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Volumn 126, Issue 20, 2013, Pages 4560-4571

Bem3, a Cdc42 GTPase-activating protein, traffics to an intracellular compartment and recruits the secretory Rab GTPase Sec4 to endomembranes

Author keywords

Bem3; Cell polarity; Recycling pathway; Secretory pathway; Vesicle trafficking

Indexed keywords

BEM3 PROTEIN; CELL MARKER; CELL PROTEIN; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; LATRUNCULIN A; LIPOSOME; MEMBRANE PROTEIN; PROTEIN CDC42; RAB PROTEIN; RCY1 PROTEIN; SEC4 PROTEIN; SLA2 PROTEIN; UNCLASSIFIED DRUG;

EID: 84885439985     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.117663     Document Type: Article
Times cited : (20)

References (88)
  • 1
    • 0037518120 scopus 로고    scopus 로고
    • The yeast Epsin Ent1 is recruited to membranes through multiple independent interactions
    • Aguilar, R. C., Watson, H. A. and Wendland, B. (2003). The yeast Epsin Ent1 is recruited to membranes through multiple independent interactions. J. Biol. Chem. 278, 10737-10743.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10737-10743
    • Aguilar, R.C.1    Watson, H.A.2    Wendland, B.3
  • 3
    • 4344670341 scopus 로고    scopus 로고
    • Involvement of the late secretory pathway in actin regulation and mRNA transport in yeast
    • Aronov, S. and Gerst, J. E. (2004). Involvement of the late secretory pathway in actin regulation and mRNA transport in yeast. J. Biol. Chem. 279, 36962-36971.
    • (2004) J. Biol. Chem. , vol.279 , pp. 36962-36971
    • Aronov, S.1    Gerst, J.E.2
  • 4
    • 0346731278 scopus 로고    scopus 로고
    • The Sla2p talin domain plays a role in endocytosis in Saccharomyces cerevisiae
    • Baggett, J. J., D'Aquino, K. E. and Wendland, B. (2003). The Sla2p talin domain plays a role in endocytosis in Saccharomyces cerevisiae. Genetics 165, 1661-1674.
    • (2003) Genetics , vol.165 , pp. 1661-1674
    • Baggett, J.J.1    D'Aquino, K.E.2    Wendland, B.3
  • 5
    • 77958496919 scopus 로고    scopus 로고
    • Endophilin functions as a membrane-bending molecule and is delivered to endocytic zones by exocytosis
    • Bai, J. H., Hu, Z. T., Dittman, J. S., Pym, E. C. G. and Kaplan, J. M. (2010). Endophilin functions as a membrane-bending molecule and is delivered to endocytic zones by exocytosis. Cell 143, 430-441.
    • (2010) Cell , vol.143 , pp. 430-441
    • Bai, J.H.1    Hu, Z.T.2    Dittman, J.S.3    Pym, E.C.G.4    Kaplan, J.M.5
  • 8
    • 0141541745 scopus 로고    scopus 로고
    • The role of Cdc42p GTPase-activating proteins in assembly of the septin ring in yeast
    • Caviston, J. P., Longtine, M., Pringle, J. R. and Bi, E. (2003). The role of Cdc42p GTPase-activating proteins in assembly of the septin ring in yeast. Mol. Biol. Cell 14, 4051-4066.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4051-4066
    • Caviston, J.P.1    Longtine, M.2    Pringle, J.R.3    Bi, E.4
  • 9
    • 0033279824 scopus 로고    scopus 로고
    • Cell polarity in yeast
    • Chant, J. (1999). Cell polarity in yeast. Annu. Rev. Cell Dev. Biol. 15, 365-391.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 365-391
    • Chant, J.1
  • 10
    • 79957845124 scopus 로고    scopus 로고
    • The mating projections of Saccharomyces cerevisiae and Candida albicans show key characteristics of hyphal growth
    • Chapa-y-Lazo, B., Lee, S., Regan, H., Sudbery, P.; Chapa-y-Lazo; Lee; Regan; Sudbery (2011). The mating projections of Saccharomyces cerevisiae and Candida albicans show key characteristics of hyphal growth. Fungal Biol. 115, 547-556.
    • (2011) Fungal Biol. , vol.115 , pp. 547-556
    • Chapa-y-Lazo, B.1    Lee, S.2    Regan, H.3    Sudbery, P.4    Chapa-y-Lazo5    Lee6    Sudbery, R.7
  • 11
    • 0035142431 scopus 로고    scopus 로고
    • Expression and functional analyses of Rab8 and Rab11a in exocytic transport from trans-Golgi network
    • Chen, W. and Wandinger-Ness, A. (2001). Expression and functional analyses of Rab8 and Rab11a in exocytic transport from trans-Golgi network. Methods Enzymol. 329, 165-175.
