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Volumn 14, Issue 7, 2003, Pages 3027-3040

Regulation of the yeast amphiphysin homologue Rvs167p by phosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

AMPHIPHYSIN; CYCLIN DEPENDENT KINASE; CYCLINE; FUNGAL PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PHEROMONE; PHOSPHOPROTEIN; PROTEIN FUS3P; PROTEIN PCL2P; PROTEIN PHO85P; PROTEIN RVS167P; PROTEIN YMR192P; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 0038783734     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E02-09-0613     Document Type: Article
Times cited : (30)

References (64)
  • 1
    • 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. 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
    • 0035863727 scopus 로고    scopus 로고
    • Specificity assay of serine proteinases by reverse-phase high-performance liquid chromatography analysis of competing oligopeptide substrate library
    • Antal, J. Pal, G., Asboth, B., Buzas, Z., Patthy, A., and Graf, L. (2001). Specificity assay of serine proteinases by reverse-phase high-performance liquid chromatography analysis of competing oligopeptide substrate library. Anal. Biochem. 288, 156-167.
    • (2001) Anal. Biochem. , vol.288 , pp. 156-167
    • Antal, J.1    Pal, G.2    Asboth, B.3    Buzas, Z.4    Patthy, A.5    Graf, L.6
  • 4
    • 0032771075 scopus 로고    scopus 로고
    • Rvs167p, the budding yeast homolog of amphiphysin, colocalizes with actin patches
    • Balguerie, A., Sivadon, P., Bonneu, M., and Aigel, M. (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    Aigel, M.4
  • 5
    • 0035971144 scopus 로고    scopus 로고
    • A conserved docking site in MEKs mediates high-affinity binding to MAP kinases and cooperates with a scaffold protein to enhance signal transmission
    • Bardwell, A.J., Flatauer, L.J., Matsukuma, K., Thorner, J., and Bardwell, L. (2001). A conserved docking site in MEKs mediates high-affinity binding to MAP kinases and cooperates with a scaffold protein to enhance signal transmission. J. Biol. Chem. 276, 10374-10386.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10374-10386
    • Bardwell, A.J.1    Flatauer, L.J.2    Matsukuma, K.3    Thorner, J.4    Bardwell, L.5
  • 6
    • 0029992810 scopus 로고    scopus 로고
    • Signaling in the yeast pheromone response pathway: Specific and high-affinity interaction of the mitogen-activated protein (MAP) kinases Kssl and Fus3 with the upstream MAP kinase kinase Ste7
    • Bardwell, L., Cook, J.G., Chang, E.C., Cairns, B.R., and Thorner, J. (1996). Signaling in the yeast pheromone response pathway: specific and high-affinity interaction of the mitogen-activated protein (MAP) kinases Kssl and Fus3 with the upstream MAP kinase kinase Ste7. Mol. Cell. Biol. 16, 3637-3650.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3637-3650
    • Bardwell, L.1    Cook, J.G.2    Chang, E.C.3    Cairns, B.R.4    Thorner, J.5
  • 7
    • 0030272039 scopus 로고    scopus 로고
    • A conserved motif at the amino termini of MEKs might mediate high-affinity interaction with the cognate MAPKs
    • Bardwell, L., and Thorner, J. (1996). A conserved motif at the amino termini of MEKs might mediate high-affinity interaction with the cognate MAPKs. Trends Biochem. Sci. 21, 373-374.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 373-374
    • Bardwell, L.1    Thorner, J.2
  • 8
    • 0027219273 scopus 로고
    • Alteration of a yeast SH3 protein leads to conditional viability and 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 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
    • 0021668558 scopus 로고
    • A positive selection for mutants lacking orotidine-5′-phosphate decarboxylase activity in yeast: 5-fluoro-orotic acid resistance
    • Boeke, J.D., Lacroute, F., and Fink, G.R. (1984). A positive selection for mutants lacking orotidine-5′-phosphate decarboxylase activity in yeast: 5-fluoro-orotic acid resistance. Mol. Gen. Genet. 197, 345-346.
