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Volumn 98, Issue 1-2, 1999, Pages 141-152

Phospholipase D as an effector for ADP-ribosylation factor in the regulation of vesicular traffic

Author keywords

ADP ribosylation factor; Diacylglycerol; Phosphatidic acid; Phosphatidylinositol (4,5)bisphosphate; Phospholipase D; Vesicle transport

Indexed keywords

DIACYLGLYCEROL; ISOENZYME; MEMBRANE ENZYME; PHOSPHATIDIC ACID; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PHOSPHOLIPASE D;

EID: 0032987261     PISSN: 00093084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-3084(99)00026-2     Document Type: Conference Paper
Times cited : (53)

References (93)
  • 1
    • 0030692015 scopus 로고    scopus 로고
    • Activation of ADP-ribosylation factor 1 GTPase-activating protein by phosphatidylcholine-derived diacylglycerols
    • Antonny B., Huber I., Paris S., Chabre M., Cassel D. Activation of ADP-ribosylation factor 1 GTPase-activating protein by phosphatidylcholine-derived diacylglycerols. J. Biol. Chem. 272:1997;30848-30851.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30848-30851
    • Antonny, B.1    Huber, I.2    Paris, S.3    Chabre, M.4    Cassel, D.5
  • 2
    • 13144294022 scopus 로고    scopus 로고
    • Modulation of intracellular transport by transported proteins-insight from regulation of COPI-mediated transport
    • Aoe T., Lee A.J., Vandonselaar E., Peters P.J., Hsu V.W. Modulation of intracellular transport by transported proteins-insight from regulation of COPI-mediated transport. Proc. Natl. Acad. Sci. USA. 95:1998;1624-1629.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1624-1629
    • Aoe, T.1    Lee, A.J.2    Vandonselaar, E.3    Peters, P.J.4    Hsu, V.W.5
  • 3
    • 0028971172 scopus 로고
    • Sequential coupling between COPII and COPI vesicle coats in endoplasmic reticulum to Golgi transport
    • Aridor M., Bannykh S.I., Rowe T., Balch W.E. Sequential coupling between COPII and COPI vesicle coats in endoplasmic reticulum to Golgi transport. J. Cell Biol. 131:1995;875-893.
    • (1995) J. Cell Biol. , vol.131 , pp. 875-893
    • Aridor, M.1    Bannykh, S.I.2    Rowe, T.3    Balch, W.E.4
  • 4
    • 0030742746 scopus 로고    scopus 로고
    • Membrane dynamics at the endoplasmic reticulum Golgi interface
    • Bannykh S.I., Balch W.E. Membrane dynamics at the endoplasmic reticulum Golgi interface. J. Cell Biol. 138:1997;1-4.
    • (1997) J. Cell Biol. , vol.138 , pp. 1-4
    • Bannykh, S.I.1    Balch, W.E.2
  • 5
    • 0028233498 scopus 로고
    • COPII:a membrane coat formed by sec proteins that drive vesicle budding from endoplasmic reticulum
    • Barlowe C., Orci L., Young T. et al. COPII:a membrane coat formed by sec proteins that drive vesicle budding from endoplasmic reticulum. Cell. 77:1994;895-907.
    • (1994) Cell , vol.77 , pp. 895-907
    • Barlowe, C.1    Orci, L.2    Young, T.3
  • 6
    • 0029558526 scopus 로고
    • COPI- And COPII-coated vesicles bud directly from the endoplasmic reticulum in yeast
    • Bednarek S.Y., Ravazzola M., Hosobuchi M. et al. COPI- and COPII-coated vesicles bud directly from the endoplasmic reticulum in yeast. Cell. 83:1995;1183-1196.
    • (1995) Cell , vol.83 , pp. 1183-1196
    • Bednarek, S.Y.1    Ravazzola, M.2    Hosobuchi, M.3
  • 7
    • 0031149834 scopus 로고    scopus 로고
    • Phosphatidic acid formation by phospholipase D is required for transport from the endoplasmic reticulum to the Golgi complex
    • Bi K., Roth M.G., Ktistakis N.T. Phosphatidic acid formation by phospholipase D is required for transport from the endoplasmic reticulum to the Golgi complex. Curr Biol. 7:1997;301-307.
    • (1997) Curr Biol , vol.7 , pp. 301-307
    • Bi, K.1    Roth, M.G.2    Ktistakis, N.T.3
  • 9
    • 0027142022 scopus 로고
    • ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity
    • Brown H.A., Gutowski S., Moomaw C.R., Slaughter C.P.C.S. ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity. Cell. 75:1993;1137-1144.
    • (1993) Cell , vol.75 , pp. 1137-1144
    • Brown, H.A.1    Gutowski, S.2    Moomaw, C.R.3    Slaughter, C.P.C.S.4
  • 10
    • 0032474821 scopus 로고    scopus 로고
    • Phospholipase D1 localises to secretory granules and lysosomes and is plasma-membrane translocated on cellular stimulation
    • Brown F.D., Thompson N., Saqib K.M. et al. Phospholipase D1 localises to secretory granules and lysosomes and is plasma-membrane translocated on cellular stimulation. Curr. Biol. 8:1998;835-838.
