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Volumn 22, Issue 20, 2002, Pages 6946-6958

Rsp5p, a new link between the actin cytoskeleton and endocytosis in the yeast Saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

F ACTIN; GENE PRODUCT; ISOPROTEIN; LATRUNCULIN A; PROTEIN RSP5P; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 0036786951     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.22.20.6946-6958.2002     Document Type: Article
Times cited : (48)

References (74)
  • 1
    • 0025969670 scopus 로고
    • Staining of actin with fluorochrome-conjugated phalloidin
    • Adams, A. E., and J. R. Pringle. 1991. Staining of actin with fluorochrome-conjugated phalloidin. Methods Enzymol. 194:729-731.
    • (1991) Methods Enzymol. , vol.194 , pp. 729-731
    • Adams, A.E.1    Pringle, J.R.2
  • 2
    • 0030978526 scopus 로고    scopus 로고
    • High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A
    • Ayscough, K. R., J. Stryker, N. Pokala, M. Sanders, P. Crews, and D. G. Drubin. 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.G.6
  • 3
    • 0023663064 scopus 로고
    • Arthrin, a myofibrillar protein of insect flight muscle, is an actin-ubiquitin conjugate
    • Ball, E., C. C. Karlik, C. J. Beall, D. L. Saville, J. C. Sparrow, B. Bullard, and E. A. Fyrberg. 1987. Arthrin, a myofibrillar protein of insect flight muscle, is an actin-ubiquitin conjugate. Cell 51:221-228.
    • (1987) Cell , vol.51 , pp. 221-228
    • Ball, E.1    Karlik, C.C.2    Beall, C.J.3    Saville, D.L.4    Sparrow, J.C.5    Bullard, B.6    Fyrberg, E.A.7
  • 4
    • 0033588918 scopus 로고    scopus 로고
    • Starvation induces vacuolar targeting and degradation of the tryptophan permease in yeast
    • Beck, T., A. Schmidt, and M. N. Hall. 1999. Starvation induces vacuolar targeting and degradation of the tryptophan permease in yeast. J. Cell Biol. 146:1227-1238.
    • (1999) J. Cell Biol. , vol.146 , pp. 1227-1238
    • Beck, T.1    Schmidt, A.2    Hall, M.N.3
  • 5
    • 0032494082 scopus 로고    scopus 로고
    • The yeast V159N actin mutant reveals roles for actin dynamics in vivo
    • Belmont, L. D., and D. G. Drubin. 1998. The yeast V159N actin mutant reveals roles for actin dynamics in vivo. J. Cell Biol. 142:1289-1299.
    • (1998) J. Cell Biol. , vol.142 , pp. 1289-1299
    • Belmont, L.D.1    Drubin, D.G.2
  • 6
    • 0028024386 scopus 로고
    • The END3 gene encodes a protein that is required for the internalization step of endocytosis and for actin cytoskeleton organization in yeast
    • Bénédetti, H., S. Raths, F. Crausaz, and H. Riezman. 1994. The END3 gene encodes a protein that is required for the internalization step of endocytosis and for actin cytoskeleton organization in yeast. Mol. Biol. Cell 5:1023-1037.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 1023-1037
    • Bénédetti, H.1    Raths, S.2    Crausaz, F.3    Riezman, H.4
  • 7
    • 0028280864 scopus 로고
    • Subcellular locations of MOD5 proteins: Mapping of sequences sufficient for targeting to mitochondria and demonstration that mitochondrial and nuclear isoforms commingle in the cytosol
    • Boguta, M., L. A. Hunter, W. C. Shen, E. C. Gillman, N. C. Martin, and A. K. Hopper. 1994. Subcellular locations of MOD5 proteins: mapping of sequences sufficient for targeting to mitochondria and demonstration that mitochondrial and nuclear isoforms commingle in the cytosol. Mol. Cell. Biol. 14:2298-2306.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2298-2306
    • Boguta, M.1    Hunter, L.A.2    Shen, W.C.3    Gillman, E.C.4    Martin, N.C.5    Hopper, A.K.6
  • 8
    • 0034617224 scopus 로고    scopus 로고
    • Rsp5 WW domains interact directly with the carboxyl-terminal domain of RNA polymerase II
    • Chang, A., S. Cheang, X. Espanel, and M. Sudol. 2000. Rsp5 WW domains interact directly with the carboxyl-terminal domain of RNA polymerase II. J. Biol. Chem. 275:20562-20571.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20562-20571
    • Chang, A.1    Cheang, S.2    Espanel, X.3    Sudol, M.4
  • 9
    • 0026599048 scopus 로고
    • One-step transformation of yeast in stationary phase
    • Chen, D. C., B. C. Yang, and T. T. Kuo. 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
  • 10
    • 0033594087 scopus 로고    scopus 로고
    • Novel protein kinases Ark1p and Prk1p associate with and regulate the cortical actin cytoskeleton in budding yeast
    • Cope, M. J., S. Yang, C. Shang, and D. G. Drubin. 1999. Novel protein kinases Ark1p and Prk1p associate with and regulate the cortical actin cytoskeleton in budding yeast. J. Cell Biol. 144:1203-1218.