    • (2001) Methods Enzymol. , vol.329 , pp. 165-175
    • Chen, W.1    Wandinger-Ness, A.2
  • 13
    • 11144333620 scopus 로고    scopus 로고
    • Ypt31/32 GTPases and their novel F-box effector protein Rcy1 regulate protein recycling
    • Chen, S. H., Chen, S., Tokarev, A. A., Liu, F. L., Jedd, G. and Segev, N. (2005). Ypt31/32 GTPases and their novel F-box effector protein Rcy1 regulate protein recycling. Mol. Biol. Cell 16, 178-192.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 178-192
    • Chen, S.H.1    Chen, S.2    Tokarev, A.A.3    Liu, F.L.4    Jedd, G.5    Segev, N.6
  • 14
    • 0033800536 scopus 로고    scopus 로고
    • The peroxisome biogenesis factors pex4p, pex22p, pex1p, and pex6p act in the terminal steps of peroxisomal matrix protein import Mol
    • Collins, C. S., Kalish, J. E., Morrel, J. C., McCaffery, J. M. and Gould, S. J. (2010). The peroxisome biogenesis factors pex4p, pex22p, pex1p, and pex6p act in the terminal steps of peroxisomal matrix protein import Mol. Cell Biol. 20, 7516-7526.
    • (2010) Cell Biol. , vol.20 , pp. 7516-7526
    • Collins, C.S.1    Kalish, J.E.2    Morrel, J.C.3    McCaffery, J.M.4    Gould, S.J.5
  • 15
    • 23744472634 scopus 로고    scopus 로고
    • Candida albicans hyphae have a Spitzenkörper that is distinct from the polarisome found in yeast and pseudohyphae
    • Crampin, H., Finley, K., Gerami-Nejad, M., Court, H., Gale, C., Berman, J. and Sudbery, P. (2005). Candida albicans hyphae have a Spitzenkörper that is distinct from the polarisome found in yeast and pseudohyphae. J. Cell Sci. 118, 2935-2947.
    • (2005) J. Cell Sci. , vol.118 , pp. 2935-2947
    • Crampin, H.1    Finley, K.2    Gerami-Nejad, M.3    Court, H.4    Gale, C.5    Berman, J.6    Sudbery, P.7
  • 18
    • 0033611051 scopus 로고    scopus 로고
    • An actin-binding protein of the Sla2/Huntingtin interacting protein 1 family is a novel component of clathrin-coated pits and vesicles
    • Engqvist-Goldstein, A. E. Y., Kessels, M. M., Chopra, V. S., Hayden, M. R. and Drubin, D. G. (1999). An actin-binding protein of the Sla2/Huntingtin interacting protein 1 family is a novel component of clathrin-coated pits and vesicles. J. Cell Biol. 147, 1503-1518.
    • (1999) J. Cell Biol. , vol.147 , pp. 1503-1518
    • Engqvist-Goldstein, A.E.Y.1    Kessels, M.M.2    Chopra, V.S.3    Hayden, M.R.4    Drubin, D.G.5
  • 19
    • 2342432240 scopus 로고    scopus 로고
    • Cdc42 -the centre of polarity
    • Etienne-Manneville, S. (2004). Cdc42 -the centre of polarity. J. Cell Sci. 117, 1291- 1300.
    • (2004) J. Cell Sci. , vol.117
    • Etienne-Manneville, S.1
  • 20
    • 0035839529 scopus 로고    scopus 로고
    • The yeast Pma1 proton pump: a model for understanding the biogenesis of plasma membrane proteins
    • Ferreira, T., Mason, A. B. and Slayman, C. W. (2001). The yeast Pma1 proton pump: a model for understanding the biogenesis of plasma membrane proteins. J. Biol. Chem. 276, 29613-29616.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29613-29616
    • Ferreira, T.1    Mason, A.B.2    Slayman, C.W.3
  • 21
    • 33846177595 scopus 로고    scopus 로고
    • Endocytic recycling in yeast is regulated by putative phospholipid translocases and the Ypt31p/32p-Rcy1p pathway
    • Furuta, N., Fujimura-Kamada, K., Saito, K., Yamamoto, T. and Tanaka, K. (2007). Endocytic recycling in yeast is regulated by putative phospholipid translocases and the Ypt31p/32p-Rcy1p pathway. Mol. Biol. Cell 18, 295-312.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 295-312
    • Furuta, N.1    Fujimura-Kamada, K.2    Saito, K.3    Yamamoto, T.4    Tanaka, K.5
  • 23
    • 0035175540 scopus 로고    scopus 로고
    • Control of pseudohyphae formation in Saccharomyces cerevisiae
    • Gancedo, J. M. (2001). Control of pseudohyphae formation in Saccharomyces cerevisiae. FEMS Microbiol. Rev. 25, 107-123.
