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Volumn 310, Issue 6, 2016, Pages C456-C469

Oligomerization of the Sec7 domain Arf guanine nucleotide exchange factor GBF1 is dispensable for Golgi localization and function but regulates degradation

Author keywords

ADP ribosylation factors; GBF1; Golgi; Membrane trafficking; Oligomerization; Sec7 guanine nucleotide exchange factor

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR; ARF PROTEIN; COAT PROTEIN COMPLEX I; GUANINE NUCLEOTIDE EXCHANGE FACTOR; VIRUS RNA; GBF1 PROTEIN, HUMAN; PROTEIN BINDING;

EID: 84983685001     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00185.2015     Document Type: Article
Times cited : (19)

References (62)
  • 1
    • 0033552616 scopus 로고    scopus 로고
    • ER to Golgi transport: Requirement for p115 at a pre-Golgi VTC stage
    • Alvarez C, Fujita H, Hubbard A, Sztul E. ER to Golgi transport: requirement for p115 at a pre-Golgi VTC stage. J Cell Biol 147: 1205–1222, 1999.
    • (1999) J Cell Biol , vol.147 , pp. 1205-1222
    • Alvarez, C.1    Fujita, H.2    Hubbard, A.3    Sztul, E.4
  • 2
    • 55549089615 scopus 로고    scopus 로고
    • Large ARF guanine nucleotide exchange factors in membrane trafficking
    • Anders N, Jurgens G. Large ARF guanine nucleotide exchange factors in membrane trafficking. Cell Mol Life Sci 65: 3433–3445, 2008.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 3433-3445
    • Anders, N.1    Jurgens, G.2
  • 3
    • 68149124204 scopus 로고    scopus 로고
    • Structural effects of a dimer interface mutation on catalytic activity of triosephosphate isomerase. The role of conserved residues and complementary mutations
    • Banerjee M, Balaram H, Balaram P. Structural effects of a dimer interface mutation on catalytic activity of triosephosphate isomerase. The role of conserved residues and complementary mutations. FEBS J 276: 4169–4183, 2009.
    • (2009) FEBS J , vol.276 , pp. 4169-4183
    • Banerjee, M.1    Balaram, H.2    Balaram, P.3
  • 4
    • 0032526720 scopus 로고    scopus 로고
    • Mapping the interaction between GRASP65 and GM130, components of a protein complex involved in the stacking of Golgi cisternae
    • Barr FA, Nakamura N, Warren G. Mapping the interaction between GRASP65 and GM130, components of a protein complex involved in the stacking of Golgi cisternae. EMBO J 17: 3258–3268, 1998.
    • (1998) EMBO J , vol.17 , pp. 3258-3268
    • Barr, F.A.1    Nakamura, N.2    Warren, G.3
  • 6
    • 57149096870 scopus 로고    scopus 로고
    • A critical role of a cellular membrane traffic protein in poliovirus RNA replication
    • Belov GA, Feng Q, Nikovics K, Jackson CL, Ehrenfeld E. A critical role of a cellular membrane traffic protein in poliovirus RNA replication. PLoS Pathog 4: e1000216, 2008.
    • (2008) Plos Pathog , vol.4
    • Belov, G.A.1    Feng, Q.2    Nikovics, K.3    Jackson, C.L.4    Ehrenfeld, E.5
  • 7
    • 78249237877 scopus 로고    scopus 로고
    • Poliovirus replication requires the N-terminus but not the catalytic Sec7 domain of ArfGEF GBF1
    • Belov GA, Kovtunovych G, Jackson CL, Ehrenfeld E. Poliovirus replication requires the N-terminus but not the catalytic Sec7 domain of ArfGEF GBF1. Cell Microbiol 12: 1463–1479, 2010.
    • (2010) Cell Microbiol , vol.12 , pp. 1463-1479
    • Belov, G.A.1    Kovtunovych, G.2    Jackson, C.L.3    Ehrenfeld, E.4
  • 8
    • 84907928930 scopus 로고    scopus 로고
    • Rewiring of cellular membrane homeostasis by picornaviruses
    • Belov GA, Sztul E. Rewiring of cellular membrane homeostasis by picornaviruses. J Virol 88: 9478–9489, 2014.
