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Volumn 9, Issue 4, 1997, Pages 519-526

The role of lipid signaling in constitutive membrane traffic

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR; CLATHRIN; DIACYLGLYCEROL; DYNAMIN; GUANINE NUCLEOTIDE EXCHANGE FACTOR; MEMBRANE LIPID; MEMBRANE PROTEIN; PHOSPHATIDIC ACID; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL; PHOSPHOLIPASE D;

EID: 0030747392     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(97)80028-2     Document Type: Article
Times cited : (93)

References (64)
  • 4
    • 0024433592 scopus 로고
    • Mechanism of membrane anchoring affects polarized expression of two proteins in MDCK cells
    • Brown DA, Crise B, Rose JK: Mechanism of membrane anchoring affects polarized expression of two proteins in MDCK cells. Science 1989, 245:1499-1501.
    • (1989) Science , vol.245 , pp. 1499-1501
    • Brown, D.A.1    Crise, B.2    Rose, J.K.3
  • 5
    • 0024468669 scopus 로고
    • A glycophospholipid membrane anchor acts as an apical targeting signal in polarized epithelial cells
    • Lisanti MP, Caras IW, Davitz MA, Rodriguez-Boulan E: A glycophospholipid membrane anchor acts as an apical targeting signal in polarized epithelial cells. J Cell Biol 1989, 109:2145-2156.
    • (1989) J Cell Biol , vol.109 , pp. 2145-2156
    • Lisanti, M.P.1    Caras, I.W.2    Davitz, M.A.3    Rodriguez-Boulan, E.4
  • 6
    • 0029166488 scopus 로고
    • Hierarchy of mechanisms involved in generating Na/K-ATPase polarity in MDCK epithelial cells
    • Mays RW, Siemers KA, Fritz BA, Lowe AW, Van Meer G, Nelson WJ: Hierarchy of mechanisms involved in generating Na/K-ATPase polarity in MDCK epithelial cells. J Cell Biol 1995, 130:1105-1115.
    • (1995) J Cell Biol , vol.130 , pp. 1105-1115
    • Mays, R.W.1    Siemers, K.A.2    Fritz, B.A.3    Lowe, A.W.4    Van Meer, G.5    Nelson, W.J.6
  • 8
    • 0030156660 scopus 로고    scopus 로고
    • Arf and PITP restore GTP-gamma-S-stimulated protein secretion from cytosol-depleted HL60 cells by promoting PIP2 synthesis
    • Fensome A, Cunningham E, Prosser S, Tan SK, Swigart P, Thomas G, Hsuan JJ: Arf and PITP restore GTP-gamma-S-stimulated protein secretion from cytosol-depleted HL60 cells by promoting PIP2 synthesis. Curr Biol 1996, 6:730-738.
    • (1996) Curr Biol , vol.6 , pp. 730-738
    • Fensome, A.1    Cunningham, E.2    Prosser, S.3    Tan, S.K.4    Swigart, P.5    Thomas, G.6    Hsuan, J.J.7
  • 9
    • 0030222298 scopus 로고    scopus 로고
    • Receptor signalling and the regulation of endocytic membrane transport
    • Seaman MNJ, Burd CG, Emr SD: Receptor signalling and the regulation of endocytic membrane transport Curr Opin Cell Biol 1996, 8:549-556.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 549-556
    • Seaman, M.N.J.1    Burd, C.G.2    Emr, S.D.3
  • 11
    • 0029968296 scopus 로고    scopus 로고
    • Phosphoinositides as regulators in membrane traffic
    • Decamilli P, Emr SD, McPherson PS, Novick P: Phosphoinositides as regulators in membrane traffic. Science 1996, 271:1533-1539.
    • (1996) Science , vol.271 , pp. 1533-1539
    • Decamilli, P.1    Emr, S.D.2    McPherson, P.S.3    Novick, P.4
  • 12
    • 0027905021 scopus 로고
    • Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene essential for protein sorting
    • Schu PV, Takegawa K, Fry MJ, Stack JH, Waterfield MD, Emr SD: Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene essential for protein sorting. Science 1993, 260:88-91.