    • (1984) Mol. Gen. Genet. , vol.197 , pp. 345-346
    • Boeke, J.D.1    Lacroute, F.2    Fink, G.R.3
  • 10
    • 0034734849 scopus 로고    scopus 로고
    • A network of proteins around Rvs167p and Rvs161p, two proteins related to the yeast actin cytoskeleton
    • Bon, E., Recordon-Navarro, P., Durrens, P., Iwase, M., Toh-e, A., and Aigle, M. (2000). A network of proteins around Rvs167p and Rvs161p, two proteins related to the yeast actin cytoskeleton. Yeast 16, 1229-1241.
    • (2000) Yeast , vol.16 , pp. 1229-1241
    • Bon, E.1    Recordon-Navarro, P.2    Durrens, P.3    Iwase, M.4    Toh-E, A.5    Aigle, M.6
  • 11
    • 0025998840 scopus 로고
    • Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates
    • Boyle, W., van der Geer, P., and Hunter, T. (1991). Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates. Methods Enzymol. 201, 110-152.
    • (1991) Methods Enzymol. , vol.201 , pp. 110-152
    • Boyle, W.1    Van der Geer, P.2    Hunter, T.3
  • 12
    • 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., Davies, A., Cost, G.J., Caputo, E., Li, J., Hieter, P., and Boeke, J.D. (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    Hieter, P.6    Boeke, J.D.7
  • 13
    • 0036607966 scopus 로고    scopus 로고
    • MAPK signaling specificity: It takes two to tango
    • Breitkreutz, A., and Tyers, M. (2002). MAPK signaling specificity: it takes two to tango. Trends Cell Biol. 12, 254-257.
    • (2002) Trends Cell Biol. , vol.12 , pp. 254-257
    • Breitkreutz, A.1    Tyers, M.2
  • 14
    • 0035928744 scopus 로고    scopus 로고
    • MAPK specificity in the yeast pheromone response independent of transcriptional activation
    • Breitkreutz, A., Boucher, L., and Tyers, M. (2001). MAPK specificity in the yeast pheromone response independent of transcriptional activation. Curr. Biol. 11, 1266-1271.
    • (2001) Curr. Biol. , vol.11 , pp. 1266-1271
    • Breitkreutz, A.1    Boucher, L.2    Tyers, M.3
  • 15
    • 0031726759 scopus 로고    scopus 로고
    • Genetic and functional relationship between Rvsp, myosin and actin in Saccharomyces cerevisiae
    • Breton, A., 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.1    Aigle, M.2
  • 16
    • 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., Schaeffer, J., and Aigle, M. (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
  • 17
    • 0032482228 scopus 로고    scopus 로고
    • Rvs161p interacts with Fus2p to promote cell fusion in Saccharomyces cerevisiae
    • Brizzio, V., Gammie, A.E., and Rose, M.D. (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.D.3
  • 18
    • 0036469785 scopus 로고    scopus 로고
    • Pho85 and signaling environmental conditions
    • Carroll, A.S., and O'Shea, E.K. (2002). Pho85 and signaling environmental conditions. Trends Biochem. Sci. 27, 87-93.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 87-93
    • Carroll, A.S.1    O'Shea, E.K.2
  • 19
    • 0032935411 scopus 로고    scopus 로고
    • A modulatory role for clathrin light chain phosphorylation in Golgi membrane protein localization during vegetative growth and during the mating response of Saccharomyces cerevisiae
    • Chu, D.S., Pishvaee, B., and Payne, G.S. (1999). A modulatory role for clathrin light chain phosphorylation in Golgi membrane protein localization during vegetative growth and during the mating response of Saccharomyces cerevisiae. Mol. Biol. Cell 10, 713-726.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 713-726
    • Chu, D.S.1    Pishvaee, B.2    Payne, G.S.3
  • 20
    • 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., Field, D., Moore, L., Friesen, J., and Andrews, B. (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
  • 21
    • 0035817637 scopus 로고    scopus 로고
    • A protein interaction map for cell polarity development
    • Drees, B.L. et al. (2001). A protein interaction map for cell polarity development. J. Cell Biol. 154, 549-571.
