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Volumn 140, Issue 1, 1998, Pages 81-90

Relocalization of phospholipase D activity mediates membrane formation during meiosis

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOLIPASE D;

EID: 0031918590     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.140.1.81     Document Type: Article
Times cited : (123)

References (53)
  • 1
    • 0023899910 scopus 로고
    • Activation of NADPH-dependent Superoxide production in plasma membrane extracts of pig neutrophils by phosphatidic acid
    • Bellavite, P., F. Corso, S. Dusi, M. Grzeskowiakk, V. Bella-Bianca, and F. Rossi. 1988. Activation of NADPH-dependent Superoxide production in plasma membrane extracts of pig neutrophils by phosphatidic acid. J. Biol. Chem. 263:8210-8214.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8210-8214
    • Bellavite, P.1    Corso, F.2    Dusi, S.3    Grzeskowiakk, M.4    Bella-Bianca, V.5    Rossi, F.6
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein-dye binding
    • Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein-dye binding. Anal. Biochem. 76:248-254.
    • (1976) Anal. Biochem. , vol.76 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0002739244 scopus 로고
    • Cytology of the yeast life cycle
    • J.N. Strathern, E.W. Jones, and J.R. Broach, editors. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Byers, B. 1981. Cytology of the yeast life cycle. In The Molecular Biology of the Yeast Saccharomyces. Life Cycle and Inheritance. J.N. Strathern, E.W. Jones, and J.R. Broach, editors. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. 59-96.
    • (1981) The Molecular Biology of the Yeast Saccharomyces. Life Cycle and Inheritance , pp. 59-96
    • Byers, B.1
  • 6
    • 23444431611 scopus 로고
    • Green fluorescent protein as a marker for gene expression
    • Chalfie, M., Y. Tu, G. Euskirchen, W.W. Ward, and D.C. Prasher. 1994. Green fluorescent protein as a marker for gene expression. Science. 263:802-805.
    • (1994) Science , vol.263 , pp. 802-805
    • Chalfie, M.1    Tu, Y.2    Euskirchen, G.3    Ward, W.W.4    Prasher, D.C.5
  • 7
    • 0029791554 scopus 로고    scopus 로고
    • The envelope of vaccinia virus reveals an unusual phospholipid in Golgi complex membranes
    • Cluett, E.B., and C.E. Machamer. 1996. The envelope of vaccinia virus reveals an unusual phospholipid in Golgi complex membranes. J. Cell Sci. 109:2121-2131.
    • (1996) J. Cell Sci. , vol.109 , pp. 2121-2131
    • Cluett, E.B.1    Machamer, C.E.2
  • 8
    • 0031105873 scopus 로고    scopus 로고
    • Phospholipase D2, a PLD1-related isoform with novel regulatory properties and discrete subcellular localization that provokes cytoskeletal reorganization
    • Colley, W.C., T.-C. Sung, R. Roll, J. Jenco, S.M. Hammond, Y. Altshuller, D. Bar-Sagi, A.J. Morris, and M.A. Frohman. 1997. Phospholipase D2, a PLD1-related isoform with novel regulatory properties and discrete subcellular localization that provokes cytoskeletal reorganization. Curr. Biol. 7:191-201.
    • (1997) Curr. Biol. , vol.7 , pp. 191-201
    • Colley, W.C.1    Sung, T.-C.2    Roll, R.3    Jenco, J.4    Hammond, S.M.5    Altshuller, Y.6    Bar-Sagi, D.7    Morris, A.J.8    Frohman, M.A.9
  • 9
    • 0026767452 scopus 로고
    • Activation of phospholipase D by protein kinase C. Evidence for a phosphorylation-independent mechanism
    • Conricode, K.M., K.A. Brewer, and J.H. Exton. 1992. Activation of phospholipase D by protein kinase C. Evidence for a phosphorylation-independent mechanism. J. Biol. Chem. 267:7199-7202.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7199-7202
    • Conricode, K.M.1    Brewer, K.A.2    Exton, J.H.3
  • 10
    • 0029973636 scopus 로고    scopus 로고
    • FACS-optimized mutants of the green fluorescent protein (GFP)
    • Cormack, B.P., R.H. Valdivis, and S. Falkow. 1996. FACS-optimized mutants of the green fluorescent protein (GFP). Gene. 173:33-38.