    • (1993) Science , vol.260 , pp. 88-91
    • Schu, P.V.1    Takegawa, K.2    Fry, M.J.3    Stack, J.H.4    Waterfield, M.D.5    Emr, S.D.6
  • 13
    • 0027256130 scopus 로고
    • A membrane-associated complex containing the Vps15 protein kinase and the Vps34 Pl 3-kinase is essential for protein sorting to the yeast lysosome-like vacuole
    • Stack JH, Herman PK, Schu PV, Emr SD: A membrane-associated complex containing the Vps15 protein kinase and the Vps34 Pl 3-kinase is essential for protein sorting to the yeast lysosome-like vacuole. EMBO J 1993, 12:2195-2204.
    • (1993) EMBO J , vol.12 , pp. 2195-2204
    • Stack, J.H.1    Herman, P.K.2    Schu, P.V.3    Emr, S.D.4
  • 15
    • 0029123267 scopus 로고
    • Wortmannin causes mistargeting of procathepsin D - The involvement of a phosphatidylinositol 3-kinase in vesicular transport to lysosomes
    • Davidson HW: Wortmannin causes mistargeting of procathepsin D - the involvement of a phosphatidylinositol 3-kinase in vesicular transport to lysosomes. J Cell Biol 1995, 130:797-805.
    • (1995) J Cell Biol , vol.130 , pp. 797-805
    • Davidson, H.W.1
  • 16
    • 0029148577 scopus 로고
    • Role for phosphatidylinositol 3-kinase in the sorting and transport of newly synthesized lysosomal enzymes in mammalian cells
    • Brown W, Dewald DB, Emr SD, Plutner H, Balch WE: Role for phosphatidylinositol 3-kinase in the sorting and transport of newly synthesized lysosomal enzymes in mammalian cells. J Cell Biol 1995, 130:781-796.
    • (1995) J Cell Biol , vol.130 , pp. 781-796
    • Brown, W.1    Dewald, D.B.2    Emr, S.D.3    Plutner, H.4    Balch, W.E.5
  • 17
    • 0027997975 scopus 로고
    • Endocytosis is required for the growth of vacuolar H(+)-ATPase-defective yeast: Identification of six new END genes
    • Munn AL, Riezman H: Endocytosis is required for the growth of vacuolar H(+)-ATPase-defective yeast: identification of six new END genes. J Cell Biol 1994, 127:373-386.
    • (1994) J Cell Biol , vol.127 , pp. 373-386
    • Munn, A.L.1    Riezman, H.2
  • 18
    • 0030764770 scopus 로고    scopus 로고
    • Inactivation of two Dictyostelium discoideum genes, DdPIK1 and DdPlk2, results in defects in endocytosis, lysosome to postlysosome transport, and actin cytoskeleton organization
    • Buckynski G, Grove G, Nomura A, Kleve M, Bush J, Firtel RA, Cardelli J: Inactivation of two Dictyostelium discoideum genes, DdPIK1 and DdPlk2, results in defects in endocytosis, lysosome to postlysosome transport, and actin cytoskeleton organization. J Cell Biol 1997, 136:1271-1286. DdPIK1 and DdPIK2 are two Pl 3-kinases that are more closely related by sequence to mammalian 110 kDa Pl 3-kinase than to the yeast Vps34p. The defects in endocytosis reported were specific in that transport of α-mannostdase through the secretory pathway to lysosomes was normal in the double deletion mutant, suggesting that the secretory pathway functioned properly. This raises the interesting possibility that different Pl 3-kinases may act as facilitators in multiple but specific segments of membrane transport pathways.
    • (1997) J Cell Biol , vol.136 , pp. 1271-1286
    • Buckynski, G.1    Grove, G.2    Nomura, A.3    Kleve, M.4    Bush, J.5    Firtel, R.A.6    Cardelli, J.7
  • 19
    • 0029933270 scopus 로고    scopus 로고
    • Wortmannin alters the transferrin receptor endocytic pathway in vivo and in vitro
    • Spiro DJ, Boll W, Kirchhausen T, Wesslingresnick M: Wortmannin alters the transferrin receptor endocytic pathway in vivo and in vitro. Mol Biol Cell 1996, 7:355-367. This work provides evidence for the involvement of wortmannin-sensitive phosphatidylinositol kinases in multiple endocytic processes.
