FEBS Lett. , vol.351 , pp. 73-79
    • David, C.1    Solimena, M.2    De Camilli, P.3
  • 15
    • 0029966290 scopus 로고    scopus 로고
    • Movement of yeast cortical actin cytoskeleton visualized in vivo
    • Doyle, T. and Botstein, D. (1996). Movement of yeast cortical actin cytoskeleton visualized in vivo. Proc. Natl. Acad. Sci. USA 93, 3886-3891.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3886-3891
    • Doyle, T.1    Botstein, D.2
  • 16
    • 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
  • 17
    • 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., Jones, H. D. and Wertman, K. F. (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
  • 18
    • 0028928903 scopus 로고
    • Evidence for a branched pathway in the polarized cell division of Saccharomyces cerevisiae
    • Durrens, P., Revardel, E., Bonneu, M. and Aigle, M. (1995). Evidence for a branched pathway in the polarized cell division of Saccharomyces cerevisiae. Curr. Genet. 27, 213-216.
    • (1995) Curr. Genet. , vol.27 , pp. 213-216
    • Durrens, P.1    Revardel, E.2    Bonneu, M.3    Aigle, M.4
  • 21
    • 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
  • 23
    • 0021369651 scopus 로고
    • Structural rearrangements of tubulin and actin during the cell cycle of the yeast Saccharomyces
    • Kilmartin, J. V. and Adams, A. E. M. (1984). Structural rearrangements of tubulin and actin during the cell cycle of the yeast Saccharomyces. J. Cell Biol. 98, 922-933.
    • (1984) J. Cell Biol. , vol.98 , pp. 922-933
    • Kilmartin, J.V.1    Adams, A.E.M.2
  • 24
    • 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., Colwill, K., Aneliunas, V., Tennyson, C., Moore, L., Ho, Y. and Andrews, B. (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    Ho, Y.6    Andrews, B.7
  • 25
    • 0031008152 scopus 로고    scopus 로고
    • A new member of the amphiphysin family connecting endocytosis and signal transduction pathways
    • Leprince, C., Romero, F., Cussac, D., Vayssiere, B., Berger, R., Tavitian, A. and Camonis, J. H. (1997). A new member of the amphiphysin family connecting endocytosis and signal transduction pathways. J. Biol. Chem. 272, 15101-15105.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15101-15105
    • Leprince, C.1    Romero, F.2    Cussac, D.3    Vayssiere, B.4    Berger, R.5    Tavitian, A.6    Camonis, J.H.7
  • 26
    • 0026639178 scopus 로고
    • Amphiphysin, a novel protein associated with synaptic vesicles
    • Lichte, B., Veh, R. W., Meyer, H. E. and Kilimann, M. W. (1992). Amphiphysin, a novel protein associated with synaptic vesicles. EMBO J. 11, 2521-2530.
    • (1992) EMBO J. , vol.11 , pp. 2521-2530
    • Lichte, B.1    Veh, R.W.2    Meyer, H.E.3    Kilimann, M.W.4
  • 27
    • 0031027546 scopus 로고    scopus 로고
    • Evidence for physical and functional interactions among two Saccharomyces cerevisiae SH3 domain proteins, adenylyl cyclase-associated protein and the actin cytoskeleton
    • Lila, T. and Drubin, D. (1997). Evidence for physical and functional interactions among two Saccharomyces cerevisiae SH3 domain proteins, 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
  • 29
    • 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., Geli, 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    Geli, M.I.3    Riezman, H.4
  • 30
    • 0031555306 scopus 로고    scopus 로고
    • Protein-protein interaction between the RVS161 and RVS167 gene products of Saccharomyces cerevisiae
    • Navarro, P., Durrens, P. and Aigle, M. (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
  • 32
    • 0020055185 scopus 로고
    • High-efficiency cloning of full-length cDNA
    • Okayama, H. and Berg, P. (1982). High-efficiency cloning of full-length cDNA. Mol. Cell. Biol. 2, 161-170.
    • (1982) Mol. Cell. Biol. , vol.2 , pp. 161-170
    • Okayama, H.1    Berg, P.2
  • 33
    • 0029847806 scopus 로고    scopus 로고
    • Crystal structure of the Aequorea victoria green fluorescent protein
    • Ormö, M., Cubitt, A. B., Kallio, K., Gross, L. A., Tsien, R. Y. and Remington, S. J. (1996). Crystal structure of the Aequorea victoria green fluorescent protein. Science 273, 1392-1395.
    • (1996) Science , vol.273 , pp. 1392-1395
    • Ormö, M.1    Cubitt, A.B.2    Kallio, K.3    Gross, L.A.4    Tsien, R.Y.5    Remington, S.J.6
  • 34
    • 0032530315 scopus 로고    scopus 로고
    • Crystal structure of the amphiphysin-2 SH3 domain and its role in the prevention of dynamin ring formation
    • Owen, D. J., Wigge, P., Vallis, Y., Moore, J. D. A., Evans, P. R. and McMahon, H. T. (1998). Crystal structure of the amphiphysin-2 SH3 domain and its role in the prevention of dynamin ring formation. EMBO J. 17, 5273-5285.