    • (2014) J Virol , vol.88 , pp. 9478-9489
    • Belov, G.A.1    Sztul, E.2
  • 10
    • 78349242595 scopus 로고    scopus 로고
    • Specific functions of BIG1 and BIG2 in endomembrane organization
    • Boal F, Stephens DJ. Specific functions of BIG1 and BIG2 in endomembrane organization. PLoS One 5: e9898, 2010.
    • (2010) Plos One , vol.5
    • Boal, F.1    Stephens, D.J.2
  • 11
    • 84869222520 scopus 로고    scopus 로고
    • A potential peptide therapeutic derived from the juxtamembrane domain of the epidermal growth factor receptor
    • Boran AD, Seco J, Jayaraman V, Jayaraman G, Zhao S, Reddy S, Chen Y, Iyengar R. A potential peptide therapeutic derived from the juxtamembrane domain of the epidermal growth factor receptor. PLoS One 7: e49702, 2012.
    • (2012) Plos One , vol.7
    • Boran, A.D.1    Seco, J.2    Jayaraman, V.3    Jayaraman, G.4    Zhao, S.5    Reddy, S.6    Chen, Y.7    Iyengar, R.8
  • 12
    • 70350070478 scopus 로고    scopus 로고
    • Large Arf1 guanine nucleotide exchange factors: Evolution, domain structure, and roles in membrane trafficking and human disease
    • Bui QT, Golinelli-Cohen MP, Jackson CL. Large Arf1 guanine nucleotide exchange factors: evolution, domain structure, and roles in membrane trafficking and human disease. Mol Genet Genomics 282: 329–350, 2009.
    • (2009) Mol Genet Genomics , vol.282 , pp. 329-350
    • Bui, Q.T.1    Golinelli-Cohen, M.P.2    Jackson, C.L.3
  • 13
  • 15
    • 23044502309 scopus 로고    scopus 로고
    • Cog1p plays a central role in the organization of the yeast conserved oligomeric Golgi complex
    • Fotso P, Koryakina Y, Pavliv O, Tsiomenko AB, Lupashin VV. Cog1p plays a central role in the organization of the yeast conserved oligomeric Golgi complex. J Biol Chem 280: 27613–27623, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 27613-27623
    • Fotso, P.1    Koryakina, Y.2    Pavliv, O.3    Tsiomenko, A.B.4    Lupashin, V.V.5
  • 16
    • 0032509448 scopus 로고    scopus 로고
    • Molecular cloning, characterization, and dynamics of rat formiminotransferase cyclodeaminase, a Golgi-associated 58-kDa protein
    • Gao YS, Alvarez C, Nelson DS, Sztul E. Molecular cloning, characterization, and dynamics of rat formiminotransferase cyclodeaminase, a Golgi-associated 58-kDa protein. J Biol Chem 273: 33825–33834, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 33825-33834
    • Gao, Y.S.1    Alvarez, C.2    Nelson, D.S.3    Sztul, E.4
  • 17
    • 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, 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: 2250–2261, 2003.
    • (2003) Mol Biol Cell , vol.14 , pp. 2250-2261
    • Garcia-Mata, R.1    Szul, T.2    Alvarez, C.3    Sztul, E.4
  • 18
    • 84885906938 scopus 로고    scopus 로고
    • Dimerization of nuclear receptors
    • Germain P, Bourguet W. Dimerization of nuclear receptors. Methods Cell Biol 117: 21–41, 2013.
    • (2013) Methods Cell Biol , vol.117 , pp. 21-41
    • Germain, P.1    Bourguet, W.2
  • 21
    • 0026746713 scopus 로고
    • Inhibition by brefeldin A of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF
    • Helms JB, Rothman JE. Inhibition by brefeldin A of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF. Nature 360: 352–354, 1992.
    • (1992) Nature , vol.360 , pp. 352-354
    • Helms, J.B.1    Rothman, J.E.2
  • 22
    • 0037183696 scopus 로고    scopus 로고
    • 2-terminal domain of Golgin-160 contains both Golgi and nuclear targeting information
    • 2-terminal domain of Golgin-160 contains both Golgi and nuclear targeting information. J Biol Chem 277: 35833–35839, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 35833-35839
    • Hicks, S.W.1    Machamer, C.E.2
  • 23
    • 48749130156 scopus 로고    scopus 로고
    • Redundant roles of BIG2 and BIG1, guanine-nucleotide exchange factors for ADP-ribosylation factors in membrane traffic between the trans-Golgi network and endosomes
    • Ishizaki R, Shin HW, Mitsuhashi H, Nakayama K. Redundant roles of BIG2 and BIG1, guanine-nucleotide exchange factors for ADP-ribosylation factors in membrane traffic between the trans-Golgi network and endosomes. Mol Biol Cell 19: 2650–2660, 2008.