    • (1999) J. Cell Biol. , vol.144 , pp. 1203-1218
    • Cope, M.J.1    Yang, S.2    Shang, C.3    Drubin, D.G.4
  • 11
    • 0031567590 scopus 로고    scopus 로고
    • Glucose activation of the yeast plasma membrane H+-ATPase requires the ubiquitin-proteasome proteolytic pathway
    • de la Fuente, N., A. M. Maldonado, and F. Portillo. 1997. Glucose activation of the yeast plasma membrane H+-ATPase requires the ubiquitin-proteasome proteolytic pathway. FEBS Lett. 411:308-312.
    • (1997) FEBS Lett. , vol.411 , pp. 308-312
    • De la Fuente, N.1    Maldonado, A.M.2    Portillo, F.3
  • 12
    • 0034932864 scopus 로고    scopus 로고
    • Yeast Eps15-like endocytic protein, Pan1p, activates the Arp2/3 complex
    • Duncan, M. C., M. J. Cope, B. L. Goode, B. Wendland, and D. G. Drubin. 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
  • 13
    • 0035149694 scopus 로고    scopus 로고
    • Domains of the Rsp5 ubiquitin-protein ligase required for receptor-mediated and fluid-phase endocytosis
    • Dunn, R., and L. Hicke. 2001. Domains of the Rsp5 ubiquitin-protein ligase required for receptor-mediated and fluid-phase endocytosis. Mol. Biol. Cell 12:421-435.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 421-435
    • Dunn, R.1    Hicke, L.2
  • 14
    • 0035854827 scopus 로고    scopus 로고
    • Multiple roles for Rsp5p-dependent ubiquitination at the internalization step of endocytosis
    • Dunn, R., and L. Hicke. 2001. Multiple roles for Rsp5p-dependent ubiquitination at the internalization step of endocytosis. J. Biol. Chem. 276:25974-25981.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25974-25981
    • Dunn, R.1    Hicke, L.2
  • 16
    • 0033553857 scopus 로고    scopus 로고
    • A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae
    • Fisk, H. A., and M. P. Yaffe. 1999. A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae. J. Cell Biol. 145:1199-1208.
    • (1999) J. Cell Biol. , vol.145 , pp. 1199-1208
    • Fisk, H.A.1    Yaffe, M.P.2
  • 18
    • 0035155749 scopus 로고    scopus 로고
    • WW domains of Rsp5p define different functions: Determination of roles in fluid phase and uracil permease endocytosis in Saccharomyces cerevisiae
    • Gajewska, B., J. Kamińska, A. Jesionowska, N. C. Martin, A. K. Hopper, and T. Zoła̧dek. 2001. WW domains of Rsp5p define different functions: determination of roles in fluid phase and uracil permease endocytosis in Saccharomyces cerevisiae. Genetics 157:91-101.