    • (2001) J. Cell Biol. , vol.154 , pp. 549-571
    • Drees, B.L.1
  • 22
    • 0034932864 scopus 로고    scopus 로고
    • Yeast Eps15-like endocytic protein, Pan1p, activates the Arp2/3 complex
    • Duncan, M.C., Cope, M.J., Goode, B.L., Wendland, B., and Drubin, D.G. (2001). Yeast Eps15-like endocytic protein, Pan1p, activates the Arp2/3 complex. Nat. Cell Biol. 3, 687-690.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 687-690
    • Duncan, M.C.1    Cope, M.J.2    Goode, B.L.3    Wendland, B.4    Drubin, D.G.5
  • 23
    • 0034854464 scopus 로고    scopus 로고
    • Mass spectrometry for the study of protein-protein interactions
    • Figeys, D., McBroom, L.D., and Moran, M.F. (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
  • 24
    • 0035896503 scopus 로고    scopus 로고
    • Amphiphysin 1 binds the cyclin-dependent kinase (cdk) 5 regulatory subunit p35 and is phosphorylated by cdk5 and cdc2
    • Floyd, S.R., Porro, E.B., Slepnev, V.I., Ochoa, G.C., Tsai, L.H., and De Camilli, P. (2001). Amphiphysin 1 binds the cyclin-dependent kinase (cdk) 5 regulatory subunit p35 and is phosphorylated by cdk5 and cdc2. J. Biol. Chem. 276, 8104-8110.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8104-8110
    • Floyd, S.R.1    Porro, E.B.2    Slepnev, V.I.3    Ochoa, G.C.4    Tsai, L.H.5    De Camilli, P.6
  • 25
    • 0032873415 scopus 로고    scopus 로고
    • Three new dominant drug resistance cassettes for gene disruption in Saccharomyces cerevisiae
    • Goldstein, A.L., and McCusker, J.H. (1999). Three new dominant drug resistance cassettes for gene disruption in Saccharomyces cerevisiae. Yeast 15, 1541-1553.
    • (1999) Yeast , vol.15 , pp. 1541-1553
    • Goldstein, A.L.1    McCusker, J.H.2
  • 26
    • 0031026823 scopus 로고    scopus 로고
    • The nuclear receptor homologue Ftz-F1 and the homeodomain protein Ftz are mutually dependent cofactors
    • Guichet, A. 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
  • 28
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S.N., Hunt, H.D., Horton, R.M., Pullen, J.K., and Pease, L.R. (1989). Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 29
    • 0029954396 scopus 로고    scopus 로고
    • Pho85p, a cyclin-dependent protein kinase, and the Snf1p protein kinase act antagonistically to control glycogen accumulation in Saccharomyces cerevisiae
    • Huang, D., Farkas, I., and Roach, P.J. (1996). Pho85p, a cyclin-dependent protein kinase, and the Snf1p protein kinase act antagonistically to control glycogen accumulation in Saccharomyces cerevisiae. Mol. Cell. Biol. 16, 4357-4365.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4357-4365
    • Huang, D.1    Farkas, I.2    Roach, P.J.3
  • 30
    • 0036295684 scopus 로고    scopus 로고
    • Dissection of a complex phenotype by functional genomics reveals roles for the yeast cyclin-dependent protein kinase Pho85 in stress adaptation and cell integrity
    • Huang, D., Moffat, J., and Andrews, B. (2002). Dissection of a complex phenotype by functional genomics reveals roles for the yeast cyclin-dependent protein kinase Pho85 in stress adaptation and cell integrity. Mol. Cell. Biol. 22, 5076-5088.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5076-5088
    • Huang, D.1    Moffat, J.2    Andrews, B.3
  • 31
    • 0033428894 scopus 로고    scopus 로고
    • Mammalian Cdk5 is a functional homologue of the budding yeast Pho85 cyclin-dependent protein kinase
    • Huang, D., Patrick, G., Moffat, J., Tsai, L.-H., and Andrews, B. (1999a). Mammalian Cdk5 is a functional homologue of the budding yeast Pho85 cyclin-dependent protein kinase. Proc. Natl. Acad. Sci. USA 96, 14445-14450.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14445-14450
    • Huang, D.1    Patrick, G.2    Moffat, J.3    Tsai, L.-H.4    Andrews, B.5
  • 32
    • 0033617289 scopus 로고    scopus 로고
    • Replacement of threonine 558, a critical site of phosphorylation of moesin in vivo, with aspartate activates F-actin binding of moesin. Regulation by conformational change
    • Huang, L., Wong, T.Y., Lin, R.C., and Furthmayr, H. (1999b). Replacement of threonine 558, a critical site of phosphorylation of moesin in vivo, with aspartate activates F-actin binding of moesin. Regulation by conformational change. J. Biol. Chem. 274, 12803-12810.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12803-12810
    • Huang, L.1    Wong, T.Y.2    Lin, R.C.3    Furthmayr, H.4
  • 33
    • 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
  • 34
    • 0035148414 scopus 로고    scopus 로고
    • Genetic evidence for a morphogenetic function of the Saccharomyces cerevisiae Pho85 cyclin-dependent kinase
    • Lenburg, M.E., and O'Shea, E.K. (2001). Genetic evidence for a morphogenetic function of the Saccharomyces cerevisiae Pho85 cyclin-dependent kinase. Genetics 157, 39-51.