    • (2008) Mol Biol Cell , vol.19 , pp. 2650-2660
    • Ishizaki, R.1    Shin, H.W.2    Mitsuhashi, H.3    Nakayama, K.4
  • 24
    • 34248155380 scopus 로고    scopus 로고
    • The brefeldin A-inhibited guanine nucleotide-exchange protein, BIG2, regulates the constitutive release of TNFR1 exosome-like vesicles
    • Islam A, Shen X, Hiroi T, Moss J, Vaughan M, Levine SJ. The brefeldin A-inhibited guanine nucleotide-exchange protein, BIG2, regulates the constitutive release of TNFR1 exosome-like vesicles. J Biol Chem 282: 9591–9599, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 9591-9599
    • Islam, A.1    Shen, X.2    Hiroi, T.3    Moss, J.4    Vaughan, M.5    Levine, S.J.6
  • 25
    • 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, 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: 483–495, 2002.
    • (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
  • 27
    • 84883654492 scopus 로고    scopus 로고
    • Deficiency of the Cog8 subunit in normal and CDG-derived cells impairs the assembly of the COG and Golgi SNARE complexes
    • Laufman O, Freeze HH, Hong W, Lev S. Deficiency of the Cog8 subunit in normal and CDG-derived cells impairs the assembly of the COG and Golgi SNARE complexes. Traffic 14: 1065–1077, 2013.
    • (2013) Traffic , vol.14 , pp. 1065-1077
    • Laufman, O.1    Freeze, H.H.2    Hong, W.3    Lev, S.4
  • 28
    • 62649159075 scopus 로고    scopus 로고
    • Ligand-induced ErbB receptor dimerization
    • Lemmon MA. Ligand-induced ErbB receptor dimerization. Exp Cell Res 315: 638–648, 2009.
    • (2009) Exp Cell Res , vol.315 , pp. 638-648
    • Lemmon, M.A.1
  • 29
    • 0034616420 scopus 로고    scopus 로고
    • Binding relationships of membrane tethering components. The giantin N terminus and the GM130 N terminus compete for binding to the p115 C terminus
    • Linstedt AD, Jesch SA, Mehta A, Lee TH, Garcia-Mata R, Nelson DS, Sztul E. Binding relationships of membrane tethering components. The giantin N terminus and the GM130 N terminus compete for binding to the p115 C terminus. J Biol Chem 275: 10196–10201, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 10196-10201
    • Linstedt, A.D.1    Jesch, S.A.2    Mehta, A.3    Lee, T.H.4    Garcia-Mata, R.5    Nelson, D.S.6    Sztul, E.7
  • 30
    • 0031863688 scopus 로고    scopus 로고
    • Building a secretory apparatus: Role of ARF1/COPI in Golgi biogenesis and maintenance
    • Lippincott-Schwartz J, Cole NB, Donaldson JG. Building a secretory apparatus: role of ARF1/COPI in Golgi biogenesis and maintenance. Histochem Cell Biol 109: 449–462, 1998.
    • (1998) Histochem Cell Biol , vol.109 , pp. 449-462
    • Lippincott-Schwartz, J.1    Cole, N.B.2    Donaldson, J.G.3
  • 32
    • 39449116332 scopus 로고    scopus 로고
    • Distinct functions for Arf guanine nucleotide exchange factors at the Golgi complex: GBF1 and BIGs are required for assembly and maintenance of the Golgi stack and trans-Golgi network, respectively
    • Manolea F, Claude A, Chun J, Rosas J, Melancon P. Distinct functions for Arf guanine nucleotide exchange factors at the Golgi complex: GBF1 and BIGs are required for assembly and maintenance of the Golgi stack and trans-Golgi network, respectively. Mol Biol Cell 19: 523–535, 2008.