    • (2001) Genetics , vol.157 , pp. 91-101
    • Gajewska, B.1    Kamińska, J.2    Jesionowska, A.3    Martin, N.C.4    Hopper, A.K.5    Zoła̧dek, T.6
  • 19
    • 15844424064 scopus 로고    scopus 로고
    • Ubiquitination mediated by the Npi1p/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease
    • Galan, J. M., V. Moreau, B. André, C. Volland, and R. Haguenauer-Tsapis. 1996. Ubiquitination mediated by the Npi1p/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease. J. Biol. Chem. 271:10946-10952.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10946-10952
    • Galan, J.M.1    Moreau, V.2    André, B.3    Volland, C.4    Haguenauer-Tsapis, R.5
  • 20
    • 0034663930 scopus 로고    scopus 로고
    • An intact SH3 domain is required for myosin I-induced actin polymerization
    • Geli, M. I., R. Lombardi, B. Schmelzl, and H. Riezman. 2000. An intact SH3 domain is required for myosin I-induced actin polymerization. EMBO J. 19:4281-4291.
    • (2000) EMBO J. , vol.19 , pp. 4281-4291
    • Geli, M.I.1    Lombardi, R.2    Schmelzl, B.3    Riezman, H.4
  • 21
    • 0031980575 scopus 로고    scopus 로고
    • Endocytic internalization in yeast and animal cells: Similar and different
    • Geli, M. I., and H. Riezman. 1998. Endocytic internalization in yeast and animal cells: similar and different. J. Cell Sci. 111:1031-1037.
    • (1998) J. Cell Sci. , vol.111 , pp. 1031-1037
    • Geli, M.I.1    Riezman, H.2
  • 22
    • 0035972165 scopus 로고    scopus 로고
    • Activation of the Arp2/3 complex by the actin filament binding protein Abp1p
    • Goode, B. L., A. A. Rodal, G. Barnes, and D. G. Drubin. 2001. Activation of the Arp2/3 complex by the actin filament binding protein Abp1p. J. Cell Biol. 153:627-634.
    • (2001) J. Cell Biol. , vol.153 , pp. 627-634
    • Goode, B.L.1    Rodal, A.A.2    Barnes, G.3    Drubin, D.G.4
  • 23
    • 0027515605 scopus 로고
    • Synthetic enhancement in gene interaction: A genetic tool come of age
    • Guarente, L. 1993. Synthetic enhancement in gene interaction: a genetic tool come of age. Trends Genet. 9:362-366.
    • (1993) Trends Genet. , vol.9 , pp. 362-366
    • Guarente, L.1
  • 24
    • 0344334023 scopus 로고    scopus 로고
    • Nedd4-like proteins: An emerging family of ubiquitin-protein ligases implicated in diverse cellular functions
    • Harvey, K. F., and S. Kumar. 1999. Nedd4-like proteins: an emerging family of ubiquitin-protein ligases implicated in diverse cellular functions. Trends Cell Biol. 9:166-169.
    • (1999) Trends Cell Biol. , vol.9 , pp. 166-169
    • Harvey, K.F.1    Kumar, S.2
  • 25
    • 0028971506 scopus 로고
    • NPl1, an essential yeast gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase
    • Hein, C., J. Y. Springael, C. Volland, R. Haguenauer-Tsapis, and B. André. 1995. NPl1, an essential yeast gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase. Mol. Microbiol. 18:77-87.
    • (1995) Mol. Microbiol. , vol.18 , pp. 77-87
    • Hein, C.1    Springael, J.Y.2    Volland, C.3    Haguenauer-Tsapis, R.4    André, B.5
  • 26
    • 0035858866 scopus 로고    scopus 로고
    • Components of a ubiquitin ligase complex specify polyubiquitination and intracellular trafficking of the general amino acid permease
    • Helliwell, S. B., S. Losko, and C. A. Kaiser. 2001. Components of a ubiquitin ligase complex specify polyubiquitination and intracellular trafficking of the general amino acid permease. J. Cell Biol. 153:649-662.
