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Volumn 583, Issue 23, 2009, Pages 3758-3763

Mechanisms of COPI vesicle formation

Author keywords

ADP ribosylation factor 1; ADP ribosylation factor GTPase activating protein 1; Brefeldin A ADP ribosylated substrate; Coat Protein I; Coatomer; Golgi specific brefeldin A resistant guanine nucleotide exchange factor 1

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR 1; CELL PROTEIN; COAT PROTEIN COMPLEX I; COATOMER PROTEIN; FISSION PROTEIN; GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; LIPID; UNCLASSIFIED DRUG;

EID: 70450223889     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.10.056     Document Type: Review
Times cited : (39)

References (58)
  • 1
    • 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., and 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
  • 2
    • 0024340753 scopus 로고
    • Purification of a novel class of coated vesicles mediating biosynthetic protein transport through the Golgi stack
    • Malhotra V., Serafini T., Orci L., Shepherd J.C., and Rothman J.E. Purification of a novel class of coated vesicles mediating biosynthetic 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
  • 3
    • 0026069437 scopus 로고
    • A coat subunit of Golgi-derived non-clathrin-coated vesicles with homology to the clathrin-coated vesicle coat protein beta-adaptin
    • Serafini T., Stenbeck G., Brecht A., Lottspeich F., Orci L., Rothman J.E., and Wieland F.T. A coat subunit of Golgi-derived non-clathrin-coated vesicles with homology to the clathrin-coated vesicle coat protein beta-adaptin. Nature 349 (1991) 215-220
    • (1991) Nature , vol.349 , pp. 215-220
    • Serafini, T.1    Stenbeck, G.2    Brecht, A.3    Lottspeich, F.4    Orci, L.5    Rothman, J.E.6    Wieland, F.T.7
  • 4
    • 0026034357 scopus 로고
    • Beta-COP, a 110 kd protein associated with non-clathrin-coated vesicles and the Golgi complex, shows homology to beta-adaptin
    • Duden R., Griffiths G., Frank R., Argos P., and Kreis T.E. Beta-COP, a 110 kd protein associated with non-clathrin-coated vesicles and the Golgi complex, shows homology to beta-adaptin. Cell 64 (1991) 649-665
    • (1991) Cell , vol.64 , pp. 649-665
    • Duden, R.1    Griffiths, G.2    Frank, R.3    Argos, P.4    Kreis, T.E.5
  • 6
    • 0027274897 scopus 로고
    • A 102 kDa subunit of a Golgi-associated particle has homology to beta subunits of trimeric G proteins
    • Harrison-Lavoie K.J., Lewis V.A., Hynes G.M., Collison K.S., Nutland E., and Willison K.R. A 102 kDa subunit of a Golgi-associated particle has homology to beta subunits of trimeric G proteins. EMBO J. 12 (1993) 2847-2853
    • (1993) EMBO J. , vol.12 , pp. 2847-2853
    • Harrison-Lavoie, K.J.1    Lewis, V.A.2    Hynes, G.M.3    Collison, K.S.4    Nutland, E.5    Willison, K.R.6
  • 7
    • 0025957468 scopus 로고
    • 'Coatomer': a cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles
    • Waters M.G., Serafini T., and 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
  • 8
    • 28444472038 scopus 로고    scopus 로고
    • Opinion: the maturing role of COPI vesicles in intra-Golgi transport
    • Rabouille C., and Klumperman J. Opinion: the maturing role of COPI vesicles in intra-Golgi transport. Nat. Rev. Mol. Cell Biol. 6 (2005) 812-817
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 812-817
    • Rabouille, C.1    Klumperman, J.2
  • 9
    • 67349283054 scopus 로고    scopus 로고
    • The evolving understanding of COPI vesicle formation