    • (1998) EMBO J. , vol.17 , pp. 5273-5285
    • Owen, D.J.1    Wigge, P.2    Vallis, Y.3    Moore, J.D.A.4    Evans, P.R.5    McMahon, H.T.6
  • 35
    • 0030908644 scopus 로고    scopus 로고
    • Identification and characterization of a nerve terminal-enriched amphiphysin isoform
    • Ramjaun, A. R., Micheva, K. D., Bouchelet, I. and McPherson, P. S. (1997). Identification and characterization of a nerve terminal-enriched amphiphysin isoform. J. Biol. Chem. 272, 16700-16706.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16700-16706
    • Ramjaun, A.R.1    Micheva, K.D.2    Bouchelet, I.3    McPherson, P.S.4
  • 36
    • 0029741917 scopus 로고    scopus 로고
    • BIN1 is a novel MYC-interacting protein with features of a tumour suppressor
    • Sakamuro, D., Elliott, K. J., Wechsler-Reya, R. and Prendergast, G. C. (1996). BIN1 is a novel MYC-interacting protein with features of a tumour suppressor. Nature Genet. 14, 69-76.
    • (1996) Nature Genet. , vol.14 , pp. 69-76
    • Sakamuro, D.1    Elliott, K.J.2    Wechsler-Reya, R.3    Prendergast, G.C.4
  • 37
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Sherman, F. (1991). Getting started with yeast. Methods Enzymol. 194, 3-21.
    • (1991) Methods Enzymol. , vol.194 , pp. 3-21
    • Sherman, F.1
  • 38
    • 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
  • 39
    • 0030697988 scopus 로고    scopus 로고
    • Functional assessment of the yeast Rvs161 and Rvs167 protein domains
    • Sivadon, P., Crouzet, M. and Aigle, M. (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
  • 40
    • 0029890281 scopus 로고    scopus 로고
    • Cloning of ligand targets: Systematic isolation of SH3 domain-containing proteins
    • Sparks, A. B., Hoffman, N. G., McConnell, S. J., Fowlkes, D. M. and Kay, B. K. (1996). Cloning of ligand targets: systematic isolation of SH3 domain-containing proteins. Nature Biotechnol. 14, 741-744.
    • (1996) Nature Biotechnol. , vol.14 , pp. 741-744
    • Sparks, A.B.1    Hoffman, N.G.2    McConnell, S.J.3    Fowlkes, D.M.4    Kay, B.K.5
  • 41
    • 0031561114 scopus 로고    scopus 로고
    • CDNA cloning of a novel amphiphysin isoform and tissue-specific expression of its multiple splice variants
    • Tsutsui, K., Maeda, Y., Tsutsui, K., Seki, S. and Tokunaga, A. (1997). cDNA cloning of a novel amphiphysin isoform and tissue-specific expression of its multiple splice variants. Biochem. Biophys. Res. Commun. 236, 178-183.
    • (1997) Biochem. Biophys. Res. Commun. , vol.236 , pp. 178-183
    • Tsutsui, K.1    Maeda, Y.2    Tsutsui, K.3    Seki, S.4    Tokunaga, A.5
  • 42
    • 0032478621 scopus 로고    scopus 로고
    • Perturbation of dynamin 11 with an amphiphysin SH3 domain increases GLUT4 glucose transporters at the plasma membrane in 3T3-L1 adipocytes
    • Volchuk, A., Narine, S., Foster, L. J., Grabs, D., De Camilli, P. and Klip, A. (1998). Perturbation of dynamin 11 with an amphiphysin SH3 domain increases GLUT4 glucose transporters at the plasma membrane in 3T3-L1 adipocytes. J. Biol. Chem. 273, 8169-8176.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8169-8176
    • Volchuk, A.1    Narine, S.2    Foster, L.J.3    Grabs, D.4    De Camilli, P.5    Klip, A.6
  • 45
    • 0032146236 scopus 로고    scopus 로고
    • The amphiphysin family of proteins and their role in endocytosis at the synapse
    • Wigge, P. and McMahon, H. T. (1998). The amphiphysin family of proteins and their role in endocytosis at the synapse. Trends Neurosci. 21, 339-344.
    • (1998) Trends Neurosci. , vol.21 , pp. 339-344
    • Wigge, P.1    McMahon, H.T.2
  • 46
    • 0031110140 scopus 로고    scopus 로고
    • Review: An overview of the Saccharomyces cerevisiae microtubule and microfilament cytoskeleton
    • Winsor, B. and Schiebel, E. (1997). Review: an overview of the Saccharomyces cerevisiae microtubule and microfilament cytoskeleton. Yeast 13, 399-434.
    • (1997) Yeast , vol.13 , pp. 399-434
    • Winsor, B.1    Schiebel, E.2
  • 47
    • 0029780351 scopus 로고    scopus 로고
    • The molecular structure of green fluorescent protein
    • Yang, F., Moss, L. G. and Phillips Jr., G. N. (1996). The molecular structure of green fluorescent protein. Nature Biotechnol. 14, 1246-1251.
    • (1996) Nature Biotechnol. , vol.14 , pp. 1246-1251
    • Yang, F.1    Moss, L.G.2    Phillips G.N., Jr.3


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