    • (2001) J. Cell Biol. , vol.153 , pp. 649-662
    • Helliwell, S.B.1    Losko, S.2    Kaiser, C.A.3
  • 27
    • 0027244817 scopus 로고
    • Synthetic-lethal interactions identify two novel genes, SLA1 and SLA2, that control membrane cytoskeleton assembly in Saccharomyces cerevisiae
    • Holtzman, D. A., S. Yang, and D. G. Drubin. 1993. Synthetic-lethal interactions identify two novel genes, SLA1 and SLA2, that control membrane cytoskeleton assembly in Saccharomyces cerevisiae. J. Cell Biol. 122:635-644.
    • (1993) J. Cell Biol. , vol.122 , pp. 635-644
    • Holtzman, D.A.1    Yang, S.2    Drubin, D.G.3
  • 28
    • 0034268493 scopus 로고    scopus 로고
    • Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing
    • Hoppe, T., K. Matuschewski, M. Rape, S. Schlenker, H. D. Ulrich, and S. Jentsch. 2000. Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing. Cell 102:577-586.
    • (2000) Cell , vol.102 , pp. 577-586
    • Hoppe, T.1    Matuschewski, K.2    Rape, M.3    Schlenker, S.4    Ulrich, H.D.5    Jentsch, S.6
  • 29
    • 0030037701 scopus 로고    scopus 로고
    • Identification of ACT4, a novel essential actin-related gene in the yeast Saccharomyces cerevisiae
    • Huang, M. E., J. L. Souciet, J. C. Chuat, and F. Galibert. 1996. Identification of ACT4, a novel essential actin-related gene in the yeast Saccharomyces cerevisiae. Yeast 12:839-848.
    • (1996) Yeast , vol.12 , pp. 839-848
    • Huang, M.E.1    Souciet, J.L.2    Chuat, J.C.3    Galibert, F.4
  • 30
    • 0029036701 scopus 로고
    • A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase
    • Huibregtse, J. M., M. Scheffner, S. Beaudenon, and P. M. Howley. 1995. A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc. Natl. Acad. Sci. USA 92:5249.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5249
    • Huibregtse, J.M.1    Scheffner, M.2    Beaudenon, S.3    Howley, P.M.4
  • 31
    • 0032992123 scopus 로고    scopus 로고
    • Cooperation of two actin-binding proteins, cofilin and Aip1, in Saccharomyces cerevisiae
    • Iida, K., and I. Yahara. 1999. Cooperation of two actin-binding proteins, cofilin and Aip1, in Saccharomyces cerevisiae. Genes Cells 4:21-32.
    • (1999) Genes Cells , vol.4 , pp. 21-32
    • Iida, K.1    Yahara, I.2
  • 32
    • 0035806991 scopus 로고    scopus 로고
    • Cytoskeleton: Actin and endocytosis-no longer the weakest link
    • Jeng, R. L., and M. D. Welch. 2001. Cytoskeleton: actin and endocytosis-no longer the weakest link. Curr. Biol. 11:R691-R694.
    • (2001) Curr. Biol. , vol.11
    • Jeng, R.L.1    Welch, M.D.2
  • 34
    • 0030797467 scopus 로고    scopus 로고
    • Cofilin promotes rapid actin filament turnover in vivo
    • Lappalainen, P., and D. G. Drubin. 1997. Cofilin promotes rapid actin filament turnover in vivo. Nature 388:78-82.
    • (1997) Nature , vol.388 , pp. 78-82
    • Lappalainen, P.1    Drubin, D.G.2
  • 35
    • 0034707580 scopus 로고    scopus 로고
    • Direct involvement of yeast type I myosins in Cdc42-dependent actin polymerization
    • Lechler, T., A. Shevchenko, and R. Li. 2000. Direct involvement of yeast type I myosins in Cdc42-dependent actin polymerization. J. Cell Biol. 148:363-373.