    • (1996) Mol Biol Cell , vol.7 , pp. 355-367
    • Spiro, D.J.1    Boll, W.2    Kirchhausen, T.3    Wesslingresnick, M.4
  • 20
    • 15844427939 scopus 로고    scopus 로고
    • Wortmannin-sensitive trafficking pathways in Chinese hamster ovary cells - Differential effects on endocytosis and lysosomal sorting
    • Martys JL, Wjasow C, Gangi DM, Kielian MC, McGraw TE, Backer JM: Wortmannin-sensitive trafficking pathways in Chinese hamster ovary cells - differential effects on endocytosis and lysosomal sorting. J Biol Chem 1996, 271:10953-10962. The authors provide evidence that wortmannin-sensitive phosphatidylinositol kinases function in three different endocytic processes, but not in the secretory pathway.
    • (1996) J Biol Chem , vol.271 , pp. 10953-10962
    • Martys, J.L.1    Wjasow, C.2    Gangi, D.M.3    Kielian, M.C.4    McGraw, T.E.5    Backer, J.M.6
  • 21
    • 0030027394 scopus 로고    scopus 로고
    • Potential sites of Pl-3 kinase function in the endocytic pathway revealed by the Pl-3 kinase inhibitor, wortmannin
    • Shpetner H, Joly M, Hartley D, Corvera S: Potential sites of Pl-3 kinase function in the endocytic pathway revealed by the Pl-3 kinase inhibitor, wortmannin. J Cell Biol 1996, 132:595-605. This study provides evidence that Pl 3-kinase is required both for recycling of endocytosed proteins to the plasma membrane and for delivery of PDGF receptors to late endosomal compartments.
    • (1996) J Cell Biol , vol.132 , pp. 595-605
    • Shpetner, H.1    Joly, M.2    Hartley, D.3    Corvera, S.4
  • 23
    • 0028862325 scopus 로고
    • Wortmannin, an inhibitor of phosphoinositide 3-kinase, inhibits transcytosis in polarized epithelial cells
    • Hansen SH, Olsson A, Casanova JE: Wortmannin, an inhibitor of phosphoinositide 3-kinase, inhibits transcytosis in polarized epithelial cells. J Biol Chem 1995, 270:28425-28432.
    • (1995) J Biol Chem , vol.270 , pp. 28425-28432
    • Hansen, S.H.1    Olsson, A.2    Casanova, J.E.3
  • 24
    • 0028979563 scopus 로고
    • Phosphatidylinositol 3-kinase regulation of fluid phase endocytosis
    • Clague MJ, Thorpe C, Jones AT: Phosphatidylinositol 3-kinase regulation of fluid phase endocytosis. FEBS Lett 1995, 367:272-274.
    • (1995) FEBS Lett , vol.367 , pp. 272-274
    • Clague, M.J.1    Thorpe, C.2    Jones, A.T.3
  • 25
    • 0029863528 scopus 로고    scopus 로고
    • The effect of wortmannin on the localisation of lysosomal type I integral membrane glycoproteins suggests a role for phosphoinositide 3-kinase activity in regulating membrane traffic late in the endocytic pathway
    • Reaves BJ, Bright NA, Mullock BM, Luzio JP: The effect of wortmannin on the localisation of lysosomal type I integral membrane glycoproteins suggests a role for phosphoinositide 3-kinase activity in regulating membrane traffic late in the endocytic pathway. J Cell Sci 1996, 109:749-762.
    • (1996) J Cell Sci , vol.109 , pp. 749-762
    • Reaves, B.J.1    Bright, N.A.2    Mullock, B.M.3    Luzio, J.P.4
  • 26
    • 0029151540 scopus 로고
    • Phosphatidylinositol 3-kinase activity is required for early endosome fusion
    • Jones AT, Clague MJ: Phosphatidylinositol 3-kinase activity is required for early endosome fusion. Biochem J 1995, 311:31-34.