    • (1998) Curr. Biol. , vol.8 , pp. 835-838
    • Brown, F.D.1    Thompson, N.2    Saqib, K.M.3
  • 12
    • 0029844904 scopus 로고    scopus 로고
    • A human exchange factor for ARF contains Sec7- And pleckstrin-homology domains
    • Chardin P., Paris S., Antonny B. et al. A human exchange factor for ARF contains Sec7- and pleckstrin-homology domains. Nature. 384:1996;481-484.
    • (1996) Nature , vol.384 , pp. 481-484
    • Chardin, P.1    Paris, S.2    Antonny, B.3
  • 13
    • 0030840865 scopus 로고    scopus 로고
    • Phospholipase D stimulates release of nascent secretory vesicles from the trans-Golgi network
    • Chen Y.G., Siddhanta A., Austin C.D. et al. Phospholipase D stimulates release of nascent secretory vesicles from the trans-Golgi network. J. Cell Biol. 138:1997;495-504.
    • (1997) J. Cell Biol. , vol.138 , pp. 495-504
    • Chen, Y.G.1    Siddhanta, A.2    Austin, C.D.3
  • 14
    • 0030011648 scopus 로고    scopus 로고
    • Phospholipid signaling in leukocytes
    • Cockcroft S. Phospholipid signaling in leukocytes. Curr. Opin. Hematol. 3:1996;48-54.
    • (1996) Curr. Opin. Hematol. , vol.3 , pp. 48-54
    • Cockcroft, S.1
  • 15
    • 0028781450 scopus 로고
    • Phospholipase D: A downstream effector of ARF in granulocytes
    • Cockcroft S., Thomas G.M.H.A.F., Geny B. et al. Phospholipase D: a downstream effector of ARF in granulocytes. Science. 263:1994;523-526.
    • (1994) Science , vol.263 , pp. 523-526
    • Cockcroft, S.1    Thomas, G.M.H.A.F.2    Geny, B.3
  • 16
    • 0031105873 scopus 로고    scopus 로고
    • Phospholipase D2, a distinct phospholipase D isoform with novel regulatory properties that provokes cytoskeletal reorganization
    • Colley W.C., Sung T.C., Roll R. et al. Phospholipase D2, a distinct phospholipase D isoform with novel regulatory properties that provokes cytoskeletal reorganization. Curr. Biol. 7:1997;191-201.
    • (1997) Curr. Biol. , vol.7 , pp. 191-201
    • Colley, W.C.1    Sung, T.C.2    Roll, R.3
  • 17
    • 0028786331 scopus 로고
    • Heterotrimeric G proteins interact with the small GTPase Arf-possibilities for the regulation of vesicular traffic
    • Colombo M.I., Inglese J., Dsouzaschorey C., Beron W., Stahl P.D. Heterotrimeric G proteins interact with the small GTPase Arf-possibilities for the regulation of vesicular traffic. J. Biol. Chem. 270:1995;24564-24571.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24564-24571
    • Colombo, M.I.1    Inglese, J.2    Dsouzaschorey, C.3    Beron, W.4    Stahl, P.D.5
  • 18
    • 0026767452 scopus 로고
    • Activation of phospholipase D by protein kinase C. Evidence for a phosphorylation-independent mechanism
    • Conricode K.M., Brewer K.A., Exton J.H. Activation of phospholipase D by protein kinase C. Evidence for a phosphorylation-independent mechanism. J. Biol. Chem. 267:1992;7199-7202.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7199-7202
    • Conricode, K.M.1    Brewer, K.A.2    Exton, J.H.3
  • 19
    • 0029416828 scopus 로고
    • The Arf1 GTPase-activating protein-zinc finger motif and Golgi complex localization
    • Cukierman E., Huber I., Rotman M., Cassel D. The Arf1 GTPase-activating protein-zinc finger motif and Golgi complex localization. Science. 270:1995;1999-2002.
    • (1995) Science , vol.270 , pp. 1999-2002
    • Cukierman, E.1    Huber, I.2    Rotman, M.3    Cassel, D.4
  • 20
    • 0027953550 scopus 로고
    • Dominant inhibitory mutants of ARF1 block endoplasmic reticulum to Golgi transport and trigger disassembly of the Golgi apparatus
    • Dascher C., Balch W. E. Dominant inhibitory mutants of ARF1 block endoplasmic reticulum to Golgi transport and trigger disassembly of the Golgi apparatus. J. Biol. Chem. 269:1994;1437-1448.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1437-1448
    • Dascher, C.1    Balch, W.E.2
  • 21
    • 0030051441 scopus 로고    scopus 로고
    • The AP-1 adaptor complex binds to immature secretory granules from PC12 cells, and is regulated by ADP-ribosylation factor
    • Dittie A.S., Hajibagheri N., Tooze S.A. The AP-1 adaptor complex binds to immature secretory granules from PC12 cells, and is regulated by ADP-ribosylation factor. J. Cell Biol. 132:1996;523-536.