    • (2000) J. Cell Biol. , vol.148 , pp. 363-373
    • Lechler, T.1    Shevchenko, A.2    Li, R.3
  • 36
    • 0031045512 scopus 로고    scopus 로고
    • Bee1, a yeast protein with homology to Wiskott-Aldrich syndrome protein, is critical for the assembly of cortical actin cytoskeleton
    • Li, R. 1997. Bee1, a yeast protein with homology to Wiskott-Aldrich syndrome protein, is critical for the assembly of cortical actin cytoskeleton. J. Cell Biol. 136:649-658.
    • (1997) J. Cell Biol. , vol.136 , pp. 649-658
    • Li, R.1
  • 37
    • 0028871169 scopus 로고
    • Regulation of cortical actin cytoskeleton assembly during polarized cell growth in budding yeast
    • Li, R., Y. Zheng, and D. G. Drubin. 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
  • 38
    • 0032585538 scopus 로고    scopus 로고
    • Scar and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex
    • Machesky, L. M., and R. H. Insall. 1998. Scar and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex. Curr. Biol. 8:1347-1356.
    • (1998) Curr. Biol. , vol.8 , pp. 1347-1356
    • Machesky, L.M.1    Insall, R.H.2
  • 39
    • 0032835492 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae homologue of human Wiskott-Aldrich syndrome protein Las17p interacts with the Arp2/3 complex
    • Madania, A., P. Dumoulin, S. Grava, H. Kitamoto, C. Scharer-Brodbeck, A. Soulard, V. Moreau, and B. Winsor. 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
  • 40
    • 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 S. W. Craig. 1997. The I/LWEQ module: a conserved sequence that signifies F-actin binding in functionally diverse proteins from yeast to mammals. Proc. Natl. Acad. Sci. USA 94:5679-5684.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5679-5684
    • McCann, R.O.1    Craig, S.W.2
  • 41
    • 0030813921 scopus 로고    scopus 로고
    • The yeast actin-related protein Arp2p is required for the internalization step of endocytosis
    • Moreau, V., J. M. Galan, G. Devilliers, R. Haguenauer-Tsapis, and B. Winsor. 1997. The yeast actin-related protein Arp2p is required for the internalization step of endocytosis. Mol. Biol. Cell 8:1361-1375.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1361-1375
    • Moreau, V.1    Galan, J.M.2    Devilliers, G.3    Haguenauer-Tsapis, R.4    Winsor, B.5
  • 42
    • 0029959468 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae actin-related protein Arp2 is involved in the actin cytoskeleton
    • Moreau, V., A. Madania, R. P. Martin, and B. Winson. 1996. The Saccharomyces cerevisiae actin-related protein Arp2 is involved in the actin cytoskeleton. J. Cell Biol. 134:117-132.
    • (1996) J. Cell Biol. , vol.134 , pp. 117-132
    • Moreau, V.1    Madania, A.2    Martin, R.P.3    Winson, B.4
  • 43
    • 0028204439 scopus 로고
    • Ultrastructure of the yeast actin cytoskeleton and its association with the plasma membrane
    • Mulholland, J., D. Preuss, A. Moon, A. Wong, D. Drubin, and D. Botstein. 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
  • 44
    • 0032568650 scopus 로고    scopus 로고
    • The interaction of Arp2/3 complex with actin: Nucleation, high affinity pointed end capping, and formation of branching networks of filaments
    • Mullins, R. D., J. A. Heuser, and T. D. Pollard. 1998. The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments. Proc. Natl. Acad. Sci. USA 95:6181-6186.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6181-6186
    • Mullins, R.D.1    Heuser, J.A.2    Pollard, T.D.3
  • 45
    • 0034801441 scopus 로고    scopus 로고
    • Rpg1p/Tif32p, a subunit of translation initiation factor 3, interacts with actin-associated protein Sla2p
    • Palecek, J., J. Hasek, and H. Ruis. 2001. Rpg1p/Tif32p, a subunit of translation initiation factor 3, interacts with actin-associated protein Sla2p. Biochem. Biophys. Res. Commun. 282:1244-1250.