    • (2001) FEMS Microbiol. Rev. , vol.25 , pp. 107-123
    • Gancedo, J.M.1
  • 26
    • 0033558093 scopus 로고    scopus 로고
    • The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis
    • Guo, W., Roth, D., Walch-Solimena, C. and Novick, P. (1999). The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis. EMBO J. 18, 1071-1080.
    • (1999) EMBO J. , vol.18 , pp. 1071-1080
    • Guo, W.1    Roth, D.2    Walch-Solimena, C.3    Novick, P.4
  • 27
    • 0028787438 scopus 로고
    • Parallel secretory pathways to the cell surface in yeast
    • Harsay, E. and Bretscher, A. (1995). Parallel secretory pathways to the cell surface in yeast. J. Cell Biol. 131, 297-310.
    • (1995) J. Cell Biol. , vol.131 , pp. 297-310
    • Harsay, E.1    Bretscher, A.2
  • 28
    • 0026044409 scopus 로고
    • Catalysis of guanine nucleotide exchange on the CDC42Hs protein by the dbl oncogene product
    • Hart, M. J., Eva, A., Evans, T., Aaronson, S. A. and Cerione, R. A. (1991). Catalysis of guanine nucleotide exchange on the CDC42Hs protein by the dbl oncogene product. Nature 354, 311-314.
    • (1991) Nature , vol.354 , pp. 311-314
    • Hart, M.J.1    Eva, A.2    Evans, T.3    Aaronson, S.A.4    Cerione, R.A.5
  • 29
    • 33947270800 scopus 로고    scopus 로고
    • Exo70p mediates the secretion of specific exocytic vesicles at early stages of the cell cycle for polarized cell growth
    • He, B., Xi, F. G., Zhang, J., TerBush, D., Zhang, X. Y. and Guo, W. (2007). Exo70p mediates the secretion of specific exocytic vesicles at early stages of the cell cycle for polarized cell growth. J. Cell Biol. 176, 771-777.
    • (2007) J. Cell Biol. , vol.176 , pp. 771-777
    • He, B.1    Xi, F.G.2    Zhang, J.3    TerBush, D.4    Zhang, X.Y.5    Guo, W.6
  • 31
    • 0036015164 scopus 로고    scopus 로고
    • Phosphoinositide-binding domains: Functional units for temporal and spatial regulation of intracellular signalling
    • Itoh, T. and Takenawa, T. (2002). Phosphoinositide-binding domains: Functional units for temporal and spatial regulation of intracellular signalling. Cell. Signal. 14, 733- 743.
    • (2002) Cell. Signal. , vol.14 , pp. 733-743
    • Itoh, T.1    Takenawa, T.2
  • 32
    • 27944479854 scopus 로고    scopus 로고
    • Rho GTPases: biochemistry and biology
    • Jaffe, A. B. and Hall, A. (2005). Rho GTPases: biochemistry and biology. Annu. Rev. Cell Dev. Biol. 21, 247-269.
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 247-269
    • Jaffe, A.B.1    Hall, A.2
  • 33
    • 0033007293 scopus 로고    scopus 로고
    • Cdc42: An essential Rho-type GTPase controlling eukaryotic cell polarity
    • Johnson, D. I. (1999). Cdc42: An essential Rho-type GTPase controlling eukaryotic cell polarity. Microbiol. Mol. Biol. Rev. 63, 54-105.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 54-105
    • Johnson, D.I.1
  • 34
    • 0025363198 scopus 로고
    • Molecular characterization of CDC42 a Saccharomyces cerevisiae gene involved in the development of cell polarity
    • Johnson, D. I. and Pringle, J. R. (1990). Molecular characterization of CDC42, a Saccharomyces cerevisiae gene involved in the development of cell polarity. J. Cell Biol. 111, 143-152.
    • (1990) J. Cell Biol. , vol.111 , pp. 143-152
    • Johnson, D.I.1    Pringle, J.R.2
  • 35
    • 77957769733 scopus 로고    scopus 로고
    • Spitzenkorper, exocyst, and polarisome components in Candida albicans hyphae show different patterns of localization and have distinct dynamic properties
    • Jones, L. A. and Sudbery, P. E. (2010). Spitzenkorper, exocyst, and polarisome components in Candida albicans hyphae show different patterns of localization and have distinct dynamic properties. Eukaryot. Cell 9, 1455-1465.