    • (1996) J. Cell Biol. , vol.132 , pp. 523-536
    • Dittie, A.S.1    Hajibagheri, N.2    Tooze, S.A.3
  • 22
    • 0026677375 scopus 로고
    • Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein
    • Donaldson J.G., Finazzi D., Klausner R.D. Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein. Nature. 360:1992;350-352.
    • (1992) Nature , vol.360 , pp. 350-352
    • Donaldson, J.G.1    Finazzi, D.2    Klausner, R.D.3
  • 24
    • 0030948743 scopus 로고    scopus 로고
    • New developments in phospholipase D
    • Exton J.H. New developments in phospholipase D. J. Biol. Chem. 272:1997;15579-15582.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15579-15582
    • Exton, J.H.1
  • 25
    • 0039311662 scopus 로고    scopus 로고
    • ADP ribosylation factor 1 is required for synaptic vesicle budding in PC12 cells
    • Faundez V., Horng J.T., Kelly R.B. ADP ribosylation factor 1 is required for synaptic vesicle budding in PC12 cells. J. Cell Biol. 138:1997;505-515.
    • (1997) J. Cell Biol. , vol.138 , pp. 505-515
    • Faundez, V.1    Horng, J.T.2    Kelly, R.B.3
  • 26
    • 0028290272 scopus 로고
    • Aluminum fluoride acts on the reversibility of ARF1-dependent coat protein binding to Golgi membranes
    • Finazzi D., Cassel D., Donaldson J.G., Klausner R.D. Aluminum fluoride acts on the reversibility of ARF1-dependent coat protein binding to Golgi membranes. J. Biol. Chem. 269:1994;13325-13330.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13325-13330
    • Finazzi, D.1    Cassel, D.2    Donaldson, J.G.3    Klausner, R.D.4
  • 27
    • 0028988228 scopus 로고
    • The small G-protein ARF1GDP binds to the Gt beta gamma subunit of transducin, but not to Gt alpha GDP-Gt beta gamma
    • Franco M., Paris S., Chabre M. The small G-protein ARF1GDP binds to the Gt beta gamma subunit of transducin, but not to Gt alpha GDP-Gt beta gamma. FEBS Lett. 362:1995;286-290.
    • (1995) FEBS Lett. , vol.362 , pp. 286-290
    • Franco, M.1    Paris, S.2    Chabre, M.3
  • 28
    • 0031982629 scopus 로고    scopus 로고
    • Arno is a guanine nucleotide exchange factor for ADP-ribosylation factor 6
    • Frank S., Upender S., Hansen S.H., Casanova J.E. Arno is a guanine nucleotide exchange factor for ADP-ribosylation factor 6. J. Biol. Chem. 273:1998;23-27.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23-27
    • Frank, S.1    Upender, S.2    Hansen, S.H.3    Casanova, J.E.4
  • 30
    • 0030812588 scopus 로고    scopus 로고
    • Functional dissection of COP-I subunits in the biogenesis of multivesicular endosomes
    • Gu F., Aniento F., Parton R.G., Gruenberg J. Functional dissection of COP-I subunits in the biogenesis of multivesicular endosomes. J. Cell Biol. 139:1997;1183-1195.
    • (1997) J. Cell Biol. , vol.139 , pp. 1183-1195
    • Gu, F.1    Aniento, F.2    Parton, R.G.3    Gruenberg, J.4
  • 31
    • 0029564902 scopus 로고
    • Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family
    • Hammond S.M., Altshuller Y.M., Sung T.C., Rudge S.A., Rose K. et al. Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family. J. Biol. Chem. 270:1995;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
  • 32
    • 0026746713 scopus 로고
    • Inhibition by brefeldin A of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF
    • Helms J.B., Rothman J.E. Inhibition by brefeldin A of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF. Nature. 360:1992;352-354.
    • (1992) Nature , vol.360 , pp. 352-354
    • Helms, J.B.1    Rothman, J.E.2
  • 33
    • 0032492689 scopus 로고    scopus 로고
    • Regulation of phospholipase D2-selective inhibition of mammalian phospholipase D isoenzymes by alpha- And beta-synucleins
    • Jenco J.M., Rawlingson A., Daniels B., Morris A.J. Regulation of phospholipase D2-selective inhibition of mammalian phospholipase D isoenzymes by alpha- and beta-synucleins. Biochemistry. 37:1998;4901-4909.
    • (1998) Biochemistry , vol.37 , pp. 4901-4909
    • Jenco, J.M.1    Rawlingson, A.2    Daniels, B.3    Morris, A.J.4
  • 34
    • 0022978533 scopus 로고
    • The protein cofactor necessary for ADP-ribosylation of Gs by cholera toxin is itself a GTP binding protein
    • Kahn R.A., Gilman A.G. The protein cofactor necessary for ADP-ribosylation of Gs by cholera toxin is itself a GTP binding protein. J. Biol. Chem. 261:1986;7906-7911.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7906-7911
    • Kahn, R.A.1    Gilman, A.G.2
  • 35
    • 0027138873 scopus 로고
    • ARF signaling: A potential role for phospholipase D in membrane traffic
    • Kahn R.A., Yucel J.K., Malhorta V. ARF signaling: a potential role for phospholipase D in membrane traffic. Cell. 75:1993;1045-1048.
