메뉴 건너뛰기




Volumn 6, Issue 10, 2007, Pages 1814-1823

Regulation of phosphoinositide levels by the phospholipid transfer protein Sec14p controls Cdc42p/p21-activated kinase-mediated cell cycle progression at cytokinesis

Author keywords

[No Author keywords available]

Indexed keywords

KES1 PROTEIN, S CEREVISIAE; MEMBRANE PROTEIN; PHOSPHATIDYLINOSITOL; PHOSPHOLIPID TRANSFER PROTEIN; PROTEIN CDC42; SACCHAROMYCES CEREVISIAE PROTEIN; SEC14 PROTEIN, S CEREVISIAE; UNCLASSIFIED DRUG;

EID: 35348860313     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00087-07     Document Type: Article
Times cited : (10)

References (72)
  • 1
    • 0035969248 scopus 로고    scopus 로고
    • Yeast Cdc42 functions at a late step in exocytosis, specifically during polarized growth of the emerging bud
    • Adamo, J. E., J. J. Moskow, A. S. Gladfelter, D. Viterbo, D. J. Lew, and P. J. Brennwald. 2001. Yeast Cdc42 functions at a late step in exocytosis, specifically during polarized growth of the emerging bud. J. Cell Biol. 155:581-592.
    • (2001) J. Cell Biol , vol.155 , pp. 581-592
    • Adamo, J.E.1    Moskow, J.J.2    Gladfelter, A.S.3    Viterbo, D.4    Lew, D.J.5    Brennwald, P.J.6
  • 2
    • 0033602422 scopus 로고    scopus 로고
    • Sec14p-like domains in NF1 and Dbl-like proteins indicate lipid regulation of Ras and Rho signaling
    • Aravind, L., A. F. Neuwald, and C. P. Ponting. 1999. Sec14p-like domains in NF1 and Dbl-like proteins indicate lipid regulation of Ras and Rho signaling. Curr. Biol. 9:R195-R197.
    • (1999) Curr. Biol , vol.9
    • Aravind, L.1    Neuwald, A.F.2    Ponting, C.P.3
  • 3
    • 0025094319 scopus 로고
    • An essential role for a phospholipid transfer protein in yeast Golgi function
    • Bankaitis, V. A., J. R. Aitken, A. E. Cleves, and W. Dowhan. 1990. An essential role for a phospholipid transfer protein in yeast Golgi function. Nature 347:561-562.
    • (1990) Nature , vol.347 , pp. 561-562
    • Bankaitis, V.A.1    Aitken, J.R.2    Cleves, A.E.3    Dowhan, W.4
  • 4
    • 0024518932 scopus 로고
    • The Saccharomyces cerevisiae SEC14 gene encodes a cytosolic factor that is required for transport of secretory proteins from the yeast Golgi complex
    • Bankaitis, V. A., D. E. Malehorn, S. D. Emr, and R. Greene. 1989. The Saccharomyces cerevisiae SEC14 gene encodes a cytosolic factor that is required for transport of secretory proteins from the yeast Golgi complex. J. Cell Biol. 108:1271-1281.
    • (1989) J. Cell Biol , vol.108 , pp. 1271-1281
    • Bankaitis, V.A.1    Malehorn, D.E.2    Emr, S.D.3    Greene, R.4
  • 5
    • 28444461398 scopus 로고    scopus 로고
    • Phosphatidylinositol transfer protein function in the yeast Saccharomyces cerevisiae
    • Bankaitis, V. A., S. Phillips, L. Yanagisawa, X. Li, S. Routt, and Z. Xie. 2005. Phosphatidylinositol transfer protein function in the yeast Saccharomyces cerevisiae. Adv. Enzyme Regul. 45:155-170.
    • (2005) Adv. Enzyme Regul , vol.45 , pp. 155-170
    • Bankaitis, V.A.1    Phillips, S.2    Yanagisawa, L.3    Li, X.4    Routt, S.5    Xie, Z.6
  • 7
    • 0035831555 scopus 로고    scopus 로고
    • Assembly of scaffold-mediated complexes containing Cdc42p, the exchange factor Cdc24p, and the effector Cla4p required for cell cycle-regulated phosphorylation of Cdc24p
    • Bose, I., J. E. Irazoqui, J. J. Moskow, E. S. Bardes, T. R. Zyla, and D. J. Lew. 2001. Assembly of scaffold-mediated complexes containing Cdc42p, the exchange factor Cdc24p, and the effector Cla4p required for cell cycle-regulated phosphorylation of Cdc24p. J. Biol. Chem. 276:7176-7186.