    • (2010) Eukaryot. Cell , vol.9 , pp. 1455-1465
    • Jones, L.A.1    Sudbery, P.E.2
  • 36
    • 9444257597 scopus 로고    scopus 로고
    • Septin ring assembly requires concerted action of polarisome components, a PAK kinase Cla4p, and the actin cytoskeleton in Saccharomyces cerevisiae
    • Kadota, J., Yamamoto, T., Yoshiuchi, S., Bi, E. F. and Tanaka, K. (2004). Septin ring assembly requires concerted action of polarisome components, a PAK kinase Cla4p, and the actin cytoskeleton in Saccharomyces cerevisiae. Mol. Biol. Cell 15, 5329- 5345.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5329-5345
    • Kadota, J.1    Yamamoto, T.2    Yoshiuchi, S.3    Bi, E.F.4    Tanaka, K.5
  • 37
    • 0026019902 scopus 로고
    • Cellular morphogenesis in the Saccharomyces cerevisiae cell cycle: localization of the CDC3 gene product and the timing of events at the budding site
    • Kim, H. B., Haarer, B. K. and Pringle, J. R. (1991). Cellular morphogenesis in the Saccharomyces cerevisiae cell cycle: localization of the CDC3 gene product and the timing of events at the budding site. J. Cell Biol. 112, 535-544.
    • (1991) J. Cell Biol. , vol.112 , pp. 535-544
    • Kim, H.B.1    Haarer, B.K.2    Pringle, J.R.3
  • 38
    • 35649010000 scopus 로고    scopus 로고
    • Phosphorylation of Bem2p and Bem3p may contribute to local activation of Cdc42p at bud emergence
    • Knaus, M., Pelli-Gulli, M. P., van Drogen, F., Springer, S., Jaquenoud, M. and Peter, M. (2007). Phosphorylation of Bem2p and Bem3p may contribute to local activation of Cdc42p at bud emergence. EMBO J. 26, 4501-4513.
    • (2007) EMBO J. , vol.26 , pp. 4501-4513
    • Knaus, M.1    Pelli-Gulli, M.P.2    van Drogen, F.3    Springer, S.4    Jaquenoud, M.5    Peter, M.6
  • 39
    • 59349119905 scopus 로고    scopus 로고
    • Growth-speed-correlated localization of exocyst and polarisome components in growth zones of Ashbya gossypii hyphal tips
    • Köhli, M., Galati, V., Boudier, K., Roberson, R. W. and Philippsen, P. (2008). Growth-speed-correlated localization of exocyst and polarisome components in growth zones of Ashbya gossypii hyphal tips. J. Cell Sci. 121, 3878-3889.
    • (2008) J. Cell Sci. , vol.121 , pp. 3878-3889
    • Köhli, M.1    Galati, V.2    Boudier, K.3    Roberson, R.W.4    Philippsen, P.5
  • 40
    • 32344443827 scopus 로고    scopus 로고
    • Interactions of myosin vb with rab11 family members and cargoes traversing the plasma membrane recycling system
    • Lapierre, L. A. and Goldenring, J. R. (2005). Interactions of myosin vb with rab11 family members and cargoes traversing the plasma membrane recycling system. Methods Enzymol. 403, 715-723.
    • (2005) Methods Enzymol. , vol.403 , pp. 715-723
    • Lapierre, L.A.1    Goldenring, J.R.2
  • 41
    • 0034663568 scopus 로고    scopus 로고
    • Signal-dependent membrane targeting by pleckstrin homology (PH) domains
    • Lemmon, M. A. and Ferguson, K. M. (2000). Signal-dependent membrane targeting by pleckstrin homology (PH) domains. Biochem. J. 350, 1-18.
    • (2000) Biochem. J. , vol.350 , pp. 1-18
    • Lemmon, M.A.1    Ferguson, K.M.2
  • 44
    • 0033957667 scopus 로고    scopus 로고
    • Characterization of alcoholinduced filamentous growth in Saccharomyces cerevisiae
    • Lorenz, M. C., Cutler, N. S. and Heitman, J. (2000). Characterization of alcoholinduced filamentous growth in Saccharomyces cerevisiae. Mol. Biol. Cell 11, 183- 199.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 183-199
    • Lorenz, M.C.1    Cutler, N.S.2    Heitman, J.3
  • 45
    • 0033999819 scopus 로고    scopus 로고
    • An endosome-to-plasma membrane pathway involved in trafficking of a mutant plasma membrane ATPase in yeast
    • Luo, W. and Chang, A. (2000). An endosome-to-plasma membrane pathway involved in trafficking of a mutant plasma membrane ATPase in yeast. Mol. Biol. Cell 11, 579- 592.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 579-592
    • Luo, W.1    Chang, A.2
  • 46
    • 34147175165 scopus 로고    scopus 로고
    • Endocytosis optimizes the dynamic localization of membrane proteins that regulate cortical polarity
    • Marco, E., Wedlich-Soldner, R., Li, R., Altschuler, S. J. and Wu, L. F. (2007). Endocytosis optimizes the dynamic localization of membrane proteins that regulate cortical polarity. Cell 129, 411-422.