    • (1993) Cell , vol.75 , pp. 1045-1048
    • Kahn, R.A.1    Yucel, J.K.2    Malhorta, V.3
  • 36
    • 0031939743 scopus 로고    scopus 로고
    • Regulation of Grp1-catalyzed ADP ribosylation factor guanine nucleotide exchange by phosphatidylinositol 3,4,5-trisphosphate
    • Klarlund J.K., Rameh L.E., Cantley L.C., Buxton J.M., Holik J.J. et al. Regulation of Grp1-catalyzed ADP ribosylation factor guanine nucleotide exchange by phosphatidylinositol 3,4,5-trisphosphate. J. Biol. Chem. 273:1998;1859-1862.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1859-1862
    • Klarlund, J.K.1    Rameh, L.E.2    Cantley, L.C.3    Buxton, J.M.4    Holik, J.J.5
  • 37
    • 0032103841 scopus 로고    scopus 로고
    • Signalling molecules and the regulation of intracellular transport
    • Ktistakis N.T. Signalling molecules and the regulation of intracellular transport. Bioessays. 20:1998;495-504.
    • (1998) Bioessays , vol.20 , pp. 495-504
    • Ktistakis, N.T.1
  • 38
    • 0029065704 scopus 로고
    • Phospholipase D is present on Golgi-enriched membranes and its activation by ADP ribosylation factor is sensitive to brefeldin A
    • Ktistakis N.T., Brown H.A., Sternweis P.C., Roth M.G. 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. 92:1995;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
  • 39
    • 0030013233 scopus 로고    scopus 로고
    • Evidence that phospholipase D mediates ADP ribosylation factor-dependent formation of Golgi coated vesicles
    • Ktistakis N.T., Brown H.A., Waters M.G., Sternweis P.C., Roth M.G. Evidence that phospholipase D mediates ADP ribosylation factor-dependent formation of Golgi coated vesicles. J. Cell Biol. 134:1996;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
  • 40
    • 0028178372 scopus 로고
    • Sar1 promotes vesicle budding from the endoplasmic reticulum but not Golgi compartments
    • Kuge O., Dascher C., Orci L. et al. Sar1 promotes vesicle budding from the endoplasmic reticulum but not Golgi compartments. J. Cell Biol. 125:1994;51-65.
    • (1994) J. Cell Biol. , vol.125 , pp. 51-65
    • Kuge, O.1    Dascher, C.2    Orci, L.3
  • 41
    • 0029019442 scopus 로고
    • Signal transduction and membrane traffic: The PITP/phosphoinositide connection
    • Liscovitch M., Cantley L.C. Signal transduction and membrane traffic: the PITP/phosphoinositide connection. Cell. 81:1995;659-662.
    • (1995) Cell , vol.81 , pp. 659-662
    • Liscovitch, M.1    Cantley, L.C.2
  • 42
    • 0030250164 scopus 로고    scopus 로고
    • Phospholipase D - Role in signal transduction and membrane traffic
    • Liscovitch M. Phospholipase D - role in signal transduction and membrane traffic. J. Lipid Med. Cell Signal. 14:1996;215-221.
    • (1996) J. Lipid Med. Cell Signal. , vol.14 , pp. 215-221
    • Liscovitch, M.1
  • 43
    • 0032557449 scopus 로고    scopus 로고
    • Cloning and initial characterization of a human phospholipase D2 (hPLD2). ADP-ribosylation factor regulates hPLD2
    • Lopez I., Arnold R.S., Lambeth J.D. Cloning and initial characterization of a human phospholipase D2 (hPLD2). ADP-ribosylation factor regulates hPLD2. J. Biol. Chem. 273:1998;12846-12852.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12846-12852
    • Lopez, I.1    Arnold, R.S.2    Lambeth, J.D.3
  • 44
    • 0024340753 scopus 로고
    • Purification of a novel class of coated vesicles mediating biosyntheting protein transport through the Golgi stack
    • Malhotra V., Serafini T., Orci L., Shepherd J.C., Rothman J.E. Purification of a novel class of coated vesicles mediating biosyntheting protein transport through the Golgi stack. Cell. 58:1989;329-336.
    • (1989) Cell , vol.58 , pp. 329-336
    • Malhotra, V.1    Serafini, T.2    Orci, L.3    Shepherd, J.C.4    Rothman, J.E.5
  • 45
    • 0027986677 scopus 로고
    • Activation of rat brain phospholipase D by ADP-ribosylation factors 1, 5, and 6: Separation of ADP-ribosylation factor-dependent and oleate-dependent enzymes
    • Massenburg D., Han J.S., Liyanage M. et al. Activation of rat brain phospholipase D by ADP-ribosylation factors 1, 5, and 6: separation of ADP-ribosylation factor-dependent and oleate-dependent enzymes. Proc. Natl. Acad. Sci. USA. 91:1994;11718-11722.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11718-11722
    • Massenburg, D.1    Han, J.S.2    Liyanage, M.3
  • 46
    • 18344405156 scopus 로고    scopus 로고
    • COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes
    • Matsuoka K., Orci L., Amherdt M. et al. COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes. Cell. 93:1998;263-275.