    • Hsu V.W., Lee S.Y., and Yang J.S. The evolving understanding of COPI vesicle formation. Nat. Rev. Mol. Cell Biol. 10 (2009) 360-364
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 360-364
    • Hsu, V.W.1    Lee, S.Y.2    Yang, J.S.3
  • 10
    • 0026623115 scopus 로고
    • ADP-ribosylation factor, a small GTP-binding protein, is required for binding of the coatomer protein beta-COP to Golgi membranes
    • Donaldson J.G., Cassel D., Kahn R.A., and Klausner R.D. ADP-ribosylation factor, a small GTP-binding protein, is required for binding of the coatomer protein beta-COP to Golgi membranes. Proc. Natl. Acad. Sci. USA 89 (1992) 6408-6412
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6408-6412
    • Donaldson, J.G.1    Cassel, D.2    Kahn, R.A.3    Klausner, R.D.4
  • 11
    • 0026677375 scopus 로고
    • Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein
    • Donaldson J.G., Finazzi D., and 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
  • 12
    • 0026746713 scopus 로고
    • Inhibition by brefeldin A of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF
    • Helms J.B., and 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
  • 13
    • 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., and 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
  • 14
    • 0029416828 scopus 로고
    • The ARF1-GTPase-activating protein: zinc finger motif and Golgi complex localization
    • Cukierman E., Huber I., Rotman M., and 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
  • 15
    • 0033582917 scopus 로고    scopus 로고
    • Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis
    • Goldberg J. Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis. Cell 96 (1999) 893-902
    • (1999) Cell , vol.96 , pp. 893-902
    • Goldberg, J.1
  • 16
    • 0034677633 scopus 로고    scopus 로고
    • Decoding of sorting signals by coatomer through a GTPase switch in the COPI coat complex
    • Goldberg J. Decoding of sorting signals by coatomer through a GTPase switch in the COPI coat complex. Cell 100 (2000) 671-679
    • (2000) Cell , vol.100 , pp. 671-679
    • Goldberg, J.1
  • 17
    • 0035945347 scopus 로고    scopus 로고
    • Sorting of Golgi resident proteins into different subpopulations of COPI vesicles: a role for ArfGAP1
    • Lanoix J., Ouwendijk J., Stark A., Szafer E., Cassel D., Dejgaard K., Weiss M., and Nilsson T. Sorting of Golgi resident proteins into different subpopulations of COPI vesicles: a role for ArfGAP1. J. Cell Biol. 155 (2001) 1199-1212
    • (2001) J. Cell Biol. , vol.155 , pp. 1199-1212
    • Lanoix, J.1    Ouwendijk, J.2    Stark, A.3    Szafer, E.4    Cassel, D.5    Dejgaard, K.6    Weiss, M.7    Nilsson, T.8
  • 18
    • 0037078331 scopus 로고    scopus 로고
    • ARFGAP1 promotes the formation of COPI vesicles, suggesting function as a component of the coat
    • Yang J.S., Lee S.Y., Gao M., Bourgoin S., Randazzo P.A., Premont R.T., and Hsu V.W. ARFGAP1 promotes the formation of COPI vesicles, suggesting function as a component of the coat. J. Cell Biol. 159 (2002) 69-78
    • (2002) J. Cell Biol. , vol.159 , pp. 69-78
    • Yang, J.S.1    Lee, S.Y.2    Gao, M.3    Bourgoin, S.4    Randazzo, P.A.5    Premont, R.T.6    Hsu, V.W.7
  • 19
    • 13844269329 scopus 로고    scopus 로고
    • ARFGAP1 plays a central role in coupling COPI cargo sorting with vesicle formation
    • Lee S.Y., Yang J.S., Hong W., Premont R.T., and Hsu V.W. ARFGAP1 plays a central role in coupling COPI cargo sorting with vesicle formation. J. Cell Biol. 168 (2005) 281-290
    • (2005) J. Cell Biol. , vol.168 , pp. 281-290