    • (2001) J. Biol. Chem , vol.276 , pp. 7176-7186
    • Bose, I.1    Irazoqui, J.E.2    Moskow, J.J.3    Bardes, E.S.4    Zyla, T.R.5    Lew, D.J.6
  • 8
    • 0037126066 scopus 로고    scopus 로고
    • Singularity in budding: A role for the evolutionarily conserved small GTPase Cdc42p
    • Caviston, J. P., S. E. Tcheperegine, and E. Bi. 2002. Singularity in budding: a role for the evolutionarily conserved small GTPase Cdc42p. Proc. Natl. Acad. Sci. USA 99:12185-12190.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12185-12190
    • Caviston, J.P.1    Tcheperegine, S.E.2    Bi, E.3
  • 9
    • 0037384105 scopus 로고    scopus 로고
    • Yeasts make their mark
    • Chang, F., and M. Peter. 2003. Yeasts make their mark. Nat. Cell Biol. 5:294-299.
    • (2003) Nat. Cell Biol , vol.5 , pp. 294-299
    • Chang, F.1    Peter, M.2
  • 10
    • 0026073075 scopus 로고
    • Mutations in the CDP-choline pathway for phospholipid biosynthesis bypass the requirement for an essential phospholipid transfer protein
    • Cleves, A. E., T. P. McGee, E. A. Whitters, K. M. Champion, J. R. Aitken, W. Dowhan, M. Goebl, and V. A. Bankaitis. 1991. Mutations in the CDP-choline pathway for phospholipid biosynthesis bypass the requirement for an essential phospholipid transfer protein. Cell 64:789-800.
    • (1991) Cell , vol.64 , pp. 789-800
    • Cleves, A.E.1    McGee, T.P.2    Whitters, E.A.3    Champion, K.M.4    Aitken, J.R.5    Dowhan, W.6    Goebl, M.7    Bankaitis, V.A.8
  • 11
    • 0029091498 scopus 로고
    • Ste20-like protein kinases are required for normal localization of cell growth and for cytokinesis in budding yeast
    • Cvrcková, F., C. De Virgilio, E. Manser, J. R. Pringle, and K. Nasmyth. 1995. Ste20-like protein kinases are required for normal localization of cell growth and for cytokinesis in budding yeast. Genes Dev. 9:1817-1830.
    • (1995) Genes Dev , vol.9 , pp. 1817-1830
    • Cvrcková, F.1    De Virgilio, C.2    Manser, E.3    Pringle, J.R.4    Nasmyth, K.5
  • 13
    • 0942265527 scopus 로고    scopus 로고
    • Mechanisms of guanine nucleotide exchange and Rac-mediated signaling revealed by a dominant negative trio mutant
    • Debreceni, B., Y. Gao, F. Guo, K. Zhu, B. Jia, and Y. Zheng. 2004. Mechanisms of guanine nucleotide exchange and Rac-mediated signaling revealed by a dominant negative trio mutant. J. Biol. Chem. 279:3777-3786.
    • (2004) J. Biol. Chem , vol.279 , pp. 3777-3786
    • Debreceni, B.1    Gao, Y.2    Guo, F.3    Zhu, K.4    Jia, B.5    Zheng, Y.6
  • 16
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • Etienne-Manneville, S., and A. Hall. 2002. Rho GTPases in cell biology. Nature 420:629-635.
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 17
    • 0029803610 scopus 로고    scopus 로고
    • Kes1p shares homology with human oxysterol binding protein and participates in a novel regulatory pathway for yeast Golgi-derived transport vesicle biogenesis
    • Fang, M., B. G. Kearns, A. Gedvilaite, S. Kagiwada, M. Kearns, M. K. Fung, and V. A. Bankaitis. 1996. Kes1p shares homology with human oxysterol binding protein and participates in a novel regulatory pathway for yeast Golgi-derived transport vesicle biogenesis. EMBO J. 15:6447-6459.
    • (1996) EMBO J , vol.15 , pp. 6447-6459
    • Fang, M.1    Kearns, B.G.2    Gedvilaite, A.3    Kagiwada, S.4    Kearns, M.5    Fung, M.K.6    Bankaitis, V.A.7
  • 19
    • 0033635230 scopus 로고    scopus 로고
    • Phosphorylation of the Cdc42 exchange factor Cdc24 by the PAK-like kinase Cla4 may regulate polarized growth in yeast
    • Gulli, M. P., M. Jaquenoud, Y. Shimada, G. Niederhauser, P. Wiget, and M. Peter. 2000. Phosphorylation of the Cdc42 exchange factor Cdc24 by the PAK-like kinase Cla4 may regulate polarized growth in yeast. Mol. Cell 6:1155-1167.