    • (1998) Cell , vol.93 , pp. 263-275
    • Matsuoka, K.1    Orci, L.2    Amherdt, M.3
  • 47
    • 0030861592 scopus 로고    scopus 로고
    • ADP-ribosylation-factor-regulated phospholipase D activity localizes to secretory vesicles and mobilizes to the plasma membrane following N-formylmethionyl-leucyl-phenylalanine stimulation of human neutrophils
    • Morgan C.P., Sengelov H., Whatmore J., Borregaard N., Cockcroft S. ADP-ribosylation-factor-regulated phospholipase D activity localizes to secretory vesicles and mobilizes to the plasma membrane following N-formylmethionyl-leucyl-phenylalanine stimulation of human neutrophils. Biochem. J. 325:1997;581-585.
    • (1997) Biochem. J. , vol.325 , pp. 581-585
    • Morgan, C.P.1    Sengelov, H.2    Whatmore, J.3    Borregaard, N.4    Cockcroft, S.5
  • 48
    • 0030659646 scopus 로고    scopus 로고
    • Cloning and expression of a cdna encoding a bovine brain brefeldin a sensitive guanine nucleotide-exchange protein for ADP-ribosylation factor
    • Morinaga N., Moss J., Vaughan M. Cloning and expression of a cdna encoding a bovine brain brefeldin a sensitive guanine nucleotide-exchange protein for ADP-ribosylation factor. Proc. Natl. Acad. Sci. USA. 94:1997;12926-12931.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12926-12931
    • Morinaga, N.1    Moss, J.2    Vaughan, M.3
  • 49
    • 0026744154 scopus 로고
    • Phosphatidic acid is a specific activator of phosphatidylinositol-4-phosphate kinase
    • Moritz A., De Graan P. N., Gispen W.H., Wirtz K.W. Phosphatidic acid is a specific activator of phosphatidylinositol-4-phosphate kinase. J. Biol. Chem. 267:1992;7207-7210.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7207-7210
    • Moritz, A.1    De Graan, P.N.2    Gispen, W.H.3    Wirtz, K.W.4
  • 51
    • 0024807217 scopus 로고
    • A novel GTP-binding protein, Sar1p, is involved in transport from the endoplasmic reticulum to the Golgi apparatus
    • Nakano A., Muramatsu M. A novel GTP-binding protein, Sar1p, is involved in transport from the endoplasmic reticulum to the Golgi apparatus. J. Cell Biol. 109:1989;2677-2691.
    • (1989) J. Cell Biol. , vol.109 , pp. 2677-2691
    • Nakano, A.1    Muramatsu, M.2
  • 52
    • 0028089202 scopus 로고
    • Inhibition of GTP hydrolysis by Sar1p causes accumulation of vesicles that are a functional intermediate of the ER-to-Golgi transport in yeast
    • Oka T., Nakano A. Inhibition of GTP hydrolysis by Sar1p causes accumulation of vesicles that are a functional intermediate of the ER-to-Golgi transport in yeast. J. Cell Biol. 124:1994;425-434.
    • (1994) J. Cell Biol. , vol.124 , pp. 425-434
    • Oka, T.1    Nakano, A.2
  • 53
    • 0032572560 scopus 로고    scopus 로고
    • ADP-Ribosylation factor 1 (ARF1) regulates recruitment of the AP-3 adaptor complex to membranes
    • Ooi C.E., Dell'Angelica E.C., Bonifacino J.S. ADP-Ribosylation factor 1 (ARF1) regulates recruitment of the AP-3 adaptor complex to membranes. J. Cell Biol. 142:1998;391-402.
    • (1998) J. Cell Biol. , vol.142 , pp. 391-402
    • Ooi, C.E.1    Dell'Angelica, E.C.2    Bonifacino, J.S.3
  • 54
    • 0023052287 scopus 로고
    • A new type of coated vesicular carrier that appears not to contain clathrin: Its possible role in protein transport within the Golgi stack
    • Orci L., Glick B.S., Rothman J.E. A new type of coated vesicular carrier that appears not to contain clathrin: its possible role in protein transport within the Golgi stack. Cell. 46:1986;171-184.
    • (1986) Cell , vol.46 , pp. 171-184
    • Orci, L.1    Glick, B.S.2    Rothman, J.E.3
  • 55
    • 0027291429 scopus 로고
    • Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol
    • Orcl L., Palmer D.J., Amherdt M., Rothman J.E. Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol. Nature. 364:1993;732-734.
    • (1993) Nature , vol.364 , pp. 732-734
    • Orcl, L.1    Palmer, D.J.2    Amherdt, M.3    Rothman, J.E.4
  • 56
    • 0027751666 scopus 로고
    • Stepwise assembly of functionally active transport vesicles
    • Ostermann J., Orci L., Tani K. et al. Stepwise assembly of functionally active transport vesicles. Cell. 75:1993;1015-1025.