    • (2007) Cell , vol.129 , pp. 411-422
    • Marco, E.1    Wedlich-Soldner, R.2    Li, R.3    Altschuler, S.J.4    Wu, L.F.5
  • 49
    • 0030930123 scopus 로고    scopus 로고
    • Yeast actin cytoskeleton mutants accumulate a new class of Golgi-derived secretary vesicle
    • Mulholland, J., Wesp, A., Riezman, H. and Botstein, D. (1997). Yeast actin cytoskeleton mutants accumulate a new class of Golgi-derived secretary 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
  • 51
    • 77955319474 scopus 로고    scopus 로고
    • Membrane organization and dynamics in cell polarity
    • Orlando, K. and Guo, W. (2009). Membrane organization and dynamics in cell polarity. Cold Spring Harb. Perspect. Biol. 1, a001321.
    • (2009) Cold Spring Harb. Perspect. Biol. , vol.1
    • Orlando, K.1    Guo, W.2
  • 52
    • 79952352917 scopus 로고    scopus 로고
    • Exo-endocytic trafficking and the septin-based diffusion barrier are required for the maintenance of Cdc42p polarization during budding yeast asymmetric growth
    • Orlando, K., Sun, X. L., Zhang, J. A., Lu, T., Yokomizo, L., Wang, P. Y. and Guo, W. (2011). Exo-endocytic trafficking and the septin-based diffusion barrier are required for the maintenance of Cdc42p polarization during budding yeast asymmetric growth. Mol. Biol. Cell 22, 624-633.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 624-633
    • Orlando, K.1    Sun, X.L.2    Zhang, J.A.3    Lu, T.4    Yokomizo, L.5    Wang, P.Y.6    Guo, W.7
  • 53
    • 78650719288 scopus 로고    scopus 로고
    • Cdc42 localization and cell polarity depend on membrane traffic
    • Osmani, N., Peglion, F., Chavrier, P. and Etienne-Manneville, S. (2010). Cdc42 localization and cell polarity depend on membrane traffic. J. Cell Biol. 191, 1261- 1269.
    • (2010) J. Cell Biol. , vol.191 , pp. 1261-1269
    • Osmani, N.1    Peglion, F.2    Chavrier, P.3    Etienne-Manneville, S.4
  • 54
    • 33947398366 scopus 로고    scopus 로고
    • Central roles of small GTPases in the development of cell polarity in yeast and beyond
    • Park, H. O. and Bi, E. F. (2007). Central roles of small GTPases in the development of cell polarity in yeast and beyond. Microbiol. Mol. Biol. Rev. 71, 48-96.
    • (2007) Microbiol. Mol. Biol. Rev. , vol.71 , pp. 48-96
    • Park, H.O.1    Bi, E.F.2
  • 55
    • 77949519353 scopus 로고    scopus 로고
    • Actin-binding proteins implicated in the formation of the punctate actin foci stimulated by the self-incompatibility response in Papaver
    • Poulter, N. S., Staiger, C. J., Rappoport, J. Z. and Franklin-Tong, V. E. (2010). Actin-binding proteins implicated in the formation of the punctate actin foci stimulated by the self-incompatibility response in Papaver. Plant Physiol. 152, 1274- 1283.
    • (2010) Plant Physiol. , vol.152 , pp. 1274-1283
    • Poulter, N.S.1    Staiger, C.J.2    Rappoport, J.Z.3    Franklin-Tong, V.E.4
  • 56
    • 1542395155 scopus 로고    scopus 로고
    • Rabs, Rips, FIPs, and endocytic membrane traffic
    • Prekeris, R. (2003). Rabs, Rips, FIPs, and endocytic membrane traffic. ScientificWorldJournal 3, 870-880.