    • (2000) Mol. Cell , vol.6 , pp. 1155-1167
    • Gulli, M.P.1    Jaquenoud, M.2    Shimada, Y.3    Niederhauser, G.4    Wiget, P.5    Peter, M.6
  • 20
    • 0037020237 scopus 로고    scopus 로고
    • The motor protein kinesin-1 links neurofibromin and merlin in a common cellular pathway of neurofibromatosis
    • Hakimi, M. A., D. W. Speicher, and R. Shiekhattar. 2002. The motor protein kinesin-1 links neurofibromin and merlin in a common cellular pathway of neurofibromatosis. J. Biol. Chem. 277:36909-36912.
    • (2002) J. Biol. Chem , vol.277 , pp. 36909-36912
    • Hakimi, M.A.1    Speicher, D.W.2    Shiekhattar, R.3
  • 21
    • 0033607537 scopus 로고    scopus 로고
    • Direct involvement of phosphatidylinositol 4-phosphate in secretion in the yeast Saccharomyces cerevisiae
    • Hama, H., E. A. Schnieders, J. Thorner, J. Y. Takemoto, and D. B. DeWald. 1999. Direct involvement of phosphatidylinositol 4-phosphate in secretion in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 274:34294-34300.
    • (1999) J. Biol. Chem , vol.274 , pp. 34294-34300
    • Hama, H.1    Schnieders, E.A.2    Thorner, J.3    Takemoto, J.Y.4    DeWald, D.B.5
  • 22
    • 0035158785 scopus 로고    scopus 로고
    • Phosphatidylcholine synthesis influences the diacylglycerol homeostasis required for SEC14p-dependent Golgi function and cell growth
    • Henneberry, A. L., T. A. Lagace, N. D. Ridgway, and C. R. McMaster. 2001. Phosphatidylcholine synthesis influences the diacylglycerol homeostasis required for SEC14p-dependent Golgi function and cell growth. Mol. Biol. Cell 12:511-520.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 511-520
    • Henneberry, A.L.1    Lagace, T.A.2    Ridgway, N.D.3    McMaster, C.R.4
  • 23
    • 0036734611 scopus 로고    scopus 로고
    • The major sites of cellular phospholipid synthesis and molecular determinants of fatty acid and lipid head group specificity
    • Henneberry, A. L., M. M. Wright, and C. R. McMaster. 2002. The major sites of cellular phospholipid synthesis and molecular determinants of fatty acid and lipid head group specificity. Mol. Biol. Cell 13:3148-3161.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3148-3161
    • Henneberry, A.L.1    Wright, M.M.2    McMaster, C.R.3
  • 24
    • 0037119971 scopus 로고    scopus 로고
    • A role for cell polarity proteins in mitotic exit
    • Höfken, T., and E. Schiebel. 2002. A role for cell polarity proteins in mitotic exit. EMBO J. 21:4851-4862.
    • (2002) EMBO J , vol.21 , pp. 4851-4862
    • Höfken, T.1    Schiebel, E.2
  • 25
    • 0037113929 scopus 로고    scopus 로고
    • Cessation of growth to prevent cell death due to inhibition of phosphatidylcholine synthesis is impaired at 37 degrees C in Saccharomyces cerevisiae
    • Howe, A. G., V. Zaremberg, and C. R. McMaster. 2002. Cessation of growth to prevent cell death due to inhibition of phosphatidylcholine synthesis is impaired at 37 degrees C in Saccharomyces cerevisiae. J. Biol. Chem. 277:44100-44107.
    • (2002) J. Biol. Chem , vol.277 , pp. 44100-44107
    • Howe, A.G.1    Zaremberg, V.2    McMaster, C.R.3
  • 26
    • 24344455560 scopus 로고    scopus 로고
    • Structural mechanism for sterol sensing and transport by OSBP-related proteins
    • Im, Y. J., S. Raychaudhuri, W. A. Prinz, and J. H. Hurley. 2005. Structural mechanism for sterol sensing and transport by OSBP-related proteins. Nature 437:154-158.
    • (2005) Nature , vol.437 , pp. 154-158
    • Im, Y.J.1    Raychaudhuri, S.2    Prinz, W.A.3    Hurley, J.H.4
  • 27
    • 0344394312 scopus 로고    scopus 로고
    • Scaffold-mediated symmetry breaking by Cdc42p
    • Irazoqui, J. E., A. S. Gladfelter, and D. J. Lew. 2003. Scaffold-mediated symmetry breaking by Cdc42p. Nat. Cell Biol. 5:1062-1070.
    • (2003) Nat. Cell Biol , vol.5 , pp. 1062-1070
    • Irazoqui, J.E.1    Gladfelter, A.S.2    Lew, D.J.3
  • 28
    • 6444227768 scopus 로고    scopus 로고
    • The ER-Golgi v-SNARE Bet1p is required for cross-linking alpha-agglutinin to the cell wall in yeast
    • Kipnis, P., N. Thomas, R. Ovalle, and P. N. Lipke. 2004. The ER-Golgi v-SNARE Bet1p is required for cross-linking alpha-agglutinin to the cell wall in yeast. Microbiology 150:3219-3228.