    • (1996) Gene , vol.173 , pp. 33-38
    • Cormack, B.P.1    Valdivis, R.H.2    Falkow, S.3
  • 12
    • 0030062093 scopus 로고    scopus 로고
    • Characterization of Saccharomyces cerevisiae deficient in expression of phospholipase D
    • Ella, K.M., J.W. Dolan, C. Qi, and K.E. Meier. 1996. Characterization of Saccharomyces cerevisiae deficient in expression of phospholipase D. Biochem. J. 314:15-19.
    • (1996) Biochem. J. , vol.314 , pp. 15-19
    • Ella, K.M.1    Dolan, J.W.2    Qi, C.3    Meier, K.E.4
  • 13
    • 0023727629 scopus 로고
    • A family of versatile centromeric vectors designed for use in the sectoring-shuffle mutagenesis assay in Saccharomyces cerevisiae
    • Elledge, S.J., and R.W. Davis. 1988. A family of versatile centromeric vectors designed for use in the sectoring-shuffle mutagenesis assay in Saccharomyces cerevisiae. Gene. 70:303-312.
    • (1988) Gene , vol.70 , pp. 303-312
    • Elledge, S.J.1    Davis, R.W.2
  • 14
    • 0028296793 scopus 로고
    • Phosphatidylcholine breakdown and signal transduction
    • Exton, J.H. 1994. Phosphatidylcholine breakdown and signal transduction. Biochem. Biophys. Acta. 1212:26-42.
    • (1994) Biochem. Biophys. Acta , vol.1212 , pp. 26-42
    • Exton, J.H.1
  • 15
    • 0030031256 scopus 로고    scopus 로고
    • Identification of a developmentally regulated septin and involvement of the septins in spore formation in Saccharomyces cerevisiae
    • Fares, H., L. Goetsch, and J.R. Pringle. 1996. Identification of a developmentally regulated septin and involvement of the septins in spore formation in Saccharomyces cerevisiae. J. Cell Biol. 132:399-411.
    • (1996) J. Cell Biol. , vol.132 , pp. 399-411
    • Fares, H.1    Goetsch, L.2    Pringle, J.R.3
  • 16
    • 0030219389 scopus 로고    scopus 로고
    • More on target with protein phosphorylation: Conferring specificity by location
    • Faux, M.C., and J.D. Scott. 1996. More on target with protein phosphorylation: conferring specificity by location. Trends Biol. Sci. 4:312-315.
    • (1996) Trends Biol. Sci. , vol.4 , pp. 312-315
    • Faux, M.C.1    Scott, J.D.2
  • 17
    • 0028071624 scopus 로고
    • Mutation of the SPSI-encoded protein kinase of Saccharomyces cerevisiae leads to defects in transcription and morphology during spore formation
    • Friesen, H., R. Lunz, S. Doyle, and J. Segall. 1994. Mutation of the SPSI-encoded protein kinase of Saccharomyces cerevisiae leads to defects in transcription and morphology during spore formation. Genes Dev. 8:2162-2175.