    • (2001) Biochem. Biophys. Res. Commun. , vol.282 , pp. 1244-1250
    • Palecek, J.1    Hasek, J.2    Ruis, H.3
  • 47
    • 0034056057 scopus 로고    scopus 로고
    • Polarization of cell growth in yeast
    • Pruyne, D., and A. Bretscher. 2000. Polarization of cell growth in yeast. J. Cell Sci. 113:571-585.
    • (2000) J. Cell Sci. , vol.113 , pp. 571-585
    • Pruyne, D.1    Bretscher, A.2
  • 48
    • 0034605038 scopus 로고    scopus 로고
    • Molecular links between endocytosis and the actin cytoskeleton
    • Qualmann, B., M. M. Kessels, and R. B. Kelly. 2000. Molecular links between endocytosis and the actin cytoskeleton. J. Cell Biol. 150:F111-F116.
    • (2000) J. Cell Biol. , vol.150
    • Qualmann, B.1    Kessels, M.M.2    Kelly, R.B.3
  • 49
    • 0027455339 scopus 로고
    • end3 and end4: Two mutants defective in receptor-mediated and fluid phase endocytosis in Saccharomyces cerevisiae
    • Raths, S., J. Rohrer, F. Crausaz, and H. Riezman. 1993. end3 and end4: two mutants defective in receptor-mediated and fluid phase endocytosis in Saccharomyces cerevisiae. J. Cell Biol. 120:55-65.
    • (1993) J. Cell Biol. , vol.120 , pp. 55-65
    • Raths, S.1    Rohrer, J.2    Crausaz, F.3    Riezman, H.4
  • 50
    • 0034677991 scopus 로고    scopus 로고
    • Ubiquitination of the PEST-like endocytosis signal of the yeast a-factor receptor
    • Roth, A. F., and N. G. Davis. 2000. Ubiquitination of the PEST-like endocytosis signal of the yeast a-factor receptor. J. Biol. Chem. 275:8143-8153.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8143-8153
    • Roth, A.F.1    Davis, N.G.2
  • 51
    • 0034235434 scopus 로고    scopus 로고
    • Ubiquitination and endocytosis of plasma membrane proteins: Role of Nedd4/Rsp5p family of ubiquitin-protein ligases
    • Rotin, D., O. Staub, and R. Haguenauer-Tsapis. 2000. Ubiquitination and endocytosis of plasma membrane proteins: role of Nedd4/Rsp5p family of ubiquitin-protein ligases. J. Membr. Biol. 176:1-17.
    • (2000) J. Membr. Biol. , vol.176 , pp. 1-17
    • Rotin, D.1    Staub, O.2    Haguenauer-Tsapis, R.3
  • 53
    • 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
  • 54
    • 0035941194 scopus 로고    scopus 로고
    • Ubiquitin is required for sorting to the vacuole of the yeast general amino acid permease, Gap1
    • Soetens, O., J. O. De Craene, and B. André. 2001. Ubiquitin is required for sorting to the vacuole of the yeast general amino acid permease, Gap1. J. Biol. Chem. 276:43949-43957.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43949-43957
    • Soetens, O.1    De Craene, J.O.2    André, B.3
  • 55
    • 0033551112 scopus 로고    scopus 로고
    • The yeast Npi1/Rsp5 ubiquitin ligase lacking its N-terminal C2 domain is competent for ubiquitination but not for subsequent endocytosis of the Gap1 permease
    • Springael, J. Y., J. O. De Craene, and B. André. 1999. The yeast Npi1/Rsp5 ubiquitin ligase lacking its N-terminal C2 domain is competent for ubiquitination but not for subsequent endocytosis of the Gap1 permease. Biochem. Biophys. Res. Commun. 257:561-566.
    • (1999) Biochem. Biophys. Res. Commun. , vol.257 , pp. 561-566
    • Springael, J.Y.1    De Craene, J.O.2    André, B.3
  • 56
    • 0030006284 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization
    • Symons, M., J. M. Derry, B. Karlak, S. Jiang, V. Lemahieu, F. Mccormick, U. Francke, and A. Abo. 1996. Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization. Cell 84:723-734.