    • (2004) Microbiology , vol.150 , pp. 3219-3228
    • Kipnis, P.1    Thomas, N.2    Ovalle, R.3    Lipke, P.N.4
  • 29
    • 13244257110 scopus 로고    scopus 로고
    • The Sec14 homology domain regulates the cellular distribution and transforming activity of the Rho-specific guanine nucleotide exchange factor Dbs
    • Kostenko, E. V., G. M. Mahon, L. Cheng, and I. P. Whitehead. 2005. The Sec14 homology domain regulates the cellular distribution and transforming activity of the Rho-specific guanine nucleotide exchange factor Dbs. J. Biol. Chem. 280:2807-2817.
    • (2005) J. Biol. Chem , vol.280 , pp. 2807-2817
    • Kostenko, E.V.1    Mahon, G.M.2    Cheng, L.3    Whitehead, I.P.4
  • 30
    • 33746939368 scopus 로고    scopus 로고
    • Homologues of oxysterol-binding proteins affect Cdc42p- and Rho1p-mediated cell polarization in Saccharomyces cerevisiae
    • Kozminski, K. G., G. Alfaro, S. Dighe, and C. T. Beh. 2006. Homologues of oxysterol-binding proteins affect Cdc42p- and Rho1p-mediated cell polarization in Saccharomyces cerevisiae. Traffic 7:1224-1242.
    • (2006) Traffic , vol.7 , pp. 1224-1242
    • Kozminski, K.G.1    Alfaro, G.2    Dighe, S.3    Beh, C.T.4
  • 31
    • 0036544518 scopus 로고    scopus 로고
    • Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex
    • Li, X., M. P. Rivas, M. Fang, J. Marchena, B. Mehrotra, A. Chaudhary, L. Feng, G. D. Prestwich, and V. A. Bankaitis. 2002. Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex. J. Cell Biol. 157:63-77.
    • (2002) J. Cell Biol , vol.157 , pp. 63-77
    • Li, X.1    Rivas, M.P.2    Fang, M.3    Marchena, J.4    Mehrotra, B.5    Chaudhary, A.6    Feng, L.7    Prestwich, G.D.8    Bankaitis, V.A.9
  • 32
    • 14744294236 scopus 로고    scopus 로고
    • Maintenance of the diacylglycerol level in the Golgi apparatus by the Nir2 protein is critical for Golgi secretory function
    • Litvak, V., N. Dahan, S. Ramachandran, H. Sabanay, and S. Lev. 2005. Maintenance of the diacylglycerol level in the Golgi apparatus by the Nir2 protein is critical for Golgi secretory function. Nat. Cell Biol. 7:225-234.
    • (2005) Nat. Cell Biol , vol.7 , pp. 225-234
    • Litvak, V.1    Dahan, N.2    Ramachandran, S.3    Sabanay, H.4    Lev, S.5
  • 33
    • 0036293678 scopus 로고    scopus 로고
    • Nir2, a human homolog of Drosophila melanogaster retinal degeneration B protein, is essential for cytokinesis
    • Litvak, V., D. Tian, S. Carmen, and S. Lev. 2002. Nir2, a human homolog of Drosophila melanogaster retinal degeneration B protein, is essential for cytokinesis. Mol. Cell. Biol. 22:5064-5075.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 5064-5075
    • Litvak, V.1    Tian, D.2    Carmen, S.3    Lev, S.4
  • 35
    • 0028178386 scopus 로고
    • A phosphatidylinositol/ phosphatidylcholine transfer protein is required for differentiation of the dimorphic yeast Yarrowia lipolytica from the yeast to the mycelial form
    • Lopez, M. C., J. M. Nicaud, H. B. Skinner, C. Vergnolle, J. C. Kader, V. A. Bankaitis, and C. Gaillardin. 1994. A phosphatidylinositol/ phosphatidylcholine transfer protein is required for differentiation of the dimorphic yeast Yarrowia lipolytica from the yeast to the mycelial form. J. Cell Biol. 125:113-127.
    • (1994) J. Cell Biol , vol.125 , pp. 113-127
    • Lopez, M.C.1    Nicaud, J.M.2    Skinner, H.B.3    Vergnolle, C.4    Kader, J.C.5    Bankaitis, V.A.6    Gaillardin, C.7
  • 36
    • 0028077593 scopus 로고
    • Phosphatidylcholine biosynthesis in Saccharomyces cerevisiae. Regulatory insights from studies employing null and chimeric sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases
    • McMaster, C. R., and R. M. Bell. 1994. Phosphatidylcholine biosynthesis in Saccharomyces cerevisiae. Regulatory insights from studies employing null and chimeric sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases. J. Biol. Chem. 269:28010-28016.