    • (1994) Genes Dev. , vol.8 , pp. 2162-2175
    • Friesen, H.1    Lunz, R.2    Doyle, S.3    Segall, J.4
  • 18
    • 0029857994 scopus 로고    scopus 로고
    • Molecular cloning of a high-affinity receptor for the growth factor-like lipid mediator lysophosphatidic acid from Xenopus oocytes
    • Guo, Z., K. Liliom, D.J. Fischer, I.C. Bathurst, L.D. Tomei, M.C. Kiefer, and G. Tigyi. 1996. Molecular cloning of a high-affinity receptor for the growth factor-like lipid mediator lysophosphatidic acid from Xenopus oocytes. Proc. Natl. Acad. Sci. USA. 93:14367-14372.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14367-14372
    • Guo, Z.1    Liliom, K.2    Fischer, D.J.3    Bathurst, I.C.4    Tomei, L.D.5    Kiefer, M.C.6    Tigyi, G.7
  • 19
    • 0029564902 scopus 로고
    • Cloning of mammalian ARF-activated phosphatidylcholine-specific phospholipase D define a new and highly conserved family of genes
    • Hammond, S.M., Y.M. Altshuller, T.-C. Sung, S.A. Rudge, K. Rose, J. Engebrecht, A.J. Morris, and M.A. Frohman. 1995. Cloning of mammalian ARF-activated phosphatidylcholine-specific phospholipase D define a new and highly conserved family of genes. J. Biol. Chem. 270:29640-29643.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29640-29643
    • Hammond, S.M.1    Altshuller, Y.M.2    Sung, T.-C.3    Rudge, S.A.4    Rose, K.5    Engebrecht, J.6    Morris, A.J.7    Frohman, M.A.8
  • 21
    • 0022781503 scopus 로고
    • Yeast/E. coli shuttle vectors with multiple unique restriction sites
    • Hill, J.E., A.M. Myers, T.J. Koerner, and A. Tzagoloff. 1986. Yeast/E. coli shuttle vectors with multiple unique restriction sites. Yeast. 2:163-167.
    • (1986) Yeast , vol.2 , pp. 163-167
    • Hill, J.E.1    Myers, A.M.2    Koerner, T.J.3    Tzagoloff, A.4
  • 22
    • 0029827247 scopus 로고    scopus 로고
    • 2 levels in human platelets are controlled by translocation of PtdIns 4-P 5-kinase C to the cytoskeleton
    • 2 levels in human platelets are controlled by translocation of PtdIns 4-P 5-kinase C to the cytoskeleton. EMBO (Eur. Mol. Biol. Organ.) J. 15:6516-6524.
    • (1996) EMBO (Eur. Mol. Biol. Organ.) J. , vol.15 , pp. 6516-6524
    • Hinchliffe, K.A.1    Irvine, R.F.2    N. Divecha, N.3
  • 23
    • 0029145505 scopus 로고
    • MSH5, a novel MutS homolog, facilitates meiotic reciprocal recombination between homologs in Saccharomyces cerevisiae but not mismatch repair
    • Hollingsworth, N.M., L. Ponte, and C. Halsey. 1995. MSH5, a novel MutS homolog, facilitates meiotic reciprocal recombination between homologs in Saccharomyces cerevisiae but not mismatch repair. Genes Dev. 9:1728-1739.
    • (1995) Genes Dev. , vol.9 , pp. 1728-1739
    • Hollingsworth, N.M.1    Ponte, L.2    Halsey, C.3
  • 24
    • 0026696154 scopus 로고
    • Commitment to meiosis in Saccharomyces cerevisiae: Involvement of the SPO14 gene
    • Honigberg, S.M., C. Conicella, and R.E. Esposito. 1992. Commitment to meiosis in Saccharomyces cerevisiae: involvement of the SPO14 gene. Genetics. 130:703-716.
    • (1992) Genetics , vol.130 , pp. 703-716
    • Honigberg, S.M.1    Conicella, C.2    Esposito, R.E.3
  • 25
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Y. Fukada, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukada, Y.2    Murata, K.3    Kimura, A.4
  • 26
    • 0016374946 scopus 로고
    • Carbohydrate metabolism during ascospore development in yeast
    • Kane, S., and J. Roth. 1974. Carbohydrate metabolism during ascospore development in yeast. J. Bacteriol. 118:8-14.