    • (2003) ScientificWorldJournal , vol.3 , pp. 870-880
    • Prekeris, R.1
  • 59
    • 79952853575 scopus 로고    scopus 로고
    • Yeast homologues of lethal giant larvae and type V myosin cooperate in the regulation of Rab-dependent vesicle clustering and polarized exocytosis
    • Rossi, G. and Brennwald, P. (2011). Yeast homologues of lethal giant larvae and type V myosin cooperate in the regulation of Rab-dependent vesicle clustering and polarized exocytosis. Mol. Biol. Cell 22, 842-857.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 842-857
    • Rossi, G.1    Brennwald, P.2
  • 60
    • 0031820277 scopus 로고    scopus 로고
    • Dominant negative alleles of SEC10 reveal distinct domains involved in secretion and morphogenesis in yeast
    • Roth, D., Guo, W. and Novick, P. (1998). Dominant negative alleles of SEC10 reveal distinct domains involved in secretion and morphogenesis in yeast. Mol. Biol. Cell 9, 1725-1739.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1725-1739
    • Roth, D.1    Guo, W.2    Novick, P.3
  • 62
    • 0024459866 scopus 로고
    • The Sec15 protein responds to the function of the GTP binding protein, Sec4, to control vesicular traffic in yeast
    • Salminen, A. and Novick, P. J. (1989). The Sec15 protein responds to the function of the GTP binding protein, Sec4, to control vesicular traffic in yeast. J. Cell Biol. 109, 1023-1036.
    • (1989) J. Cell Biol. , vol.109 , pp. 1023-1036
    • Salminen, A.1    Novick, P.J.2
  • 63
    • 0032127912 scopus 로고    scopus 로고
    • GTPase-activating proteins: helping hands to complement an active site
    • Scheffzek, K., Ahmadian, M. R. and Wittinghofer, A. (1998). GTPase-activating proteins: helping hands to complement an active site. Trends Biochem. Sci. 23, 257- 262.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 257-262
    • Scheffzek, K.1    Ahmadian, M.R.2    Wittinghofer, A.3
  • 64
    • 70450250211 scopus 로고    scopus 로고
    • Coats of endosomal protein sorting: retromer and ESCRT
    • Schellmann, S. and Pimpl, P. (2009). Coats of endosomal protein sorting: retromer and ESCRT. Curr. Opin. Plant Biol. 12, 670-676.
    • (2009) Curr. Opin. Plant Biol. , vol.12 , pp. 670-676
    • Schellmann, S.1    Pimpl, P.2
  • 65
    • 75749097390 scopus 로고    scopus 로고
    • ImageJ, a useful tool for biological image processing and analysis
    • Sheffield, J. B. (2007). ImageJ, a useful tool for biological image processing and analysis. Microsc. Microanal. 13, 200-201.
    • (2007) Microsc. Microanal. , vol.13 , pp. 200-201
    • Sheffield, J.B.1
  • 66
    • 0034896910 scopus 로고    scopus 로고
    • PX domains: attracted by phosphoinositides
    • Simonsen, A. and Stenmark, H. (2001). PX domains: attracted by phosphoinositides. Nat. Cell Biol. 3, E179-E182.
    • (2001) Nat. Cell Biol. , vol.3
    • Simonsen, A.1    Stenmark, H.2
  • 67
    • 71649099053 scopus 로고    scopus 로고
    • Dual modes of cdc42 recycling fine-tune polarized morphogenesis
    • Slaughter, B. D., Das, A., Schwartz, J. W., Rubinstein, B. and Li, R. (2009). Dual modes of cdc42 recycling fine-tune polarized morphogenesis. Dev. Cell 17, 823-835.
    • (2009) Dev. Cell , vol.17 , pp. 823-835
    • Slaughter, B.D.1    Das, A.2    Schwartz, J.W.3    Rubinstein, B.4    Li, R.5
  • 69
    • 33947258955 scopus 로고    scopus 로고
    • Lipid requirements for endocytosis in yeast
    • Souza, C. M. and Pichler, H. (2007). Lipid requirements for endocytosis in yeast. Biochim. Biophys. Acta 1771, 442-454.
    • (2007) Biochim. Biophys. Acta , vol.1771 , pp. 442-454
    • Souza, C.M.1    Pichler, H.2
  • 70
    • 16244404272 scopus 로고    scopus 로고
    • The phosphoinositide phosphatase Sjl2 is recruited to cortical actin patches in the control of vesicle formation and fission during endocytosis
    • Stefan, C. J., Padilla, S. M., Audhya, A. and Emr, S. D. (2005). The phosphoinositide phosphatase Sjl2 is recruited to cortical actin patches in the control of vesicle formation and fission during endocytosis. Mol. Cel. Biol. 25, 2910-2923.
    • (2005) Mol. Cel. Biol. , vol.25 , pp. 2910-2923
    • Stefan, C.J.1    Padilla, S.M.2    Audhya, A.3    Emr, S.D.4
  • 71
    • 33947644066 scopus 로고    scopus 로고
    • Hyphal growth: a tale of motors, lipids, and the Spitzenkörper
    • Steinberg, G. (2007). Hyphal growth: a tale of motors, lipids, and the Spitzenkörper. Eukaryot. Cell 6, 351-360.