    • (1996) Cell , vol.84 , pp. 723-734
    • Symons, M.1    Derry, J.M.2    Karlak, B.3    Jiang, S.4    Lemahieu, V.5    Mccormick, F.6    Francke, U.7    Abo, A.8
  • 57
    • 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 M. Cai. 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
  • 58
    • 0344279906 scopus 로고    scopus 로고
    • EH domain proteins Pan1p and End3p are components of a complex that plays a dual role in organization of the cortical actin cytoskeleton and endocytosis in Saccharomyces cerevisiae
    • Tang, H. Y., A. Munn, and M. Cai. 1997. EH domain proteins Pan1p and End3p are components of a complex that plays a dual role in organization of the cortical actin cytoskeleton and endocytosis in Saccharomyces cerevisiae. Mol. Cell. Biol. 17:4294-4304.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4294-4304
    • Tang, H.Y.1    Munn, A.2    Cai, M.3
  • 59
    • 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., J. Xu, and M. Cai. 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
  • 60
    • 0031416482 scopus 로고    scopus 로고
    • Actin-binding verprolin is a polarity development protein required for the morphogenesis and function of the yeast actin cytoskeleton
    • Vaduva, G., N. C. Martin, and A. K. Hopper. 1997. Actin-binding verprolin is a polarity development protein required for the morphogenesis and function of the yeast actin cytoskeleton. J. Cell Biol. 139:1821-1833.
    • (1997) J. Cell Biol. , vol.139 , pp. 1821-1833
    • Vaduva, G.1    Martin, N.C.2    Hopper, A.K.3
  • 61
    • 0028307059 scopus 로고
    • Endocytosis and degradation of the yeast uracil permease under adverse conditions
    • Volland, C., D. Urban-Grimal, G. Geraud, and R. Haguenauer-Tsapis. 1994. Endocytosis and degradation of the yeast uracil permease under adverse conditions. J. Biol. Chem. 269:9833-9841.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9833-9841
    • Volland, C.1    Urban-Grimal, D.2    Geraud, G.3    Haguenauer-Tsapis, R.4
  • 63
    • 0032489873 scopus 로고    scopus 로고
    • Pan1, yeast eps15, functions as a multivalent adaptor that coordinates protein-protein interactions essential for endocytosis
    • Wendland, B., and S. D. Emr. 1998. Pan1, yeast eps15, functions as a multivalent adaptor that coordinates protein-protein interactions essential for endocytosis. J. Cell Biol. 141:71-84.
    • (1998) J. Cell Biol. , vol.141 , pp. 71-84
    • Wendland, B.1    Emr, S.D.2
  • 64
    • 0033575748 scopus 로고    scopus 로고
    • Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin and are required for endocytosis
    • Wendland, B., K. E. Steece, and S. D. Emr. 1999. Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin and are required for endocytosis. EMBO J. 18:4383-4393.
    • (1999) EMBO J. , vol.18 , pp. 4383-4393
    • Wendland, B.1    Steece, K.E.2    Emr, S.D.3
  • 65
    • 0030785341 scopus 로고    scopus 로고
    • End4p/Sla2p interacts with actin-associated proteins for endocytosis in Saccharomyces cerevisiae
    • Wesp, A., L. Hicke, J. Palecek, R. Lombardi, T. Aust, A. L. Munn, and H. Riezman. 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
  • 66
    • 0033528995 scopus 로고    scopus 로고
    • Activation of the yeast Arp2/3 complex by Bee1p, a WASP-family protein
    • Winter, D., T. Lechler, and R. Li. 1999. Activation of the yeast Arp2/3 complex by Bee1p, a WASP-family protein. Curr. Biol. 9:501-504.