    • (1995) Biochem J , vol.311 , pp. 31-34
    • Jones, A.T.1    Clague, M.J.2
  • 27
    • 0029015694 scopus 로고
    • A wortmannin-sensitive phosphatidylinositol 4-kinase that regulates hormone-sensitive pools of inositolphospholipids
    • Nakanishi S, Catt KJ, Balla T: A wortmannin-sensitive phosphatidylinositol 4-kinase that regulates hormone-sensitive pools of inositolphospholipids. Proc Natl Acad Sci USA 1995, 92:5317-5321.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5317-5321
    • Nakanishi, S.1    Catt, K.J.2    Balla, T.3
  • 28
    • 0029954611 scopus 로고    scopus 로고
    • Cloning and characterization of a 92 kda soluble phosphatidylinositol 4-kinase
    • Nakagawa T, Goto K, Kondo H: Cloning and characterization of a 92 kda soluble phosphatidylinositol 4-kinase. Biochem J 1996, 320:643-649.
    • (1996) Biochem J , vol.320 , pp. 643-649
    • Nakagawa, T.1    Goto, K.2    Kondo, H.3
  • 29
    • 0028850452 scopus 로고
    • Wortmannin and its structural analogue demethoxyviridin inhibit stimulated phospholipase A2 activity in Swiss 3T3 cells. Wortmannin is not a specific inhibitor of phosphatidylinositol 3-kinase
    • Cross MJ, Stewart A, Hodgkin MN, Kerr DJ, Wakelam MJ: Wortmannin and its structural analogue demethoxyviridin inhibit stimulated phospholipase A2 activity in Swiss 3T3 cells. Wortmannin is not a specific inhibitor of phosphatidylinositol 3-kinase. J Biol Chem 1995, 270:25352-25355.
    • (1995) J Biol Chem , vol.270 , pp. 25352-25355
    • Cross, M.J.1    Stewart, A.2    Hodgkin, M.N.3    Kerr, D.J.4    Wakelam, M.J.5
  • 30
    • 0029851773 scopus 로고    scopus 로고
    • Nucleotide exchange on ARF mediated by yeast Gea1 protein
    • Peyroche A, Paris S, Jackson CL: Nucleotide exchange on ARF mediated by yeast Gea1 protein. Nature 1996, 384:479-481.
    • (1996) Nature , vol.384 , pp. 479-481
    • Peyroche, A.1    Paris, S.2    Jackson, C.L.3
  • 32
    • 0030975196 scopus 로고    scopus 로고
    • Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains
    • 2. Like ARNO, cytohesin-1 has guanine nucleotide exchange activity for an ARF, at least in vitro [34]. These observations may indicate the potential for differential regulation of ARFs by unique phosphatidylinositol kinases.
    • (1997) Science , vol.275 , pp. 1927-1930
    • Klarlund, J.K.1    Guilherme, A.2    Holik, J.J.3    Virbasius, J.V.4    Chawla, A.5    Czech, M.P.6
  • 33
  • 34
    • 0026788419 scopus 로고
    • Cloning and sequencing of a human cDNA from cytolytic NK/T cells with homology to yeast SEC7
    • Liu L, Pohajdak B: Cloning and sequencing of a human cDNA from cytolytic NK/T cells with homology to yeast SEC7. Biochim Biophys Acta 1992, 1132:75-78.
    • (1992) Biochim Biophys Acta , vol.1132 , pp. 75-78
    • Liu, L.1    Pohajdak, B.2
  • 35
    • 0030602819 scopus 로고    scopus 로고
    • Alpha L beta 2 integrin/LFA-1 binding to ICAM-1 induced by cytohesin-1, a cytoplasmic regulatory molecule
    • Kolanus W, Nagel W, Schiller B, Zeitlmann L, Godar S, Stockinger H, Seed B: Alpha L beta 2 integrin/LFA-1 binding to ICAM-1 induced by cytohesin-1, a cytoplasmic regulatory molecule. Cell 1996, 86:233-242.
    • (1996) Cell , vol.86 , pp. 233-242
    • Kolanus, W.1    Nagel, W.2    Schiller, B.3    Zeitlmann, L.4    Godar, S.5    Stockinger, H.6    Seed, B.7
  • 36
    • 0028278346 scopus 로고
    • GTP hydrolysis by ADP-ribosylation factor is dependent on both an ADP-ribosylation factor GTPase-activating protein and acid phospholipids
    • Randazzo PA, Kahn RA: GTP hydrolysis by ADP-ribosylation factor is dependent on both an ADP-ribosylation factor GTPase-activating protein and acid phospholipids. J Biol Chem 1994, 269:10758-10763.