    • (1994) J. Biol. Chem , vol.269 , pp. 28010-28016
    • McMaster, C.R.1    Bell, R.M.2
  • 37
    • 0028176089 scopus 로고
    • Phosphatidylcholine biosynthesis via the CDP-choline pathway in Saccharomyces cerevisiae. Multiple mechanisms of regulation
    • McMaster, C. R., and R. M. Bell. 1994. Phosphatidylcholine biosynthesis via the CDP-choline pathway in Saccharomyces cerevisiae. Multiple mechanisms of regulation. J. Biol. Chem. 269:14776-14783.
    • (1994) J. Biol. Chem , vol.269 , pp. 14776-14783
    • McMaster, C.R.1    Bell, R.M.2
  • 38
    • 0030806560 scopus 로고    scopus 로고
    • The phosphatidylinositol transfer protein domain of Drosophila retinal degeneration B protein is essential for photoreceptor cell survival and recovery from light stimulation
    • Milligan, S. C., J. G. Alb, Jr., R. B. Elagina, V. A. Bankaitis, and D. R. Hyde. 1997. The phosphatidylinositol transfer protein domain of Drosophila retinal degeneration B protein is essential for photoreceptor cell survival and recovery from light stimulation. J. Cell Biol. 139:351-363.
    • (1997) J. Cell Biol , vol.139 , pp. 351-363
    • Milligan, S.C.1    Alb Jr., J.G.2    Elagina, R.B.3    Bankaitis, V.A.4    Hyde, D.R.5
  • 39
    • 0345598924 scopus 로고    scopus 로고
    • Crystal structure of human alpha-tocopherol transfer protein bound to its ligand: Implications for ataxia with vitamin E deficiency
    • Min, K. C., R. A. Kovall, and W. A Hendrickson. 2003. Crystal structure of human alpha-tocopherol transfer protein bound to its ligand: implications for ataxia with vitamin E deficiency. Proc. Natl. Acad. Sci. USA 100:14713-14718.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14713-14718
    • Min, K.C.1    Kovall, R.A.2    Hendrickson, W.A.3
  • 40
    • 0029786540 scopus 로고    scopus 로고
    • Cloning of Candida albicans SEC14 gene homologue coding for a putative essential function
    • Monteoliva, L., M. Sanchez, J. Pla, C. Gil, and C. Nombela. 1996. Cloning of Candida albicans SEC14 gene homologue coding for a putative essential function. Yeast 12:1097-1105.
    • (1996) Yeast , vol.12 , pp. 1097-1105
    • Monteoliva, L.1    Sanchez, M.2    Pla, J.3    Gil, C.4    Nombela, C.5
  • 41
    • 14844307033 scopus 로고    scopus 로고
    • Nte1p-mediated deacylation of phosphatidylcholine functionally interacts with Sec14p
    • Murray, J. P., and C. R. McMaster. 2005. Nte1p-mediated deacylation of phosphatidylcholine functionally interacts with Sec14p. J. Biol. Chem. 280:8544-8552.
    • (2005) J. Biol. Chem , vol.280 , pp. 8544-8552
    • Murray, J.P.1    McMaster, C.R.2
  • 43
    • 0034724534 scopus 로고    scopus 로고
    • Trio combines with dock to regulate Pak activity during photoreceptor axon pathfinding in Drosophila
    • Newsome, T. P., S. Schmidt, G. Dietzl, K. Keleman, B. Asling, A. Debant, and B. J. Dickson. 2000. Trio combines with dock to regulate Pak activity during photoreceptor axon pathfinding in Drosophila. Cell 101:283-294.
    • (2000) Cell , vol.101 , pp. 283-294
    • Newsome, T.P.1    Schmidt, S.2    Dietzl, G.3    Keleman, K.4    Asling, B.5    Debant, A.6    Dickson, B.J.7
  • 44
    • 0018930046 scopus 로고
    • Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway
    • Novick, P., C. Field, and R. Schekman. 1980. Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell 21:205-215.
    • (1980) Cell , vol.21 , pp. 205-215
    • Novick, P.1    Field, C.2    Schekman, R.3
  • 45
    • 0030465534 scopus 로고    scopus 로고
    • Functional analysis of the interaction between the small GTP binding protein Cdc42 and the Ste20 protein kinase in yeast
    • Peter, M., A. M. Neiman, H. O. Park, M. van Lohuizen, and I. Herskowitz. 1996. Functional analysis of the interaction between the small GTP binding protein Cdc42 and the Ste20 protein kinase in yeast. EMBO J. 15:7046-7059.