    • Lee, S.Y.1    Yang, J.S.2    Hong, W.3    Premont, R.T.4    Hsu, V.W.5
  • 20
    • 0028233498 scopus 로고
    • COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum
    • Barlowe C., et al. COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum. Cell 77 (1994) 895-907
    • (1994) Cell , vol.77 , pp. 895-907
    • Barlowe, C.1
  • 21
    • 0346756190 scopus 로고    scopus 로고
    • Lipid packing sensed by ArfGAP1 couples COPI coat disassembly to membrane bilayer curvature
    • Bigay J., Gounon P., Robineau S., and Antonny B. Lipid packing sensed by ArfGAP1 couples COPI coat disassembly to membrane bilayer curvature. Nature 426 (2003) 563-566
    • (2003) Nature , vol.426 , pp. 563-566
    • Bigay, J.1    Gounon, P.2    Robineau, S.3    Antonny, B.4
  • 22
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodelling
    • McMahon H.T., and Gallop J.L. Membrane curvature and mechanisms of dynamic cell membrane remodelling. Nature 438 (2005) 590-596
    • (2005) Nature , vol.438 , pp. 590-596
    • McMahon, H.T.1    Gallop, J.L.2
  • 23
    • 33644846421 scopus 로고    scopus 로고
    • How proteins produce cellular membrane curvature
    • Zimmerberg J., and Kozlov M.M. How proteins produce cellular membrane curvature. Nat. Rev. Mol. Cell Biol. 7 (2006) 9-19
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 9-19
    • Zimmerberg, J.1    Kozlov, M.M.2
  • 24
    • 0029147574 scopus 로고
    • An integral membrane component of coatomer-coated transport vesicles defines a family of proteins involved in budding [published erratum appears in Proc Natl Acad Sci USA 1995 Nov 7;92(23):10816]
    • Stamnes M.A., Craighead M.W., Hoe M.H., Lampen N., Geromanos S., Tempst P., and Rothman J.E. An integral membrane component of coatomer-coated transport vesicles defines a family of proteins involved in budding [published erratum appears in Proc Natl Acad Sci USA 1995 Nov 7;92(23):10816]. Proc. Natl. Acad. Sci. USA 92 (1995) 8011-8015
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8011-8015
    • Stamnes, M.A.1    Craighead, M.W.2    Hoe, M.H.3    Lampen, N.4    Geromanos, S.5    Tempst, P.6    Rothman, J.E.7
  • 25
    • 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., and 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
  • 26
    • 0032530193 scopus 로고    scopus 로고
    • Coatomer, Arf1p, and nucleotide are required to bud coat protein complex I-coated vesicles from large synthetic liposomes
    • Spang A., Matsuoka K., Hamamoto S., Schekman R., and Orci L. Coatomer, Arf1p, and nucleotide are required to bud coat protein complex I-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
  • 27
    • 0033582648 scopus 로고    scopus 로고
    • Coupling of coat assembly and vesicle budding to packaging of putative cargo receptors
    • Bremser M., et al. Coupling of coat assembly and vesicle budding to packaging of putative cargo receptors. Cell 96 (1999) 495-506
    • (1999) Cell , vol.96 , pp. 495-506
    • Bremser, M.1
  • 28
    • 0038492465 scopus 로고    scopus 로고
    • Functional reconstitution of COPI coat assembly and disassembly using chemically defined components
    • Reinhard C., Schweikert M., Wieland F.T., and Nickel W. Functional reconstitution of COPI coat assembly and disassembly using chemically defined components. Proc. Natl. Acad. Sci. USA 100 (2003) 8253-8257
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8253-8257
    • Reinhard, C.1    Schweikert, M.2    Wieland, F.T.3    Nickel, W.4
  • 29
    • 35348885467 scopus 로고    scopus 로고
    • Two human ARFGAPs associated with COP-I-coated vesicles