    • (1994) J Biol Chem , vol.269 , pp. 10758-10763
    • Randazzo, P.A.1    Kahn, R.A.2
  • 37
    • 0028900483 scopus 로고
    • ADP-ribosylation factor-directed GTPase-activating protein. Purification and partial characterization
    • Makler V, Cukierman E, Rotman M, Admon A, Cassel D: ADP-ribosylation factor-directed GTPase-activating protein. Purification and partial characterization. J Biol Chem 1995, 270:5232-5237.
    • (1995) J Biol Chem , vol.270 , pp. 5232-5237
    • Makler, V.1    Cukierman, E.2    Rotman, M.3    Admon, A.4    Cassel, D.5
  • 38
    • 0030944208 scopus 로고    scopus 로고
    • Functional interaction of ADP-ribosylation factor 1 with phosphatidylinositol 4,5-bisphosphate
    • Randazzo PA: Functional interaction of ADP-ribosylation factor 1 with phosphatidylinositol 4,5-bisphosphate. J Biol Chem 1997, 272:7688-7692.
    • (1997) J Biol Chem , vol.272 , pp. 7688-7692
    • Randazzo, P.A.1
  • 39
    • 0028030072 scopus 로고
    • Effects of acid phospholipids on nucleotide exchange properties of ADP-ribosylation factor 1. Evidence for specific interaction with phosphatidylinositol 4,5-bisphosphate
    • Terui T, Kahn RA, Randazzo PA: Effects of acid phospholipids on nucleotide exchange properties of ADP-ribosylation factor 1. Evidence for specific interaction with phosphatidylinositol 4,5-bisphosphate. J Biol Chem 1994, 269:28130-28135.
    • (1994) J Biol Chem , vol.269 , pp. 28130-28135
    • Terui, T.1    Kahn, R.A.2    Randazzo, P.A.3
  • 40
    • 0030600145 scopus 로고    scopus 로고
    • Dynamin and receptor-mediated endocytosis
    • Damke H: Dynamin and receptor-mediated endocytosis. FEBS Lett 1996, 389:48-51.
    • (1996) FEBS Lett , vol.389 , pp. 48-51
    • Damke, H.1
  • 41
    • 0001351392 scopus 로고    scopus 로고
    • Regulation of dynamin I GTPase activity by G protein beta-gamma subunits and phosphatidylinositol 4,5-bisphosphate
    • 2 also enhanced the apparent affinity of dynamin for Gβγ. Gβγ inhibited the GTPase activity of monomeric dynamin proteins, but did not affect oligomeric dynamin. A model is proposed whereby dynamin GTPase is activated by the phospholipid but held in check by the free Gβγ subunits.
    • (1996) J Biol Chem , vol.271 , pp. 27979-27982
    • Lin, H.C.1    Gilman, A.G.2
  • 43
    • 0029942238 scopus 로고    scopus 로고
    • Association of a dynamin-like protein with the Golgi apparatus in mammalian cells
    • Henley JR, McNiven MA: Association of a dynamin-like protein with the Golgi apparatus in mammalian cells. J Cell Biol 1996, 133:761-775.
    • (1996) J Cell Biol , vol.133 , pp. 761-775
    • Henley, J.R.1    McNiven, M.A.2
  • 44
    • 0029060795 scopus 로고
    • The protein deficient in Lowe syndrome is a phosphatidylinositol-4,5-bisphosphate 5-phosphatase
    • Zhang X, Jefferson AB, Auethavekiat V, Majerus PW: The protein deficient in Lowe syndrome is a phosphatidylinositol-4,5-bisphosphate 5-phosphatase. Proc Natl Acad Sci USA 1995, 92:4853-4856.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4853-4856
    • Zhang, X.1    Jefferson, A.B.2    Auethavekiat, V.3    Majerus, P.W.4
  • 45
    • 0028880052 scopus 로고
    • Lowe syndrome, a deficiency of phosphatidylinositol 4,5-bisphosphate 5-phosphatase in the Golgi apparatus
    • Suchy SF, Olivos-Glander IM, Nussabaum RL: Lowe syndrome, a deficiency of phosphatidylinositol 4,5-bisphosphate 5-phosphatase in the Golgi apparatus. Hum Mol Genet 1995, 4:2245-2250.