    • (1996) EMBO J , vol.15 , pp. 7046-7059
    • Peter, M.1    Neiman, A.M.2    Park, H.O.3    van Lohuizen, M.4    Herskowitz, I.5
  • 46
    • 0034002965 scopus 로고    scopus 로고
    • Polarization of cell growth in yeast. I. Establishment and maintenance of polarity states
    • Pruyne, D., and A Bretscher. 2000. Polarization of cell growth in yeast. I. Establishment and maintenance of polarity states. J. Cell Sci. 113:365-375.
    • (2000) J. Cell Sci , vol.113 , pp. 365-375
    • Pruyne, D.1    Bretscher, A.2
  • 47
    • 0036615365 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Cdc42p localizes to cellular membranes and clusters at sites of polarized growth
    • Richman, T. J., M. M. Sawyer, and D. I. Johnson. 2002. Saccharomyces cerevisiae Cdc42p localizes to cellular membranes and clusters at sites of polarized growth. Eukaryot. Cell 1:458-468.
    • (2002) Eukaryot. Cell , vol.1 , pp. 458-468
    • Richman, T.J.1    Sawyer, M.M.2    Johnson, D.I.3
  • 48
    • 0032874292 scopus 로고    scopus 로고
    • Pleiotropic alterations in lipid metabolism in yeast sac1 mutants: Relationship to "bypass Sec14p" and inositol auxotrophy
    • Rivas, M. P., B. G. Kearns, Z. Xie, S. Guo, M. C. Sekar, K. Hosaka, S. Kagiwada, J. D. York, and V. A. Bankaitis. 1999. Pleiotropic alterations in lipid metabolism in yeast sac1 mutants: relationship to "bypass Sec14p" and inositol auxotrophy. Mol. Biol. Cell 10:2235-2250.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2235-2250
    • Rivas, M.P.1    Kearns, B.G.2    Xie, Z.3    Guo, S.4    Sekar, M.C.5    Hosaka, K.6    Kagiwada, S.7    York, J.D.8    Bankaitis, V.A.9
  • 49
    • 0033574722 scopus 로고    scopus 로고
    • The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly
    • Rohatgi, R., L. Ma, H. Miki, M. Lopez, T. Kirchhausen, T. Takenawa, and M. W. Kirschner. 1999. The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell 97:221-231.
    • (1999) Cell , vol.97 , pp. 221-231
    • Rohatgi, R.1    Ma, L.2    Miki, H.3    Lopez, M.4    Kirchhausen, T.5    Takenawa, T.6    Kirschner, M.W.7
  • 50
    • 13444252631 scopus 로고    scopus 로고
    • GEF means go: Turning on RHO GTPases with guanine nucleotide-exchange factors
    • Rossman, K. L., C. J. Der, and J. Sondek. 2005. GEF means go: turning on RHO GTPases with guanine nucleotide-exchange factors. Nat. Rev. Mol. Cell Biol. 6:167-180.
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 167-180
    • Rossman, K.L.1    Der, C.J.2    Sondek, J.3
  • 51
    • 0037086652 scopus 로고    scopus 로고
    • A crystallographic view of interactions between Dbs and Cdc42: PH domain-assisted guanine nucleotide exchange
    • Rossman, K. L., D. K. Worthylake, J. T. Snyder, D. P. Siderovski, S. L. Campbell, and J. Sondek. 2002. A crystallographic view of interactions between Dbs and Cdc42: PH domain-assisted guanine nucleotide exchange. EMBO J. 21:1315-1326.
    • (2002) EMBO J , vol.21 , pp. 1315-1326
    • Rossman, K.L.1    Worthylake, D.K.2    Snyder, J.T.3    Siderovski, D.P.4    Campbell, S.L.5    Sondek, J.6
  • 52
    • 2342618157 scopus 로고    scopus 로고
    • Biological functions of phosphatidylinositol transfer proteins
    • Routt, S. M., and V. A. Bankaitis. 2004. Biological functions of phosphatidylinositol transfer proteins. Biochem. Cell Biol. 82:254-262.
    • (2004) Biochem. Cell Biol , vol.82 , pp. 254-262
    • Routt, S.M.1    Bankaitis, V.A.2
  • 53
    • 27744604253 scopus 로고    scopus 로고
    • Nonclassical PITPs activate PLD via the Stt4p PtdIns-4-kinase and modulate function of late stages of exocytosis in vegetative yeast
    • Routt, S. M., M. M. Ryan, K. Tyeryar, K. E. Rizzieri, C. Mousley, O. Roumanie, P. J. Brennwald, and V. A. Bankaitis. 2005. Nonclassical PITPs activate PLD via the Stt4p PtdIns-4-kinase and modulate function of late stages of exocytosis in vegetative yeast. Traffic 6:1157-1172.