    • (1999) Curr. Biol. , vol.9 , pp. 501-504
    • Winter, D.1    Lechler, T.2    Li, R.3
  • 67
    • 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., E. Y. Choe, and R. Li. 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
  • 68
    • 0033506495 scopus 로고    scopus 로고
    • Ubiquitin metabolism affects cellular response to volatile anesthetics in yeast
    • Wolfe, D., T. Reiner, J. L. Keeley, M. Pizzini, and R. L. Keil. 1999. Ubiquitin metabolism affects cellular response to volatile anesthetics in yeast. Mol. Cell. Biol. 19:8254-8262.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8254-8262
    • Wolfe, D.1    Reiner, T.2    Keeley, J.L.3    Pizzini, M.4    Keil, R.L.5
  • 69
    • 0032589216 scopus 로고    scopus 로고
    • Sla2p is associated with the yeast cortical actin cytoskeleton via redundant localization signals
    • Yang, S., M. J. Cope, and D. G. Drubin. 1999. Sla2p is associated with the yeast cortical actin cytoskeleton via redundant localization signals. Mol. Biol. Cell 10:2265-2283.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2265-2283
    • Yang, S.1    Cope, M.J.2    Drubin, D.G.3
  • 70
    • 0030006865 scopus 로고    scopus 로고
    • Bul1, a new protein that binds to the Rsp5 ubiquitin ligase in Saccharomyces cerevisiae
    • Yashiroda, H., T. Oguchi, Y. Yasuda, E. Toh, and Y. Kikuchi. 1996. Bul1, a new protein that binds to the Rsp5 ubiquitin ligase in Saccharomyces cerevisiae. Mol. Cell. Biol. 16:3255-3263.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3255-3263
    • Yashiroda, H.1    Oguchi, T.2    Yasuda, Y.3    Toh, E.4    Kikuchi, Y.5
  • 71
    • 0033545185 scopus 로고    scopus 로고
    • Regulation of the actin cytoskeleton organization in yeast by a novel serine/threonine kinase Prk1p
    • Zeng, G., and M. Cal. 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    Cal, M.2
  • 72
    • 1842374437 scopus 로고    scopus 로고
    • MDP1, a Saccharomyces cerevisiae gene involved in mitochondrial/cytoplasmic protein distribution, is identical to the ubiquitin-protein ligase gene RSP5
    • Zoła̧dek, T., A. Tobiasz, G. Vaduva, M. Boguta, N. C. Martin, and A. K. Hopper. 1997. MDP1, a Saccharomyces cerevisiae gene involved in mitochondrial/cytoplasmic protein distribution, is identical to the ubiquitin-protein ligase gene RSP5. Genetics 145:595-603.
    • (1997) Genetics , vol.145 , pp. 595-603
    • Zoła̧dek, T.1    Tobiasz, A.2    Vaduva, G.3    Boguta, M.4    Martin, N.C.5    Hopper, A.K.6
  • 73
    • 0028791882 scopus 로고
    • Mutations altering the mitochondrial-cytoplasmic distribution of Mod5p implicate the actin cytoskeleton and mRNA 3′ ends and/or protein synthesis in mitochondrial delivery
    • Zoła̧dek, T., G. Vaduva, L. A. Hunter, M. Boguta, B. D. Go, N. C. Martin, and A. K. Hopper. 1995. Mutations altering the mitochondrial-cytoplasmic distribution of Mod5p implicate the actin cytoskeleton and mRNA 3′ ends and/or protein synthesis in mitochondrial delivery. Mol. Cell. Biol. 15:6884-6894.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6884-6894
    • Zoła̧dek, T.1    Vaduva, G.2    Hunter, L.A.3    Boguta, M.4    Go, B.D.5    Martin, N.C.6    Hopper, A.K.7
  • 74
    • 0032832577 scopus 로고    scopus 로고
    • Temperature-sensitive mutations in the Saccharomyces cerevisiae MRT4, GRC5, SLA2 and THS1 genes result in defects in mRNA turnover
    • Zuk, D., J. P. Belk, and A. Jacobson. 1999. Temperature-sensitive mutations in the Saccharomyces cerevisiae MRT4, GRC5, SLA2 and THS1 genes result in defects in mRNA turnover. Genetics 153:35-47.
    • (1999) Genetics , vol.153 , pp. 35-47
    • Zuk, D.1    Belk, J.P.2    Jacobson, A.3


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