    • (1995) Hum Mol Genet , vol.4 , pp. 2245-2250
    • Suchy, S.F.1    Olivos-Glander, I.M.2    Nussabaum, R.L.3
  • 47
    • 0030985247 scopus 로고    scopus 로고
    • Regulatory interactions in the recognition of endocytic sorting signals by AP-2 complexes
    • Papoport I, Miyazaki M, Boll W, Duckworth B, Cantley L, Shoelson S, Kirchhausen T: Regulatory interactions in the recognition of endocytic sorting signals by AP-2 complexes. EMBO J 1997, 17:2240-2250. Phosphatidylinositol 3-phosphate (Ptdlns(3)P) was shown to increase the affinity of the AP2 complex for internalization signals. This effect was specific for phosphatidylinositols with phosphate at the 3′ position of the inositol ring, suggesting that one role of Pl 3-kinases in secretion may be to activate coat components for binding cargo. Binding to clathrin also increased the affinity of AP2 for internalization signals, but the effects of clathrin and Ptdlns(3)P were not additive.
    • (1997) EMBO J , vol.17 , pp. 2240-2250
    • Papoport, I.1    Miyazaki, M.2    Boll, W.3    Duckworth, B.4    Cantley, L.5    Shoelson, S.6    Kirchhausen, T.7
  • 48
    • 0030907067 scopus 로고    scopus 로고
    • Regulation of eukaryotic phosphatidylinositol-specific phospholipase C and phospholipase D
    • in press
    • Singer WD, Brown HA, Sternweis PC: Regulation of eukaryotic phosphatidylinositol-specific phospholipase C and phospholipase D. Annu Rev Biochem 1997, 66:in press.
    • (1997) Annu Rev Biochem , vol.66
    • Singer, W.D.1    Brown, H.A.2    Sternweis, P.C.3
  • 49
    • 0027142022 scopus 로고
    • ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity
    • Brown HA, Gutowski S, Moomaw CR, Slaughter C, Sternweis PC: ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity. Cell 1993, 75:1137-1144.
    • (1993) Cell , vol.75 , pp. 1137-1144
    • Brown, H.A.1    Gutowski, S.2    Moomaw, C.R.3    Slaughter, C.4    Sternweis, P.C.5
  • 51
    • 0029065704 scopus 로고
    • Phospholipase D is present on Golgi-enriched membranes and its activation by ADP ribosylation factor is sensitive to brefeldin A
    • Ktistakis NT, Brown HA, Sternweis PC, Roth MG: Phospholipase D is present on Golgi-enriched membranes and its activation by ADP ribosylation factor is sensitive to brefeldin A. Proc Natl Acad Sci USA 1995, 92:4952-4956.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4952-4956
    • Ktistakis, N.T.1    Brown, H.A.2    Sternweis, P.C.3    Roth, M.G.4
  • 52
    • 0026767452 scopus 로고
    • Activation of phospholipase D by protein kinase C. Evidence for a phosphorylation-independent mechanism
    • Conricode KM, Brewer KA, Exton JH: Activation of phospholipase D by protein kinase C. Evidence for a phosphorylation-independent mechanism. J Biol Chem 1992, 267:7199-7202.
    • (1992) J Biol Chem , vol.267 , pp. 7199-7202
    • Conricode, K.M.1    Brewer, K.A.2    Exton, J.H.3
  • 53
    • 0029671455 scopus 로고    scopus 로고
    • Regulation of phospholipase D by protein kinase C is synergistic with ADP- Ribosylation factor and independent of protein kinase activity
    • Singer WD, Brown HA, Jiang X, Sternweis PC: Regulation of phospholipase D by protein kinase C is synergistic with ADP- ribosylation factor and independent of protein kinase activity, J Biol Chem 1996, 271:4504-4510. This paper describes the synergistic stimulation of PLD by PKCα and other activators. More significantly, the experiments established a novel mechanism for action of PLD in that the regulation of PLD was mediated by the regulatory domain of the PKCα rather than by PKCα's catalytic protein kinase domain. This indicates that protein kinase inhibitors will not block all of the actions of these protein kinases.