    • (2001) Genetics , vol.157 , pp. 39-51
    • Lenburg, M.E.1    O'Shea, E.K.2
  • 35
    • 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 Drubin, D. (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
  • 36
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine, M.S., McKenzie, A., DeMarini, D.J., Shah, N.G., Wach, A., Brachat, A., Philippsen, P., and Pringle, J.R. (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    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 37
    • 0032835492 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae homologue of human Wiskott-Aldrich syndrome protein Las17p interacts with the Arp2/3 complex
    • Madania, A., Dumoulin, P., Grava, S., Kitamoto, H., Scharer-Brodbeck, C., Soulard, A., Moreau, V., and Winsor, B. (1999). The Saccharomyces cerevisiae homologue of human Wiskott-Aldrich syndrome protein Las17p interacts with the Arp2/3 complex. Mol. Biol. Cell 10, 3521-3538.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3521-3538
    • Madania, A.1    Dumoulin, P.2    Grava, S.3    Kitamoto, H.4    Scharer-Brodbeck, C.5    Soulard, A.6    Moreau, V.7    Winsor, B.8
  • 38
    • 0028589197 scopus 로고
    • The Pcl2 (ORFD)-Pho85 cyclin-dependent kinase complex: A cell cycle regulator in yeast
    • Measday, V., Moore, L., Ogas, J., Tyers, M., and Andrews, B. (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
  • 40
    • 0034017609 scopus 로고    scopus 로고
    • Degradation of the transcription factor Gcn4 requires the kinase Pho85 and the SCF-CDC4 ubiquitin-ligase complex
    • Meimoun, A., Holtzman, T., Weissman, Z., McBride, H.J., Stillman, D.J., Fink, G.R., and Kornitzer, D. (2000). Degradation of the transcription factor Gcn4 requires the kinase Pho85 and the SCF-CDC4 ubiquitin-ligase complex. Mol. Biol. Cell 11, 915-927.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 915-927
    • Meimoun, A.1    Holtzman, T.2    Weissman, Z.3    McBride, H.J.4    Stillman, D.J.5    Fink, G.R.6    Kornitzer, D.7
  • 41
    • 0033628520 scopus 로고    scopus 로고
    • Functions of Pho85 cyclin-dependent kinases in budding yeast
    • Moffat, J., Huang, D., and Andrews, B.J. (2000). Functions of Pho85 cyclin-dependent kinases in budding yeast. Prog. Cell Cycle Res. 4, 97-106.