    • Frigerio G., Grimsey N., Dale M., Majoul I., and Duden R. Two human ARFGAPs associated with COP-I-coated vesicles. Traffic 8 (2007) 1644-1655
    • (2007) Traffic , vol.8 , pp. 1644-1655
    • Frigerio, G.1    Grimsey, N.2    Dale, M.3    Majoul, I.4    Duden, R.5
  • 32
    • 0029851773 scopus 로고    scopus 로고
    • Nucleotide exchange on ARF mediated by yeast Gea1 protein
    • Peyroche A., Paris S., and Jackson C.L. Nucleotide exchange on ARF mediated by yeast Gea1 protein. Nature 384 (1996) 479-481
    • (1996) Nature , vol.384 , pp. 479-481
    • Peyroche, A.1    Paris, S.2    Jackson, C.L.3
  • 34
    • 0033549576 scopus 로고    scopus 로고
    • GBF1: a novel Golgi-associated BFA-resistant guanine nucleotide exchange factor that displays specificity for ADP-ribosylation factor 5
    • Claude A., et al. GBF1: a novel Golgi-associated BFA-resistant guanine nucleotide exchange factor that displays specificity for ADP-ribosylation factor 5. J. Cell Biol. 146 (1999) 71-84
    • (1999) J. Cell Biol. , vol.146 , pp. 71-84
    • Claude, A.1
  • 35
    • 0036017789 scopus 로고    scopus 로고
    • GBF1, a guanine nucleotide exchange factor for ADP-ribosylation factors, is localized to the cis-Golgi and involved in membrane association of the COPI coat
    • Kawamoto K., Yoshida Y., Tamaki H., Torii S., Shinotsuka C., Yamashina S., and Nakayama K. GBF1, a guanine nucleotide exchange factor for ADP-ribosylation factors, is localized to the cis-Golgi and involved in membrane association of the COPI coat. Traffic 3 (2002) 483-495
    • (2002) Traffic , vol.3 , pp. 483-495
    • Kawamoto, K.1    Yoshida, Y.2    Tamaki, H.3    Torii, S.4    Shinotsuka, C.5    Yamashina, S.6    Nakayama, K.7
  • 36
    • 17344391184 scopus 로고    scopus 로고
    • ADP-ribosylation factor/COPI-dependent events at the endoplasmic reticulum-Golgi interface are regulated by the guanine nucleotide exchange factor GBF1
    • Garcia-Mata R., Szul T., Alvarez C., and Sztul E. ADP-ribosylation factor/COPI-dependent events at the endoplasmic reticulum-Golgi interface are regulated by the guanine nucleotide exchange factor GBF1. Mol. Biol. Cell 14 (2003) 2250-2261
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2250-2261
    • Garcia-Mata, R.1    Szul, T.2    Alvarez, C.3    Sztul, E.4
  • 37
    • 14844333247 scopus 로고    scopus 로고
    • Dynamics of GBF1, a brefeldin A-sensitive Arf1 exchange factor at the Golgi
    • Niu T.K., Pfeifer A.C., Lippincott-Schwartz J., and Jackson C.L. Dynamics of GBF1, a brefeldin A-sensitive Arf1 exchange factor at the Golgi. Mol. Biol. Cell 16 (2005) 1213-1222
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1213-1222
    • Niu, T.K.1    Pfeifer, A.C.2    Lippincott-Schwartz, J.3    Jackson, C.L.4
  • 38
    • 58049099709 scopus 로고    scopus 로고
    • A COPI coat subunit interacts directly with an early-Golgi localized Arf exchange factor
    • Deng Y., Golinelli-Cohen M.P., Smirnova E., and Jackson C.L. A COPI coat subunit interacts directly with an early-Golgi localized Arf exchange factor. EMBO Rep. 10 (2009) 58-64
    • (2009) EMBO Rep. , vol.10 , pp. 58-64
    • Deng, Y.1    Golinelli-Cohen, M.P.2    Smirnova, E.3    Jackson, C.L.4
  • 39
    • 28644440953 scopus 로고    scopus 로고
    • A role for BARS at the fission step of COPI vesicle formation from Golgi membrane
    • Yang J.S., et al. A role for BARS at the fission step of COPI vesicle formation from Golgi membrane. EMBO J. 24 (2005) 4133-4143
    • (2005) EMBO J. , vol.24 , pp. 4133-4143
    • Yang, J.S.1
  • 41
    • 0028014643 scopus 로고