    • (1974) J. Bacteriol. , vol.118 , pp. 8-14
    • Kane, S.1    Roth, J.2
  • 28
    • 0029615509 scopus 로고
    • Protein kinase C is regulated in vivo by three functionally distinct phosphorylations
    • Keranen, L.M., E.M. Dutil, and A.C. Newton. 1995. Protein kinase C is regulated in vivo by three functionally distinct phosphorylations. Curr. Biol. 5: 1394-1403.
    • (1995) Curr. Biol. , vol.5 , pp. 1394-1403
    • Keranen, L.M.1    Dutil, E.M.2    Newton, A.C.3
  • 29
    • 0020265993 scopus 로고
    • Rat monoclonal antitubulin antibodies derived by using a new nonsecreting rat cell line
    • Kilmartin, J.V., B. Wright, and C. Milstein. 1982. Rat monoclonal antitubulin antibodies derived by using a new nonsecreting rat cell line. J. Cell Biol. 93: 576-582.
    • (1982) J. Cell Biol. , vol.93 , pp. 576-582
    • Kilmartin, J.V.1    Wright, B.2    Milstein, C.3
  • 30
    • 0025145657 scopus 로고
    • Epidermal growth factor and platelet-derived growth factor promote translocation of phospholipase C-γ from cytosol to membrane
    • Kim, U.H., H.S. Kim, and S.G. Rhee. 1990. Epidermal growth factor and platelet-derived growth factor promote translocation of phospholipase C-γ from cytosol to membrane. FEBS Lett. 270:33-36.
    • (1990) FEBS Lett. , vol.270 , pp. 33-36
    • Kim, U.H.1    Kim, H.S.2    Rhee, S.G.3
  • 31
    • 0027967087 scopus 로고
    • SMK1, a developmentally regulated MAP kinase, is required for spore wall assembly in Saccharomyces cerevisiae
    • Krisak, L., R. Strich, R.S. Winters, J.P. Hall, M.J. Mallory, D. Kreitzer, R.S. Tuan, and E. Winters. 1994. SMK1, a developmentally regulated MAP kinase, is required for spore wall assembly in Saccharomyces cerevisiae. Genes Dev. 10:2151-2161.
    • (1994) Genes Dev. , vol.10 , pp. 2151-2161
    • Krisak, L.1    Strich, R.2    Winters, R.S.3    Hall, J.P.4    Mallory, M.J.5    Kreitzer, D.6    Tuan, R.S.7    Winters, E.8
  • 32
    • 0030013233 scopus 로고    scopus 로고
    • Evidence that phospholipase D mediates ADP ribosylation factor-dependent formation of Golgi coated vesicles
    • Ktistakis, N.T., H.A. Brown, M.G. Waters, P.C. Sternweis, and M.G. Roth. 1996. Evidence that phospholipase D mediates ADP ribosylation factor-dependent formation of Golgi coated vesicles. J. Cell Biol. 134:295-306.
    • (1996) J. Cell Biol. , vol.134 , pp. 295-306
    • Ktistakis, N.T.1    Brown, H.A.2    Waters, M.G.3    Sternweis, P.C.4    Roth, M.G.5
  • 33
    • 0029019442 scopus 로고
    • Signal transduction and membrane traffic: The PITP/phosphoinositide connection
    • Liscovitch, M., and L.C. Cantley. 1995. Signal transduction and membrane traffic: the PITP/phosphoinositide connection. Cell. 81:659-662.
    • (1995) Cell , vol.81 , pp. 659-662
    • Liscovitch, M.1    Cantley, L.C.2
  • 34
    • 0029947711 scopus 로고    scopus 로고
    • Regulation of cAMP-dependent protein kinase of a G-protein-mediated phospholipase C
    • Liu, M., and M. Simon. 1996. Regulation of cAMP-dependent protein kinase of a G-protein-mediated phospholipase C. Nature. 382:83-87.