    • (1996) J Biol Chem , vol.271 , pp. 4504-4510
    • Singer, W.D.1    Brown, H.A.2    Jiang, X.3    Sternweis, P.C.4
  • 55
    • 0027967774 scopus 로고
    • Export of protein from the endoplasmic reticulum is regulated by a diacylglycerol/phorbol ester binding protein
    • Fabbri M, Bannykh S, Balch WE: Export of protein from the endoplasmic reticulum is regulated by a diacylglycerol/phorbol ester binding protein. J Biol Chem 1994, 269:26848-26857.
    • (1994) J Biol Chem , vol.269 , pp. 26848-26857
    • Fabbri, M.1    Bannykh, S.2    Balch, W.E.3
  • 56
    • 0029911415 scopus 로고    scopus 로고
    • The production of post-Golgi vesicles requires a protein kinase C-like molecule, but not its phosphorylating activity
    • Simon JP, Ivanov IE, Adesnik M, Sabatini DD: The production of post-Golgi vesicles requires a protein kinase C-like molecule, but not its phosphorylating activity. J Cell Biol 1996, 135:355-370.
    • (1996) J Cell Biol , vol.135 , pp. 355-370
    • Simon, J.P.1    Ivanov, I.E.2    Adesnik, M.3    Sabatini, D.D.4
  • 57
    • 0029564902 scopus 로고
    • Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family
    • Hammond SM, Altshuller YM, Sung TC, Rudge SA, Rose K, Engebrecht J, Morris AJ, Frohman MA: Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family. J Biol Chem 1995, 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
  • 59
    • 0031149834 scopus 로고    scopus 로고
    • Formation of phosphatidic acid by phospholipase D is required for transport from the endoplasmic reticulum to the Golgi complex in Chinese hamster ovary cells
    • Bi K, Roth MG, Ktistakis NT: Formation of phosphatidic acid by phospholipase D is required for transport from the endoplasmic reticulum to the Golgi complex in Chinese hamster ovary cells. Curr Biol 1997, 7:301-307.
    • (1997) Curr Biol , vol.7 , pp. 301-307
    • Bi, K.1    Roth, M.G.2    Ktistakis, N.T.3
  • 60
    • 0025094319 scopus 로고
    • An essential role for a phospholipid transfer protein in yeast Golgi
    • Bankaitis VA, Aitken JR, Cleves AE, Dowhan W: An essential role for a phospholipid transfer protein in yeast Golgi. Nature 1990, 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
  • 61
    • 0026073075 scopus 로고
    • Mutations in the CDP-choline pathway for phospholipid biosynthesis bypass the requirement for an essential phospholipid transfer protein
    • Cleves AE, McGee TP, Whitters EA, Champion KM, Aitken JR, Dowhan W, Goebl M, Bankaitis VA: Mutations in the CDP-choline pathway for phospholipid biosynthesis bypass the requirement for an essential phospholipid transfer protein. Cell 1991, 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
  • 62
    • 0030952220 scopus 로고    scopus 로고
    • An essential role for diacylglycerol in protein transport from the yeast Golgi complex
    • Kearns, B, McGee TP, Mayinger P, Gedvilaite A, Phillips SE, Kagiwada S, Bankaitis VA: An essential role for diacylglycerol in protein transport from the yeast Golgi complex. Nature 1997, 386:101-105. The defect in the S. cerevisiae secretion mutant sec 14 can be suppressed by supplying the Golgi complex with DAG either genetically or with exogenous lipid. These results suggest that the critical function of Sec14p may be to maintain sufficient pools of DAG to support secretion. The exact role played by DAG, however, is still unknown.
    • (1997) Nature , vol.386 , pp. 101-105
    • Kearns, B.1    McGee, T.P.2    Mayinger, P.3    Gedvilaite, A.4    Phillips, S.E.5    Kagiwada, S.6    Bankaitis, V.A.7
  • 64
    • 0026774637 scopus 로고
    • Bacterial ADP-ribosyltransferase with a substrate specificity of the Rho protein disassembles the Golgi apparatus in Vero cells and mimics the action of brefeldin A
    • Sugai M, Chen CH, Wu HC: Bacterial ADP-ribosyltransferase with a substrate specificity of the Rho protein disassembles the Golgi apparatus in Vero cells and mimics the action of brefeldin A. Proc Natl Acad Sci USA 1992, 89:8903-8907.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8903-8907
    • Sugai, M.1    Chen, C.H.2    Wu, H.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.