    • (2007) Eukaryot. Cell , vol.6 , pp. 351-360
    • Steinberg, G.1
  • 72
    • 80052965456 scopus 로고    scopus 로고
    • Growth of Candida albicans hyphae
    • Sudbery, P. E. (2011). Growth of Candida albicans hyphae. Nat. Rev. Microbiol. 9, 737- 748.
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 737-748
    • Sudbery, P.E.1
  • 73
    • 34247526437 scopus 로고    scopus 로고
    • PtdIns(4,5)P2 turnover is required for multiple stages during clathrin- and actindependent endocytic internalization
    • Sun, Y. D., Carroll, S., Kaksonen, M., Toshima, J. Y. and Drubin, D. G. (2007). PtdIns(4,5)P2 turnover is required for multiple stages during clathrin- and actindependent endocytic internalization. J. Cell Biol. 177, 355-367.
    • (2007) J. Cell Biol. , vol.177 , pp. 355-367
    • Sun, Y.D.1    Carroll, S.2    Kaksonen, M.3    Toshima, J.Y.4    Drubin, D.G.5
  • 75
    • 37049012678 scopus 로고    scopus 로고
    • Identification of novel membrane-binding domains in multiple yeast Cdc42 effectors
    • Takahashi, S. and Pryciak, P. M. (2007). Identification of novel membrane-binding domains in multiple yeast Cdc42 effectors. Mol. Biol. Cell 18, 4945-4956.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 4945-4956
    • Takahashi, S.1    Pryciak, P.M.2
  • 76
    • 0035980759 scopus 로고    scopus 로고
    • Phosphoinositides, key molecules for regulation of actin cytoskeletal organization and membrane traffic from the plasma membrane
    • Takenawa, T. and Itoh, T. (2001). Phosphoinositides, key molecules for regulation of actin cytoskeletal organization and membrane traffic from the plasma membrane. Biochim. Biophys. Acta 1533, 190-206.
    • (2001) Biochim. Biophys. Acta , vol.1533 , pp. 190-206
    • Takenawa, T.1    Itoh, T.2
  • 77
    • 34247168575 scopus 로고    scopus 로고
    • Vps4 regulates a subset of protein interactions at the multivesicular endosome
    • Vajjhala, P. R., Catchpoole, E., Nguyen, C. H., Kistler, C. and Munn, A. L. (2007). Vps4 regulates a subset of protein interactions at the multivesicular endosome. FEBS J. 274, 1894-1907.
    • (2007) FEBS J. , vol.274 , pp. 1894-1907
    • Vajjhala, P.R.1    Catchpoole, E.2    Nguyen, C.H.3    Kistler, C.4    Munn, A.L.5
  • 78
    • 33745179370 scopus 로고    scopus 로고
    • The Spitzenkörper: a molecular perspective
    • Virag, A. and Harris, S. D. (2006). The Spitzenkörper: a molecular perspective. Mycol. Res. 110, 4-13.
    • (2006) Mycol. Res. , vol.110 , pp. 4-13
    • Virag, A.1    Harris, S.D.2
  • 79
    • 0026639464 scopus 로고
    • Hydrolysis of GTP by Sec4 protein plays an important role in vesicular transport and is stimulated by a GTPase-activating protein in Saccharomyces cerevisiae
    • Walworth, N. C., Brennwald, P., Kabcenell, A. K., Garrett, M. and Novick, P. (1992). Hydrolysis of GTP by Sec4 protein plays an important role in vesicular transport and is stimulated by a GTPase-activating protein in Saccharomyces cerevisiae. Mol. Cell. Biol. 12, 2017-2028.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2017-2028
    • Walworth, N.C.1    Brennwald, P.2    Kabcenell, A.K.3    Garrett, M.4    Novick, P.5
  • 80
    • 0343134529 scopus 로고    scopus 로고
    • A putative endosomal t-SNARE links exo- and endocytosis in the phytopathogenic fungus Ustilago maydis
    • Wedlich-Söldner, R., Bölker, M., Kahmann, R. and Steinberg, G. (2000). A putative endosomal t-SNARE links exo- and endocytosis in the phytopathogenic fungus Ustilago maydis. EMBO J. 19, 1974-1986.