    • (2005) Traffic , vol.6 , pp. 1157-1172
    • Routt, S.M.1    Ryan, M.M.2    Tyeryar, K.3    Rizzieri, K.E.4    Mousley, C.5    Roumanie, O.6    Brennwald, P.J.7    Bankaitis, V.A.8
  • 54
    • 2142759571 scopus 로고    scopus 로고
    • 23 genes, 23 years later
    • Schekman, R., and P. Novick. 2004. 23 genes, 23 years later. Cell 116:S13-S15.
    • (2004) Cell , vol.116
    • Schekman, R.1    Novick, P.2
  • 55
    • 0032576758 scopus 로고    scopus 로고
    • Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol- transfer protein
    • Sha, B., S. E. Phillips, V. A. Bankaitis, and M. Luo. 1998. Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol- transfer protein. Nature 391:506-510.
    • (1998) Nature , vol.391 , pp. 506-510
    • Sha, B.1    Phillips, S.E.2    Bankaitis, V.A.3    Luo, M.4
  • 56
    • 0242664602 scopus 로고    scopus 로고
    • Concerted regulation of cell dynamics by BNIP-2 and Cdc42GAP homology/Sec14p-like, proline-rich, and GTPase-activating protein domains of a novel Rho GTPase-activating protein, BPGAP1
    • Shang, X., Y. T. Zhou, and B. C. Low. 2003. Concerted regulation of cell dynamics by BNIP-2 and Cdc42GAP homology/Sec14p-like, proline-rich, and GTPase-activating protein domains of a novel Rho GTPase-activating protein, BPGAP1. J. Biol. Chem. 278:45903-45914.
    • (2003) J. Biol. Chem , vol.278 , pp. 45903-45914
    • Shang, X.1    Zhou, Y.T.2    Low, B.C.3
  • 57
    • 1842472163 scopus 로고    scopus 로고
    • The nucleotide exchange factor Cdc24p may be regulated by auto-inhibition
    • Shimada, Y., P. Wiget, M. P. Gulli, E. Bi, and M. Peter. 2004. The nucleotide exchange factor Cdc24p may be regulated by auto-inhibition. EMBO J. 23:1051-1062.
    • (2004) EMBO J , vol.23 , pp. 1051-1062
    • Shimada, Y.1    Wiget, P.2    Gulli, M.P.3    Bi, E.4    Peter, M.5
  • 58
    • 0032479169 scopus 로고    scopus 로고
    • Sreenivas, A., J. L. Patton-Vogt, V. Bruno, P. Griac, and S. A. Henry. 1998. A role for phospholipase D (Pld1p) in growth, secretion, and regulation of membrane lipid synthesis in yeast. J. Biol. Chem. 273:16635-16638.
    • Sreenivas, A., J. L. Patton-Vogt, V. Bruno, P. Griac, and S. A. Henry. 1998. A role for phospholipase D (Pld1p) in growth, secretion, and regulation of membrane lipid synthesis in yeast. J. Biol. Chem. 273:16635-16638.
  • 60
    • 2442430347 scopus 로고    scopus 로고
    • Separate membrane targeting and anchoring domains function in the localization of the S. cerevisiae Cdc24p guanine nucleotide exchange factor
    • Toenjes, K., D. Simpson, and D. I. Johnson. 2004. Separate membrane targeting and anchoring domains function in the localization of the S. cerevisiae Cdc24p guanine nucleotide exchange factor. Curr. Genet. 45:257-264.
    • (2004) Curr. Genet , vol.45 , pp. 257-264
    • Toenjes, K.1    Simpson, D.2    Johnson, D.I.3
  • 61
    • 2442562704 scopus 로고    scopus 로고
    • Role of the Sec14-like domain of Dbl family exchange factors in the regulation of Rho family GTPases in different subcellular sites
    • Ueda, S., T. Kataoka, and T. Satoh. 2004. Role of the Sec14-like domain of Dbl family exchange factors in the regulation of Rho family GTPases in different subcellular sites. Cell. Signal. 16:899-906.
    • (2004) Cell. Signal , vol.16 , pp. 899-906
    • Ueda, S.1    Kataoka, T.2    Satoh, T.3
  • 62
    • 1442334322 scopus 로고    scopus 로고
    • Septin collar formation in budding yeast requires GTP binding and direct phosphorylation by the PAK, Cla4
    • Versele, M., and J. Thorner. 2004. Septin collar formation in budding yeast requires GTP binding and direct phosphorylation by the PAK, Cla4. J. Cell Biol. 164:701-715.