    • (1993) Cell , vol.75 , pp. 1015-1025
    • Ostermann, J.1    Orci, L.2    Tani, K.3
  • 57
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein synthesis
    • Palade G.E. Intracellular aspects of the process of protein synthesis. Science. 189:1975;347-358.
    • (1975) Science , vol.189 , pp. 347-358
    • Palade, G.E.1
  • 58
    • 0027263507 scopus 로고
    • Binding of coatomer to Golgi membranes requires ADP-ribosylation factor
    • Palmer D.J., Helms J.B., Beckers C.J., Orci L., Rothman J.E. Binding of coatomer to Golgi membranes requires ADP-ribosylation factor. J. Biol. Chem. 268:1993;12083-12089.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12083-12089
    • Palmer, D.J.1    Helms, J.B.2    Beckers, C.J.3    Orci, L.4    Rothman, J.E.5
  • 59
    • 0030698071 scopus 로고    scopus 로고
    • Cloning and characterization of phospholipase D from rat brain
    • Park S.K., Provost J.J., Bae C.D., Ho W.T., Exton J.H. Cloning and characterization of phospholipase D from rat brain. J. Biol. Chem. 272:1997;29263-292671.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29263-292671
    • Park, S.K.1    Provost, J.J.2    Bae, C.D.3    Ho, W.T.4    Exton, J.H.5
  • 60
    • 0030760711 scopus 로고    scopus 로고
    • Diacylglycerol and phosphatidate generated by phospholipases C and D, respectively, have distinct fatty acid compositions and functions. Phospholipase D-derived diacylglycerol does not activate protein kinase C in porcine aortic endothelial cells
    • Pettitt T.R., Martin A., Horton T., Liossis C., Lord J.M., Wakelam M.J. Diacylglycerol and phosphatidate generated by phospholipases C and D, respectively, have distinct fatty acid compositions and functions. Phospholipase D-derived diacylglycerol does not activate protein kinase C in porcine aortic endothelial cells. J. Biol. Chem. 272:1997;17354-17359.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17354-17359
    • Pettitt, T.R.1    Martin, A.2    Horton, T.3    Liossis, C.4    Lord, J.M.5    Wakelam, M.J.6
  • 62
    • 0027193417 scopus 로고
    • Activation of ADP-ribosylation factor by Golgi membranes. Evidence for a brefeldin A- And protease-sensitive activating factor on Golgi membranes
    • Randazzo P.A., Yang Y.C., Rulka C., Kahn R.A. Activation of ADP-ribosylation factor by Golgi membranes. Evidence for a brefeldin A- and protease-sensitive activating factor on Golgi membranes. J. Biol. Chem. 268:1993;9555-9563.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9555-9563
    • Randazzo, P.A.1    Yang, Y.C.2    Rulka, C.3    Kahn, R.A.4
  • 63
    • 0030944208 scopus 로고    scopus 로고
    • Functional interaction of Adp-ribosylation factor 1 with phosphatidylinositol 4,5-bisphosphate
    • Randazzo P.A. Functional interaction of Adp-ribosylation factor 1 with phosphatidylinositol 4,5-bisphosphate. J. Biol. Chem. 272:1997;7688-7692.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7688-7692
    • Randazzo, P.A.1
  • 64
    • 0026627966 scopus 로고
    • Recruitment of coat proteins onto Golgi membranes in intact and permeabilized cells: Effects of brefeldin A and G protein activators
    • Robinson M.S., Kreis T.E. Recruitment of coat proteins onto Golgi membranes in intact and permeabilized cells: effects of brefeldin A and G protein activators. Cell. 69:1992;129-138.
    • (1992) Cell , vol.69 , pp. 129-138
    • Robinson, M.S.1    Kreis, T.E.2
  • 66
    • 0030747392 scopus 로고    scopus 로고
    • The role of lipid signaling in constitutive membrane traffic
    • Roth M.G., Sternweis P.C. The role of lipid signaling in constitutive membrane traffic. Curr. Opin. Cell Biol. 9:1997;519-526.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 519-526
    • Roth, M.G.1    Sternweis, P.C.2
  • 67
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman J. Mechanisms of intracellular protein transport. Nature. 372:1994;55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.1
  • 68
    • 0031856517 scopus 로고    scopus 로고
    • ADP-Ribosylation factors do not activate yeast phospholipase Ds but are required for sporulation
    • Rudge S.A., Cavenagh M.M., Kamath R. et al. ADP-Ribosylation factors do not activate yeast phospholipase Ds but are required for sporulation. Mol. Biol. Cell. 9:1998;2025-2036.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2025-2036
    • Rudge, S.A.1    Cavenagh, M.M.2    Kamath, R.3
  • 69
    • 0031918590 scopus 로고    scopus 로고
    • Relocalization of phospholipase D activity mediates membrane formation during meiosis
    • Rudge S.A., Morris A.J., Engebrecht J. Relocalization of phospholipase D activity mediates membrane formation during meiosis. J. Cell Biol. 140:1998;81-90.