    • (2008) Mol Biol Cell , vol.19 , pp. 523-535
    • Manolea, F.1    Claude, A.2    Chun, J.3    Rosas, J.4    Melancon, P.5
  • 33
    • 0032400953 scopus 로고    scopus 로고
    • Human GBF1 is a ubiquitously expressed gene of the Sec7 domain family mapping to 10q24
    • Mansour SJ, Herbrick JA, Scherer SW, Melancon P. Human GBF1 is a ubiquitously expressed gene of the Sec7 domain family mapping to 10q24. Genomics 54: 323–327, 1998.
    • (1998) Genomics , vol.54 , pp. 323-327
    • Mansour, S.J.1    Herbrick, J.A.2    Scherer, S.W.3    Melancon, P.4
  • 34
    • 0033529249 scopus 로고    scopus 로고
    • P200 ARF-GEP1: A Golgi-localized guanine nucleotide exchange protein whose Sec7 domain is targeted by the drug brefeldin A
    • Mansour SJ, Skaug J, Zhao XH, Giordano J, Scherer SW, Melancon P. p200 ARF-GEP1: a Golgi-localized guanine nucleotide exchange protein whose Sec7 domain is targeted by the drug brefeldin A. Proc Natl Acad Sci USA 96: 7968–7973, 1999.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 7968-7973
    • Mansour, S.J.1    Skaug, J.2    Zhao, X.H.3    Giordano, J.4    Scherer, S.W.5    Melancon, P.6
  • 35
    • 84856225186 scopus 로고    scopus 로고
    • Glu-108 is essential for subunit assembly and dimer stability of D-phosphoglycerate dehydrogenase from Entamoeba histolytica
    • Mishra V, Kumar A, Ali V, Nozaki T, Zhang KY, Bhakuni V. Glu-108 is essential for subunit assembly and dimer stability of D-phosphoglycerate dehydrogenase from Entamoeba histolytica. Mol Biochem Parasitol 181: 117–124, 2012.
    • (2012) Mol Biochem Parasitol , vol.181 , pp. 117-124
    • Mishra, V.1    Kumar, A.2    Ali, V.3    Nozaki, T.4    Zhang, K.Y.5    Bhakuni, V.6
  • 36
    • 34347386746 scopus 로고    scopus 로고
    • Rab1b interacts with GBF1, modulates both ARF1 dynamics and COPI association
    • Monetta P, Slavin I, Romero N, Alvarez C. Rab1b interacts with GBF1, modulates both ARF1 dynamics and COPI association. Mol Biol Cell 18: 2400–2410, 2007.
    • (2007) Mol Biol Cell , vol.18 , pp. 2400-2410
    • Monetta, P.1    Slavin, I.2    Romero, N.3    Alvarez, C.4
  • 37
    • 0348047597 scopus 로고    scopus 로고
    • Crystal structure of ARF1*Sec7 complexed with Brefeldin A and its implications for the guanine nucleotide exchange mechanism
    • Mossessova E, Corpina RA, Goldberg J. Crystal structure of ARF1*Sec7 complexed with Brefeldin A and its implications for the guanine nucleotide exchange mechanism. Mol Cell 12: 1403–1411, 2003.
    • (2003) Mol Cell , vol.12 , pp. 1403-1411
    • Mossessova, E.1    Corpina, R.A.2    Goldberg, J.3
  • 38
    • 0032488847 scopus 로고    scopus 로고
    • Structure of the guanine nucleotide exchange factor Sec7 domain of human Arno and analysis of the interaction with ARF GTPase
    • Mossessova E, Gulbis JM, Goldberg J. Structure of the guanine nucleotide exchange factor Sec7 domain of human Arno and analysis of the interaction with ARF GTPase. Cell 92: 415–423, 1998.
    • (1998) Cell , vol.92 , pp. 415-423
    • Mossessova, E.1    Gulbis, J.M.2    Goldberg, J.3
  • 39
    • 0032547807 scopus 로고    scopus 로고
    • The membrane transport factor TAP/p115 cycles between the Golgi and earlier secretory compartments and contains distinct domains required for its localization and function
    • Nelson DS, Alvarez C, Gao YS, Garcia-Mata R, Fialkowski E, Sztul E. The membrane transport factor TAP/p115 cycles between the Golgi and earlier secretory compartments and contains distinct domains required for its localization and function. J Cell Biol 143: 319–331, 1998.