    • (1996) Nature , vol.382 , pp. 83-87
    • Liu, M.1    Simon, M.2
  • 35
    • 0029131503 scopus 로고
    • Regulation of phospholipase D by protein kinase C in human neutrophils
    • Lopez, I., D.J. Burns, J.D. Lambeth. 1995. Regulation of phospholipase D by protein kinase C in human neutrophils. J. Biol. Chem. 270:19465-19472.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19465-19472
    • Lopez, I.1    Burns, D.J.2    Lambeth, J.D.3
  • 36
    • 0026744154 scopus 로고
    • Phosphatidic acid is a specific activator of phosphatidylinositol-4-phosphate kinase
    • Moritz, A., P.N.D. Graan, W.H. Gispen, and K.W. Wirtz. 1992. Phosphatidic acid is a specific activator of phosphatidylinositol-4-phosphate kinase. J. Biol. Chem. 267:7207-7210.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7207-7210
    • Moritz, A.1    Graan, P.N.D.2    Gispen, W.H.3    Wirtz, K.W.4
  • 38
    • 0031940772 scopus 로고    scopus 로고
    • Prospore membrane formation defines a developmentally regulated branch of the secretory pathway in yeast
    • Neiman, A.M. 1998. Prospore membrane formation defines a developmentally regulated branch of the secretory pathway in yeast. J. Cell Biol. 140:29-37.
    • (1998) J. Cell Biol. , vol.140 , pp. 29-37
    • Neiman, A.M.1
  • 39
    • 0031019157 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae HOC1, a suppressor of pkc1, encodes a putative glycosyltransferase
    • Neiman, A.M., V. Mhaiskar, V. Manus, F. Galibert, and N. Dean. 1997. Saccharomyces cerevisiae HOC1, a suppressor of pkc1, encodes a putative glycosyltransferase. Genetics. 145:637-645.
    • (1997) Genetics , vol.145 , pp. 637-645
    • Neiman, A.M.1    Mhaiskar, V.2    Manus, V.3    Galibert, F.4    Dean, N.5
  • 40
    • 0029060391 scopus 로고
    • Protein kinase C and lipid signaling for sustained cellular responses
    • Nishizuka, Y. 1995. Protein kinase C and lipid signaling for sustained cellular responses. FASEB (Fed. Eur. Soc. Exp. Biol.) J. 9:484-496.
    • (1995) FASEB (Fed. Eur. Soc. Exp. Biol.) J. , vol.9 , pp. 484-496
    • Nishizuka, Y.1
  • 41
    • 0028829555 scopus 로고
    • A downstream target of RHO1 small GTP-binding protein is PKC1, a homolog of protein kinase C, which leads to activation of the MAP kinase cascade in Saccharomyces cerevisiae
    • Nonaka, H., K. Tanaka, H. Hirano, T. Fujiwara, H. Kohno, M. Umikawa, A. Mino, and Y. Takai. 1995. A downstream target of RHO1 small GTP-binding protein is PKC1, a homolog of protein kinase C, which leads to activation of the MAP kinase cascade in Saccharomyces cerevisiae. EMBO (Eur. Mol. Biol. Organ.) J. 14:5931-5938.
    • (1995) EMBO (Eur. Mol. Biol. Organ.) J. , vol.14 , pp. 5931-5938
    • Nonaka, H.1    Tanaka, K.2    Hirano, H.3    Fujiwara, T.4    Kohno, H.5    Umikawa, M.6    Mino, A.7    Takai, Y.8
  • 42
    • 0030861295 scopus 로고    scopus 로고
    • Role of the yeast phosphatidylinositol/phosphatidylcholine transfer protein (Sec14p) in phosphatidylcholine turnover and INO1 regulation
    • Patton-Vogt, J.L., R. Griac, A. Sreenivas, V. Bruno, S. Dowd, M.J. Swede, and S.A. Henry. 1997. Role of the yeast phosphatidylinositol/phosphatidylcholine transfer protein (Sec14p) in phosphatidylcholine turnover and INO1 regulation. J. Biol. Chem. 272:20873-20883.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20873-20883
    • Patton-Vogt, J.L.1    Griac, R.2    Sreenivas, A.3    Bruno, V.4    Dowd, S.5    Swede, M.J.6    Henry, S.A.7
  • 43
    • 0029850711 scopus 로고    scopus 로고
    • Novel domains in NADPH oxidase subunits, sorting nexins, and Ptdlns 3-kinases: Binding partners of SH3 domains?