    • Stimulation of endogenous ADP-ribosylation by brefeldin A
    • De Matteis M.A., et al. Stimulation of endogenous ADP-ribosylation by brefeldin A. Proc. Natl. Acad. Sci. USA 91 (1994) 1114-1118
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1114-1118
    • De Matteis, M.A.1
  • 42
    • 0033580845 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of brefeldin A-ADP-ribosylated substrate. A novel protein involved in the maintenance of the Golgi structure
    • Spano S., et al. Molecular cloning and functional characterization of brefeldin A-ADP-ribosylated substrate. A novel protein involved in the maintenance of the Golgi structure. J. Biol. Chem. 274 (1999) 17705-17710
    • (1999) J. Biol. Chem. , vol.274 , pp. 17705-17710
    • Spano, S.1
  • 43
    • 0036314926 scopus 로고    scopus 로고
    • Overlapping and unique roles for C-terminal binding protein 1 (CtBP1) and CtBP2 during mouse development
    • Hildebrand J.D., and Soriano P. Overlapping and unique roles for C-terminal binding protein 1 (CtBP1) and CtBP2 during mouse development. Mol. Cell Biol. 22 (2002) 5296-5307
    • (2002) Mol. Cell Biol. , vol.22 , pp. 5296-5307
    • Hildebrand, J.D.1    Soriano, P.2
  • 44
    • 0028264318 scopus 로고
    • Disruptions in Golgi structure and membrane traffic in a conditional lethal mammalian cell mutant are corrected by epsilon-COP
    • Guo Q., Vasile E., and Krieger M. Disruptions in Golgi structure and membrane traffic in a conditional lethal mammalian cell mutant are corrected by epsilon-COP. J. Cell Biol. 125 (1994) 1213-1224
    • (1994) J. Cell Biol. , vol.125 , pp. 1213-1224
    • Guo, Q.1    Vasile, E.2    Krieger, M.3
  • 46
    • 0033604565 scopus 로고    scopus 로고
    • CtBP/BARS induces fission of Golgi membranes by acylating lysophosphatidic acid
    • Weigert R., et al. CtBP/BARS induces fission of Golgi membranes by acylating lysophosphatidic acid. Nature 402 (1999) 429-433
    • (1999) Nature , vol.402 , pp. 429-433
    • Weigert, R.1
  • 47
    • 28444437745 scopus 로고    scopus 로고
    • Endophilin and CtBP/BARS are not acyl transferases in endocytosis or Golgi fission
    • Gallop J.L., Butler P.J., and McMahon H.T. Endophilin and CtBP/BARS are not acyl transferases in endocytosis or Golgi fission. Nature 438 (2005) 675-678
    • (2005) Nature , vol.438 , pp. 675-678
    • Gallop, J.L.1    Butler, P.J.2    McMahon, H.T.3
  • 48
    • 53349165606 scopus 로고    scopus 로고
    • A role for phosphatidic acid in COPI vesicle fission yields insights into Golgi maintenance
    • Yang J.S., et al. A role for phosphatidic acid in COPI vesicle fission yields insights into Golgi maintenance. Nat. Cell Biol. 10 (2008) 1146-1153
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1146-1153
    • Yang, J.S.1
  • 49
    • 34548496498 scopus 로고    scopus 로고
    • Diacylglycerol is required for the formation of COPI vesicles in the Golgi-to-ER transport pathway
    • Fernandez-Ulibarri I., et al. Diacylglycerol is required for the formation of COPI vesicles in the Golgi-to-ER transport pathway. Mol. Biol. Cell 18 (2007) 3250-3263
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3250-3263
    • Fernandez-Ulibarri, I.1
  • 50
    • 64049104855 scopus 로고    scopus 로고
    • Early stages of Golgi vesicle and tubule formation require diacylglycerol
    • Asp L., et al. Early stages of Golgi vesicle and tubule formation require diacylglycerol. Mol. Biol. Cell 20 (2009) 780-790
    • (2009) Mol. Biol. Cell , vol.20 , pp. 780-790
    • Asp, L.1
  • 51
    • 0027153957 scopus 로고