    • (1998) J. Cell Biol. , vol.140 , pp. 81-90
    • Rudge, S.A.1    Morris, A.J.2    Engebrecht, J.3
  • 70
    • 0026052099 scopus 로고
    • Distribution of the intermediate elements operating in ER to Golgi transport
    • Saraste J., Svensson K. Distribution of the intermediate elements operating in ER to Golgi transport. J. Cell Sci. 100:1991;415-430.
    • (1991) J. Cell Sci. , vol.100 , pp. 415-430
    • Saraste, J.1    Svensson, K.2
  • 71
    • 0030928782 scopus 로고    scopus 로고
    • Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI
    • Scales S.J., Pepperkok R., Kreis T.E. Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI. Cell. 90:1997;1137-1148.
    • (1997) Cell , vol.90 , pp. 1137-1148
    • Scales, S.J.1    Pepperkok, R.2    Kreis, T.E.3
  • 72
    • 0029872276 scopus 로고    scopus 로고
    • Coat proteins and vesicle budding
    • Schekman R., Orci L. Coat proteins and vesicle budding. Science. 271:1996;1526-1533.
    • (1996) Science , vol.271 , pp. 1526-1533
    • Schekman, R.1    Orci, L.2
  • 73
    • 0030957355 scopus 로고    scopus 로고
    • Clathrin-coated vesicle formation and protein sorting: An integrated process
    • Schmid S.L. Clathrin-coated vesicle formation and protein sorting: an integrated process. Annu. Rev. Biochem. 66:1997;511-548.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 511-548
    • Schmid, S.L.1
  • 74
    • 0025760015 scopus 로고
    • The isolated ER-Golgi intermediate compartment exhibits properties that are different from ER and cis-Golgi
    • Schweizer A., Matter K., Ketcham C.M., Hauri H.P. The isolated ER-Golgi intermediate compartment exhibits properties that are different from ER and cis-Golgi. J. Cell Biol. 113:1991;45-54.
    • (1991) J. Cell Biol. , vol.113 , pp. 45-54
    • Schweizer, A.1    Matter, K.2    Ketcham, C.M.3    Hauri, H.P.4
  • 75
    • 0029795180 scopus 로고    scopus 로고
    • Cytosolic and membrane-associated proteins involved in the recruitment of AP-1 adaptors onto the trans-Golgi network
    • Seaman M.N.J., Sowerby P.J., Robinson M.S. Cytosolic and membrane-associated proteins involved in the recruitment of AP-1 adaptors onto the trans-Golgi network. J. Biol. Chem. 271:1996;25446-25451.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25446-25451
    • Seaman, M.N.J.1    Sowerby, P.J.2    Robinson, M.S.3
  • 76
    • 0026001029 scopus 로고
    • ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: A novel role for a GTP-binding protein
    • Serafini T., Orci L., Amherdt M., Brunner M., Kahn R.A., Rothman J.E. ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein. Cell. 67:1991;239-253.
    • (1991) Cell , vol.67 , pp. 239-253
    • Serafini, T.1    Orci, L.2    Amherdt, M.3    Brunner, M.4    Kahn, R.A.5    Rothman, J.E.6
  • 77
    • 0028966452 scopus 로고
    • Human SEC13Rp functions in yeast and is located on transport vesicles budding from the endoplasmic reticulum
    • Shaywitz D.A., Orci L., Ravazzola M., Swaroop A., Kaiser C.A. Human SEC13Rp functions in yeast and is located on transport vesicles budding from the endoplasmic reticulum. J. Cell Biol. 128:1995;769-777.
    • (1995) J. Cell Biol. , vol.128 , pp. 769-777
    • Shaywitz, D.A.1    Orci, L.2    Ravazzola, M.3    Swaroop, A.4    Kaiser, C.A.5
  • 78
    • 0029020350 scopus 로고
    • Resolved phospholipase D activity is modulated by cytosolic factors other than Arf
    • Singer W.D., Brown H.A., Bokoch G.M., Sternweis P.C. Resolved phospholipase D activity is modulated by cytosolic factors other than Arf. J. Biol. Chem. 270:1995;14944-14950.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14944-14950
    • Singer, W.D.1    Brown, H.A.2    Bokoch, G.M.3    Sternweis, P.C.4
  • 79
    • 0030907067 scopus 로고    scopus 로고
    • Regulation of eukaryotic phosphatidylinositol-specific phospholipase C and phospholipase D
    • Singer W.D., Brown H., Sternweis P. C. Regulation of eukaryotic phosphatidylinositol-specific phospholipase C and phospholipase D. Annu. Rev. Biochem. 66:1997;475-509.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 475-509
    • Singer, W.D.1    Brown, H.2    Sternweis, P.C.3
  • 80
    • 0032530193 scopus 로고    scopus 로고
    • Coatomer, Arf1p, and nucleotide are required to bud COPI-coated vesicles from large synthetic liposomes
    • Spang A., Matsuoka K., Hamamoto S., Schekman R., Orci L. Coatomer, Arf1p, and nucleotide are required to bud COPI-coated vesicles from large synthetic liposomes. Proc. Natl. Acad. Sci. USA. 95:1998;11199-11204.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11199-11204
    • Spang, A.1    Matsuoka, K.2    Hamamoto, S.3    Schekman, R.4    Orci, L.5
  • 81
    • 0027155088 scopus 로고
    • The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein
    • Stamnes M.A., Rothman J.E. The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein. Cell. 73:1993;999-1005.