    • (2000) EMBO J. , vol.19 , pp. 1974-1986
    • Wedlich-Söldner, R.1    Bölker, M.2    Kahmann, R.3    Steinberg, G.4
  • 81
    • 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
  • 82
    • 0034678365 scopus 로고    scopus 로고
    • The F-box protein Rcy1p is involved in endocytic membrane traffic and recycling out of an early endosome in Saccharomyces cerevisiae
    • Wiederkehr, A., Avaro, S., Prescianotto-Baschong, C., Haguenauer-Tsapis, R. and Riezman, H. (2000). The F-box protein Rcy1p is involved in endocytic membrane traffic and recycling out of an early endosome in Saccharomyces cerevisiae. J. Cell Biol. 149, 397-410.
    • (2000) J. Cell Biol. , vol.149 , pp. 397-410
    • Wiederkehr, A.1    Avaro, S.2    Prescianotto-Baschong, C.3    Haguenauer-Tsapis, R.4    Riezman, H.5
  • 83
    • 0033019161 scopus 로고    scopus 로고
    • Functional implications of genetic interactions between genes encoding small GTPases involved in vesicular transport in yeast
    • Yoo, J. S., Grabowski, R., Xing, L., Trepte, H. H., Schmitt, H. D. and Gallwitz, D. (1999). Functional implications of genetic interactions between genes encoding small GTPases involved in vesicular transport in yeast. Mol. Gen. Genet. 261, 80-91.
    • (1999) Mol. Gen. Genet. , vol.261 , pp. 80-91
    • Yoo, J.S.1    Grabowski, R.2    Xing, L.3    Trepte, H.H.4    Schmitt, H.D.5    Gallwitz, D.6
  • 84
    • 0034994132 scopus 로고    scopus 로고
    • End13p/Vps4p is required for efficient transport from early to late endosomes in Saccharomyces cerevisiae
    • Zahn, R., Stevenson, B. J., Schröder-Köhne, S., Zanolari, B., Riezman, H. and Munn, A. L. (2001). End13p/Vps4p is required for efficient transport from early to late endosomes in Saccharomyces cerevisiae. J. Cell Sci. 114, 1935-1947.
    • (2001) J. Cell Sci. , vol.114 , pp. 1935-1947
    • Zahn, R.1    Stevenson, B.J.2    Schröder-Köhne, S.3    Zanolari, B.4    Riezman, H.5    Munn, A.L.6
  • 85
    • 14844310335 scopus 로고    scopus 로고
    • Cyclical regulation of the exocyst and cell polarity determinants for polarized cell growth
    • Zajac, A., Sun, X. L., Zhang, J. and Guo, W. (2005). Cyclical regulation of the exocyst and cell polarity determinants for polarized cell growth. Mol. Biol. Cell 16, 1500- 1512.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1500-1512
    • Zajac, A.1    Sun, X.L.2    Zhang, J.3    Guo, W.4
  • 86
    • 79953155321 scopus 로고    scopus 로고
    • Transport to the plasma membrane is regulated differently early and late in the cell cycle in Saccharomyces cerevisiae
    • Zanolari, B., Rockenbauch, U., Trautwein, M., Clay, L., Barral, Y. and Spang, A. (2011). Transport to the plasma membrane is regulated differently early and late in the cell cycle in Saccharomyces cerevisiae. J. Cell Sci. 124, 1055-1066.
    • (2011) J. Cell Sci. , vol.124 , pp. 1055-1066
    • Zanolari, B.1    Rockenbauch, U.2    Trautwein, M.3    Clay, L.4    Barral, Y.5    Spang, A.6
  • 87
    • 5644261225 scopus 로고    scopus 로고
    • Sec15 is an effector for the Rab11 GTPase in mammalian cells
    • Zhang, X. M., Ellis, S., Sriratana, A., Mitchell, C. A. and Rowe, T. (2004). Sec15 is an effector for the Rab11 GTPase in mammalian cells. J. Biol. Chem. 279, 43027- 43034.
    • (2004) J. Biol. Chem. , vol.279 , pp. 43027-43034
    • Zhang, X.M.1    Ellis, S.2    Sriratana, A.3    Mitchell, C.A.4    Rowe, T.5
  • 88
    • 22944450057 scopus 로고    scopus 로고
    • Lethal giant larvae proteins interact with the exocyst complex and are involved in polarized exocytosis
    • Zhang, X. Y., Wang, P. Y., Gangar, A., Zhang, J., Brennwald, P., TerBush, D. and Guo, W. (2005). Lethal giant larvae proteins interact with the exocyst complex and are involved in polarized exocytosis. J. Cell Biol. 170, 273-283.
    • (2005) J. Cell Biol. , vol.170 , pp. 273-283
    • Zhang, X.Y.1    Wang, P.Y.2    Gangar, A.3    Zhang, J.4    Brennwald, P.5    TerBush, D.6    Guo, W.7


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