    • (1998) J Cell Biol , vol.143 , pp. 319-331
    • Nelson, D.S.1    Alvarez, C.2    Gao, Y.S.3    Garcia-Mata, R.4    Fialkowski, E.5    Sztul, E.6
  • 40
    • 14844333247 scopus 로고    scopus 로고
    • Dynamics of GBF1, a Brefeldin A-sensitive Arf1 exchange factor at the Golgi
    • Niu TK, Pfeifer AC, Lippincott-Schwartz J, Jackson CL. Dynamics of GBF1, a Brefeldin A-sensitive Arf1 exchange factor at the Golgi. Mol Biol Cell 16: 1213–1222, 2004.
    • (2004) Mol Biol Cell , vol.16 , pp. 1213-1222
    • Niu, T.K.1    Pfeifer, A.C.2    Lippincott-Schwartz, J.3    Jackson, C.L.4
  • 41
    • 23044497706 scopus 로고    scopus 로고
    • Mutations in a highly conserved region of the Arf1p activator GEA2 block anterograde Golgi transport but not COPI recruitment to membranes
    • Park SK, Hartnell LM, Jackson CL. Mutations in a highly conserved region of the Arf1p activator GEA2 block anterograde Golgi transport but not COPI recruitment to membranes. Mol Biol Cell 16: 3786–3799, 2005.
    • (2005) Mol Biol Cell , vol.16 , pp. 3786-3799
    • Park, S.K.1    Hartnell, L.M.2    Jackson, C.L.3
  • 42
    • 0002955384 scopus 로고    scopus 로고
    • Brefeldin A acts to stabilize an abortive ARF-GDP-Sec7 domain protein complex: Involvement of specific residues of the Sec7 domain
    • Peyroche A, Antonny B, Robineau S, Acker J, Cherfils J, Jackson CL. Brefeldin A acts to stabilize an abortive ARF-GDP-Sec7 domain protein complex: involvement of specific residues of the Sec7 domain. Mol Cell 3: 275–285, 1999.
    • (1999) Mol Cell , vol.3 , pp. 275-285
    • Peyroche, A.1    Antonny, B.2    Robineau, S.3    Acker, J.4    Cherfils, J.5    Jackson, C.L.6
  • 43
    • 0034943777 scopus 로고    scopus 로고
    • The ARF exchange factors Gea1p and Gea2p regulate Golgi structure and function in yeast
    • Peyroche A, Courbeyrette R, Rambourg A, Jackson CL. The ARF exchange factors Gea1p and Gea2p regulate Golgi structure and function in yeast. J Cell Sci 114: 2241–2253, 2001.
    • (2001) J Cell Sci , vol.114 , pp. 2241-2253
    • Peyroche, A.1    Courbeyrette, R.2    Rambourg, A.3    Jackson, C.L.4
  • 44
    • 0035139832 scopus 로고    scopus 로고
    • Functional analysis of ADP-ribosylation factor (ARF) guanine nucleotide exchange factors Gea1p and Gea2p in yeast
    • Peyroche A, Jackson CL. Functional analysis of ADP-ribosylation factor (ARF) guanine nucleotide exchange factors Gea1p and Gea2p in yeast. Methods Enzymol 329: 290–300, 2001.
    • (2001) Methods Enzymol , vol.329 , pp. 290-300
    • Peyroche, A.1    Jackson, C.L.2
  • 46
    • 0034700364 scopus 로고    scopus 로고
    • Molecular aspects of the cellular activities of ADP-ribosylation factors
    • re1
    • Randazzo PA, Nie Z, Miura K, Hsu VW. Molecular aspects of the cellular activities of ADP-ribosylation factors. Sci STKE 2000: re1, 2000.