    • (1993) Cell , vol.73 , pp. 999-1005
    • Stamnes, M.A.1    Rothman, J.E.2
  • 82
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle - A cascade of protein-protein interactions
    • Sudhof T.C. The synaptic vesicle cycle - a cascade of protein-protein interactions. Nature. 375:1995;645-653.
    • (1995) Nature , vol.375 , pp. 645-653
    • Sudhof, T.C.1
  • 83
    • 0027724473 scopus 로고
    • Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles
    • Tanigawa G., Orci L., Amherdt M., Ravazzola M., Helms J.B., Rothman J.E. Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles. J. Cell Biol. 123:1993;1365-1371.
    • (1993) J. Cell Biol. , vol.123 , pp. 1365-1371
    • Tanigawa, G.1    Orci, L.2    Amherdt, M.3    Ravazzola, M.4    Helms, J.B.5    Rothman, J.E.6
  • 85
    • 0039265562 scopus 로고    scopus 로고
    • Cooperativity of phosphatidylinositol transfer protein and phospholipase d in secretory vesicle formation from the TGN-phosphoinositides as a common denominator
    • Tuscher O., Lorra C., Bouma B., Wirtz K.W.A., Huttner W.B. Cooperativity of phosphatidylinositol transfer protein and phospholipase d in secretory vesicle formation from the TGN-phosphoinositides as a common denominator. FEBS Lett. 419:1997;271-275.
    • (1997) FEBS Lett. , vol.419 , pp. 271-275
    • Tuscher, O.1    Lorra, C.2    Bouma, B.3    Wirtz, K.W.A.4    Huttner, W.B.5
  • 86
    • 0025957468 scopus 로고
    • 'Coatomer': A cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles
    • Waters M.G., Serafini T., Rothman J.E. 'Coatomer': a cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles. Nature. 349:1991;248-251.
    • (1991) Nature , vol.349 , pp. 248-251
    • Waters, M.G.1    Serafini, T.2    Rothman, J.E.3
  • 87
    • 0032079523 scopus 로고    scopus 로고
    • Protein kinase B and rac are activated in parallel within a phosphatidylinositide 30H-kinase-controlled signaling pathway
    • Welch H., Eguinoa A., Stephens L.R., Hawkins P.T. Protein kinase B and rac are activated in parallel within a phosphatidylinositide 30H-kinase-controlled signaling pathway. J. Biol. Chem. 273:1998;11248-11256.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11248-11256
    • Welch, H.1    Eguinoa, A.2    Stephens, L.R.3    Hawkins, P.T.4
  • 88
    • 0030881255 scopus 로고    scopus 로고
    • The role of ADP-ribosylation factor and phospholipase D in adaptor recruitment
    • West M.A., Bright N.A., Robinson M.S. The role of ADP-ribosylation factor and phospholipase D in adaptor recruitment. J. Cell Biol. 138:1997;1239-1254.
    • (1997) J. Cell Biol. , vol.138 , pp. 1239-1254
    • West, M.A.1    Bright, N.A.2    Robinson, M.S.3
  • 89
    • 0030458832 scopus 로고    scopus 로고
    • ADP-ribosylation factor 1-regulated phospholipase D activity is localized at the plasma membrane and intracellular organelles in HL60 cells
    • Whatmore J., Morgan C.P., Cunningham E., Collison K.S., Willison K.R., Cockcroft S. ADP-ribosylation factor 1-regulated phospholipase D activity is localized at the plasma membrane and intracellular organelles in HL60 cells. Biochem. J. 320:1996;785-794.
    • (1996) Biochem. J. , vol.320 , pp. 785-794
    • Whatmore, J.1    Morgan, C.P.2    Cunningham, E.3    Collison, K.S.4    Willison, K.R.5    Cockcroft, S.6
  • 92
    • 0032584676 scopus 로고    scopus 로고
    • A family of Arf effectors defined as suppressors of the loss of Arf function in the yeast Saccharomyces cerevisiae
    • Zhang C.J., Cavenagh M.M., Kahn R.A. A family of Arf effectors defined as suppressors of the loss of Arf function in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 273:1998;19792-19796.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19792-19796
    • Zhang, C.J.1    Cavenagh, M.M.2    Kahn, R.A.3
  • 93
    • 0030984537 scopus 로고    scopus 로고
    • Direct and GTP-dependent interaction of ADP ribosylation factor 1 with coatomer subunit beta
    • Zhao L., Helms J., Brugger B. et al. Direct and GTP-dependent interaction of ADP ribosylation factor 1 with coatomer subunit beta. Proc Natl Acad Sci USA. 94:1997;4418-4423.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4418-4423
    • Zhao, L.1    Helms, J.2    Brugger, B.3


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