    • Two distinct populations of ARF bound to Golgi membranes
    • Helms J.B., Palmer D.J., and Rothman J.E. Two distinct populations of ARF bound to Golgi membranes. J. Cell Biol. 121 (1993) 751-760
    • (1993) J. Cell Biol. , vol.121 , pp. 751-760
    • Helms, J.B.1    Palmer, D.J.2    Rothman, J.E.3
  • 52
    • 58149177285 scopus 로고    scopus 로고
    • Structure and membrane interaction of myristoylated ARF1
    • Liu Y., Kahn R.A., and Prestegard J.H. Structure and membrane interaction of myristoylated ARF1. Structure 17 (2009) 79-87
    • (2009) Structure , vol.17 , pp. 79-87
    • Liu, Y.1    Kahn, R.A.2    Prestegard, J.H.3
  • 53
    • 23944488301 scopus 로고    scopus 로고
    • Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle
    • Lee M.C., Orci L., Hamamoto S., Futai E., Ravazzola M., and Schekman R. Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle. Cell 122 (2005) 605-617
    • (2005) Cell , vol.122 , pp. 605-617
    • Lee, M.C.1    Orci, L.2    Hamamoto, S.3    Futai, E.4    Ravazzola, M.5    Schekman, R.6
  • 54
    • 29144454715 scopus 로고    scopus 로고
    • Regulation of Sar1 NH2 terminus by GTP binding and hydrolysis promotes membrane deformation to control COPII vesicle fission
    • Bielli A., Haney C.J., Gabreski G., Watkins S.C., Bannykh S.I., and Aridor M. Regulation of Sar1 NH2 terminus by GTP binding and hydrolysis promotes membrane deformation to control COPII vesicle fission. J. Cell Biol. 171 (2005) 919-924
    • (2005) J. Cell Biol. , vol.171 , pp. 919-924
    • Bielli, A.1    Haney, C.J.2    Gabreski, G.3    Watkins, S.C.4    Bannykh, S.I.5    Aridor, M.6
  • 55
    • 50149083446 scopus 로고    scopus 로고
    • Membrane curvature induced by Arf1-GTP is essential for vesicle formation
    • Beck R., et al. Membrane curvature induced by Arf1-GTP is essential for vesicle formation. Proc. Natl. Acad. Sci. USA 105 (2008) 11731-11736
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 11731-11736
    • Beck, R.1
  • 56
    • 55549125212 scopus 로고    scopus 로고
    • Arf1-GTP-induced tubule formation suggests a function of Arf family proteins in curvature acquisition at sites of vesicle budding
    • Krauss M., Jia J.Y., Roux A., Beck R., Wieland F.T., De Camilli P., and Haucke V. Arf1-GTP-induced tubule formation suggests a function of Arf family proteins in curvature acquisition at sites of vesicle budding. J. Biol. Chem. 283 (2008) 27717-27723
    • (2008) J. Biol. Chem. , vol.283 , pp. 27717-27723
    • Krauss, M.1    Jia, J.Y.2    Roux, A.3    Beck, R.4    Wieland, F.T.5    De Camilli, P.6    Haucke, V.7
  • 57
    • 50949133967 scopus 로고    scopus 로고
    • Arf family GTP loading is activated by, and generates, positive membrane curvature
    • Lundmark R., Doherty G.J., Vallis Y., Peter B.J., and McMahon H.T. Arf family GTP loading is activated by, and generates, positive membrane curvature. Biochem. J. 414 (2008) 189-194
    • (2008) Biochem. J. , vol.414 , pp. 189-194
    • Lundmark, R.1    Doherty, G.J.2    Vallis, Y.3    Peter, B.J.4    McMahon, H.T.5
  • 58
    • 55949131570 scopus 로고    scopus 로고
    • COPI coat assembly occurs on liquid-disordered domains and the associated membrane deformations are limited by membrane tension
    • Manneville J.B., et al. COPI coat assembly occurs on liquid-disordered domains and the associated membrane deformations are limited by membrane tension. Proc. Natl. Acad. Sci. USA 105 (2008) 16946-16951
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 16946-16951
    • Manneville, J.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.