    • (2000) Prog. Cell Cycle Res. , vol.4 , pp. 97-106
    • Moffat, J.1    Huang, D.2    Andrews, B.J.3
  • 42
    • 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
  • 43
    • 0031671237 scopus 로고    scopus 로고
    • Phosphorylation of Sic1, a cyclin-dependent kinase (Cdk) inhibitor, by Cdk including Pho85 kinase is required for its prompt degradation
    • Nishizawa, M., Kawasumi, M., Fujino, M., and Toh-e, A. (1998). Phosphorylation of Sic1, a cyclin-dependent kinase (Cdk) inhibitor, by Cdk including Pho85 kinase is required for its prompt degradation. Mol. Biol. Cell 9, 2393-2405.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2393-2405
    • Nishizawa, M.1    Kawasumi, M.2    Fujino, M.3    Toh-E, A.4
  • 44
    • 0030059223 scopus 로고    scopus 로고
    • Regulation of Pho4 nuclear localization by the Pho80-Pho85 cyclin-CDK complex
    • O'Neill, E.M., Kaffman, A., Jolly, E.R., and O'Shea, E.K. (1996). Regulation of Pho4 nuclear localization by the Pho80-Pho85 cyclin-CDK complex. Science 271, 209-212.
    • (1996) Science , vol.271 , pp. 209-212
    • O'Neill, E.M.1    Kaffman, A.2    Jolly, E.R.3    O'Shea, E.K.4
  • 45
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • Pawson, T., and Scott, J.D. (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
  • 46
    • 0027191189 scopus 로고
    • FAR1 links the signal transduction pathway to the cell cycle machinery in yeast
    • Peter, M., Gartner, A., Horecka, J., Ammerer, G., and Herskowitz, I. (1993). FAR1 links the signal transduction pathway to the cell cycle machinery in yeast. Cell 73:747-760.
    • (1993) Cell , vol.73 , pp. 747-760
    • Peter, M.1    Gartner, A.2    Horecka, J.3    Ammerer, G.4    Herskowitz, I.5
  • 47
    • 0030838041 scopus 로고    scopus 로고
    • Use of conditional promoters for expression of heterologous proteins in Saccharomyces cerevisiae
    • Ronicke, V., Graulich, W., Mumberg, D., Muller, R., and Funk, M. (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
    • Ronicke, V.1    Graulich, W.2    Mumberg, D.3    Muller, R.4    Funk, M.5
  • 48
    • 0036311160 scopus 로고    scopus 로고
    • Regulation of the transcription factor Gcn4 by Pho85-Cyclin Pcl5
    • Shemer, R., Meimoun, A., Holtzman, T., and Kornitzer, D. (2002). Regulation of the transcription factor Gcn4 by Pho85-Cyclin Pcl5. Mol. Cell. Biol. 22, 5395-5404.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5395-5404
    • Shemer, R.1    Meimoun, A.2    Holtzman, T.3    Kornitzer, D.4
  • 49
    • 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
  • 50
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • Sicheri, F., Moarefi, I., and Kuriyan, J. (1997). Crystal structure of the Src family tyrosine kinase Hck. Nature 385, 602-609.
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 51
    • 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-Krüger, B., and Ferro-Novick, S. (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-Krüger, B.1    Ferro-Novick, S.2
  • 52
    • 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
  • 53
    • 0032493929 scopus 로고    scopus 로고
    • Role of phosphorylation in regulation of the assembly of endocytic coat complexes
    • Slepnev, V.I., Ochoa, G.C., Butler, M.H., Grabs, D., and De Camilli, P.D. (1998). Role of phosphorylation in regulation of the assembly of endocytic coat complexes. Science 281, 821-824.