    • (2004) J. Cell Biol , vol.164 , pp. 701-715
    • Versele, M.1    Thorner, J.2
  • 65
    • 2342430611 scopus 로고    scopus 로고
    • The p21-activated protein kinase-related kinase Cla4 is a coincidence detector of signaling by Cdc42 and phosphatidylinositol 4-phosphate
    • Wild, A. C., J. W. Yu, M. A. Lemmon, and K. J. Blumer. 2004. The p21-activated protein kinase-related kinase Cla4 is a coincidence detector of signaling by Cdc42 and phosphatidylinositol 4-phosphate. J. Biol. Chem. 279:17101-17110.
    • (2004) J. Biol. Chem , vol.279 , pp. 17101-17110
    • Wild, A.C.1    Yu, J.W.2    Lemmon, M.A.3    Blumer, K.J.4
  • 66
    • 24644457550 scopus 로고    scopus 로고
    • Membrane metabolism mediated by Sec14 family members influences Arf GTPase activating protein activity for transport from the trans-Golgi
    • Wong, T. A., G. D. Fairn, P. P. Poon, M. Shmulevitz, C. R. McMaster, R. A. Singer, and G. C. Johnston. 2005. Membrane metabolism mediated by Sec14 family members influences Arf GTPase activating protein activity for transport from the trans-Golgi. Proc. Natl. Acad. Sci. USA 102:12777-12782.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 12777-12782
    • Wong, T.A.1    Fairn, G.D.2    Poon, P.P.3    Shmulevitz, M.4    McMaster, C.R.5    Singer, R.A.6    Johnston, G.C.7
  • 67
    • 0035162567 scopus 로고    scopus 로고
    • Evidence for an intrinsic toxicity of phosphatidylcholine to Sec14p-dependent protein transport from the yeast Golgi complex
    • Xie, Z., M. Fang, and V. A Bankaitis. 2001. Evidence for an intrinsic toxicity of phosphatidylcholine to Sec14p-dependent protein transport from the yeast Golgi complex. Mol. Biol. Cell 12:1117-1129.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1117-1129
    • Xie, Z.1    Fang, M.2    Bankaitis, V.A.3
  • 69
    • 0035947559 scopus 로고    scopus 로고
    • Novel members of the human oxysterol-binding protein family bind phospholipids and regulate vesicle transport
    • Xu, Y., Y. Liu, N. D. Ridgway, and C. R. McMaster. 2001. Novel members of the human oxysterol-binding protein family bind phospholipids and regulate vesicle transport. J. Biol. Chem. 276:18407-18414.
    • (2001) J. Biol. Chem , vol.276 , pp. 18407-18414
    • Xu, Y.1    Liu, Y.2    Ridgway, N.D.3    McMaster, C.R.4
  • 70
    • 27844522310 scopus 로고    scopus 로고
    • Cytotoxicity of an anti-cancer lysophospholipid through selective modification of lipid raft composition
    • Zaremberg, V., C. Gajate, L. M. Cacharro, F. Mollinedo, and C. R. McMaster. 2005. Cytotoxicity of an anti-cancer lysophospholipid through selective modification of lipid raft composition. J. Biol. Chem. 280:38047-38058.
    • (2005) J. Biol. Chem , vol.280 , pp. 38047-38058
    • Zaremberg, V.1    Gajate, C.2    Cacharro, L.M.3    Mollinedo, F.4    McMaster, C.R.5
  • 71
    • 0025847665 scopus 로고
    • Mutational analysis of CDC42Sc, a Saccharomyces cerevisiae gene that encodes a putative GTP-binding protein involved in the control of cell polarity
    • Ziman, M., J. M. O'Brien, L. A. Ouellette, W. R. Church, and D. I. Johnson. 1991. Mutational analysis of CDC42Sc, a Saccharomyces cerevisiae gene that encodes a putative GTP-binding protein involved in the control of cell polarity. Mol. Cell. Biol. 11:3537-3544.
    • (1991) Mol. Cell. Biol , vol.11 , pp. 3537-3544
    • Ziman, M.1    O'Brien, J.M.2    Ouellette, L.A.3    Church, W.R.4    Johnson, D.I.5
  • 72
    • 0027744475 scopus 로고
    • Subcellular localization of Cdc42p, a Saccharomyces cerevisiae GTP-binding protein involved in the control of cell polarity
    • Ziman, M., D. Preuss, J. Mulholland, J. M. O'Brien, D. Botstein, and D. I. Johnson. 1993. Subcellular localization of Cdc42p, a Saccharomyces cerevisiae GTP-binding protein involved in the control of cell polarity. Mol. Biol. Cell 4:1307-1316.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1307-1316
    • Ziman, M.1    Preuss, D.2    Mulholland, J.3    O'Brien, J.M.4    Botstein, D.5    Johnson, D.I.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.