    • Ponting, C.P. 1997. Novel domains in NADPH oxidase subunits, sorting nexins, and Ptdlns 3-kinases: binding partners of SH3 domains? Protein Sci. 5:2353-2357.
    • (1997) Protein Sci. , vol.5 , pp. 2353-2357
    • Ponting, C.P.1
  • 47
    • 0029020350 scopus 로고    scopus 로고
    • Resolved phospholipase D activity is modulated by cytosolic factors other than Arf
    • Singer, W.D., H.A. Brown, G.M. Bokoch, and P.C. Sternweis. 1996. Resolved phospholipase D activity is modulated by cytosolic factors other than Arf. J. Biol. Chem. 270:14944-14950.
    • (1996) J. Biol. Chem. , vol.270 , pp. 14944-14950
    • Singer, W.D.1    Brown, H.A.2    Bokoch, G.M.3    Sternweis, P.C.4
  • 49
    • 0027274889 scopus 로고
    • Rapid attenuation of receptor-induced diacylglycerol and phosphatidic acid by phospholipase D-mediated transphosphatidylation: Formation of bisphosphatidic acid
    • van Blitterswijk, W.J., and H. Hilkmann. 1993. Rapid attenuation of receptor-induced diacylglycerol and phosphatidic acid by phospholipase D-mediated transphosphatidylation: formation of bisphosphatidic acid. EMBO (Eur. Mol. Biol. Organ.) J. 12:2655-2662.
    • (1993) EMBO (Eur. Mol. Biol. Organ.) J. , vol.12 , pp. 2655-2662
    • Van Blitterswijk, W.J.1    Hilkmann, H.2
  • 50
    • 0030027564 scopus 로고    scopus 로고
    • Identification and characterization of a gene encoding phospholipase D activity in yeast
    • Waksman, M., Y. Eli, M. Liscovitch, and J.E. Gerst. 1996. Identification and characterization of a gene encoding phospholipase D activity in yeast. J. Biol. Chem. 271:2361-2364.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2361-2364
    • Waksman, M.1    Eli, Y.2    Liscovitch, M.3    Gerst, J.E.4
  • 52
    • 0026774568 scopus 로고
    • Activated phosphoinositide 3-kinase associates with membrane skeleton in thrombin-exposed platelets
    • Zhang, J., M.J. Fry, M.D. Waterfield, S. Jaken, L. Liano, J.E.B. Fox and S.E. Rittenhouse. 1992. Activated phosphoinositide 3-kinase associates with membrane skeleton in thrombin-exposed platelets. J. Biol. Chem. 267:4686-4692.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4686-4692
    • Zhang, J.1    Fry, M.J.2    Waterfield, M.D.3    Jaken, S.4    Liano, L.5    Fox, J.E.B.6    Rittenhouse, S.E.7
  • 53
    • 0027262361 scopus 로고
    • Stimulation by phospholipids of a protein-tyrosine-phosphatase containing two src homology 2 domains
    • Zhao, Z., S.H. Shen, and E.H. Fischer. 1993. Stimulation by phospholipids of a protein-tyrosine-phosphatase containing two src homology 2 domains. Proc. Natl. Acad. Sci. USA. 90:4251-4255.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4251-4255
    • Zhao, Z.1    Shen, S.H.2    Fischer, E.H.3


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