    • (1998) Science , vol.281 , pp. 821-824
    • Slepnev, V.I.1    Ochoa, G.C.2    Butler, M.H.3    Grabs, D.4    De Camilli, P.D.5
  • 54
    • 0029772320 scopus 로고    scopus 로고
    • The EH-domain-containing protein Pan1 is required for normal organization of the actin cytoskeleton in Saccharomyces cerevisiae
    • Tang, H.Y., and Cai, M. (1996). The EH-domain-containing protein Pan1 is required for normal organization of the actin cytoskeleton in Saccharomyces cerevisiae. Mol. Cell. Biol. 16, 4897-4914.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4897-4914
    • Tang, H.Y.1    Cai, M.2
  • 55
    • 0033622305 scopus 로고    scopus 로고
    • Pan1p, End3p, and S1a1p, three yeast proteins required for normal cortical actin cytoskeleton organization, associate with each other and play essential roles in cell wall morphogenesis
    • Tang, H.Y., Xu, J., and Cai, M. (2000). Pan1p, End3p, and S1a1p, three yeast proteins required for normal cortical actin cytoskeleton organization, associate with each other and play essential roles in cell wall morphogenesis. Mol. Cell. Biol. 20, 12-25.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 12-25
    • Tang, H.Y.1    Xu, J.2    Cai, M.3
  • 56
    • 0037059461 scopus 로고    scopus 로고
    • A combined experimental and computational strategy to define protein interaction networks for peptide recognition modules
    • Tong, A.H. et 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.1
  • 57
    • 0035861532 scopus 로고    scopus 로고
    • Systematic genetic analysis with ordered arrays of yeast deletion mutants
    • Tong, A.H. 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
  • 58
    • 0028332389 scopus 로고
    • Phosphopeptide mapping and phosphoamino acid analysis by electrophoresis and chromatography on thin-layer cellulose plates
    • van der Geer, P., and Hunter, T. (1994). Phosphopeptide mapping and phosphoamino acid analysis by electrophoresis and chromatography on thin-layer cellulose plates. Electrophoresis 15, 544-554.
    • (1994) Electrophoresis , vol.15 , pp. 544-554
    • Van der Geer, P.1    Hunter, T.2
  • 59
    • 0026099833 scopus 로고
    • Labeling of RNA and phosphoproteins in Saccharomyces cerevisiae
    • Warner, J.R. (1991). Labeling of RNA and phosphoproteins in Saccharomyces cerevisiae. Methods Enzymol. 194, 423-434.
    • (1991) Methods Enzymol. , vol.194 , pp. 423-434
    • Warner, J.R.1
  • 60
    • 0035196516 scopus 로고    scopus 로고
    • In vivo role for actin-regulating kinases in endocytosis and yeast epsin phosphorylation
    • Watson, H.A., Cope, M.J., Groen, A.C., Drubin, D.G., and Wendland, B. (2001). In vivo role for actin-regulating kinases in endocytosis and yeast epsin phosphorylation. Mol. Biol. Cell 12:3668-3679.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3668-3679
    • Watson, H.A.1    Cope, M.J.2    Groen, A.C.3    Drubin, D.G.4    Wendland, B.5
  • 61
    • 0033594955 scopus 로고    scopus 로고
    • Genetic dissection of the budding yeast Arp2/3 complex: A comparison of the in vivo and structural roles of individual subunits
    • Winter, D.C., Choe, E.Y., and Li, R. (1999). Genetic dissection of the budding yeast Arp2/3 complex: a comparison of the in vivo and structural roles of individual subunits. Proc. Natl. Acad. Sci. USA 96, 7288-7293.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7288-7293
    • Winter, D.C.1    Choe, E.Y.2    Li, R.3
  • 62
    • 0033529707 scopus 로고    scopus 로고
    • Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis
    • Winzeler, E.A. 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.A.1
  • 63
    • 0033545185 scopus 로고    scopus 로고
    • Regulation of the actin cytoskeleton organization in yeast by a novel serine/threonine kinase Prk1p
    • Zeng, G., and Cai, M. (1999). Regulation of the actin cytoskeleton organization in yeast by a novel serine/threonine kinase Prk1p. J. Cell Biol. 144, 71-82.
    • (1999) J. Cell Biol. , vol.144 , pp. 71-82
    • Zeng, G.1    Cai, M.2
  • 64
    • 0035658368 scopus 로고    scopus 로고
    • Regulation of yeast actin cytoskeleton-regulatory complex Pan1p/S1a1p/End3p by serine/ threonine kinase Prk1p
    • Singer-Kruger and Ferro-Novick 1997
    • Zeng, G., Yu, X., and Cai, M. (2001). Regulation of yeast actin cytoskeleton-regulatory complex Pan1p/S1a1p/End3p by serine/ threonine kinase Prk1p. Mol. Biol. Cell 12, 3759-3772. Singer-Kruger and Ferro-Novick 1997
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3759-3772
    • Zeng, G.1    Yu, X.2    Cai, M.3


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