    • (2000) Sci STKE 2000
    • Randazzo, P.A.1    Nie, Z.2    Miura, K.3    Hsu, V.W.4
  • 47
    • 15444363889 scopus 로고    scopus 로고
    • BIG1 is a binding partner of myosin IXb and regulates its Rho-GTPase activating protein activity
    • Saeki N, Tokuo H, Ikebe M. BIG1 is a binding partner of myosin IXb and regulates its Rho-GTPase activating protein activity. J Biol Chem 280: 10128–10134, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 10128-10134
    • Saeki, N.1    Tokuo, H.2    Ikebe, M.3
  • 49
    • 33846561669 scopus 로고    scopus 로고
    • BIG1, a brefeldin A-inhibited guanine nucleotide-exchange protein, is required for correct glycosylation and function of integrin beta1
    • Shen X, Hong MS, Moss J, Vaughan M. BIG1, a brefeldin A-inhibited guanine nucleotide-exchange protein, is required for correct glycosylation and function of integrin beta1. Proc Natl Acad Sci USA 104: 1230–1235, 2007.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 1230-1235
    • Shen, X.1    Hong, M.S.2    Moss, J.3    Vaughan, M.4
  • 50
    • 33644555815 scopus 로고    scopus 로고
    • Association of brefeldin A-inhibited guanine nucleotide-exchange protein 2 (BIG2) with recycling endosomes during transferrin uptake
    • Shen X, Xu KF, Fan Q, Pacheco-Rodriguez G, Moss J, Vaughan M. Association of brefeldin A-inhibited guanine nucleotide-exchange protein 2 (BIG2) with recycling endosomes during transferrin uptake. Proc Natl Acad Sci USA 103: 2635–2640, 2006.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 2635-2640
    • Shen, X.1    Xu, K.F.2    Fan, Q.3    Pacheco-Rodriguez, G.4    Moss, J.5    Vaughan, M.6
  • 51
    • 38749097326 scopus 로고    scopus 로고
    • Mint3/X11gamma is an ADP-ribosylation factor-dependent adaptor that regulates the traffic of the Alzheimer’s Precursor protein from the trans-Golgi network
    • Shrivastava-Ranjan P, Faundez V, Fang G, Rees H, Lah JJ, Levey AI, Kahn RA. Mint3/X11gamma is an ADP-ribosylation factor-dependent adaptor that regulates the traffic of the Alzheimer’s Precursor protein from the trans-Golgi network. Mol Biol Cell 19: 51–64, 2008.
    • (2008) Mol Biol Cell , vol.19 , pp. 51-64
    • Shrivastava-Ranjan, P.1    Faundez, V.2    Fang, G.3    Rees, H.4    Lah, J.J.5    Levey, A.I.6    Kahn, R.A.7
  • 52
  • 53
    • 0035172344 scopus 로고    scopus 로고
    • The ADP ribosylation factor-nucleotide exchange factors Gea1p and Gea2p have overlapping, but not redundant functions in retrograde transport from the Golgi to the endoplasmic reticulum
    • Spang A, Herrmann JM, Hamamoto S, Schekman R. The ADP ribosylation factor-nucleotide exchange factors Gea1p and Gea2p have overlapping, but not redundant functions in retrograde transport from the Golgi to the endoplasmic reticulum. Mol Biol Cell 12: 1035–1045, 2001.
    • (2001) Mol Biol Cell , vol.12 , pp. 1035-1045
    • Spang, A.1    Herrmann, J.M.2    Hamamoto, S.3    Schekman, R.4
  • 54
    • 70450223107 scopus 로고    scopus 로고
    • Role of vesicle tethering factors in the ER-Golgi membrane traffic
    • Sztul E, Lupashin V. Role of vesicle tethering factors in the ER-Golgi membrane traffic. FEBS Lett 583: 3770–3783, 2009.
    • (2009) FEBS Lett , vol.583 , pp. 3770-3783
    • Sztul, E.1    Lupashin, V.2
  • 55
    • 17444409335 scopus 로고    scopus 로고
    • Dissection of membrane dynamics of the ARF-guanine nucleotide exchange factor GBF1
    • Szul T, Garcia-Mata R, Brandon E, Shestopal S, Alvarez C, Sztul E. Dissection of membrane dynamics of the ARF-guanine nucleotide exchange factor GBF1. Traffic 6: 374–385, 2005.
    • (2005) Traffic , vol.6 , pp. 374-385
    • Szul, T.1    Garcia-Mata, R.2    Brandon, E.3    Shestopal, S.4    Alvarez, C.5    Sztul, E.6
  • 56
    • 37249041571 scopus 로고    scopus 로고
    • Dissecting the role of the ARF guanine nucleotide exchange factor GBF1 in Golgi biogenesis and protein trafficking
    • Szul T, Grabski R, Lyons S, Morohashi Y, Shestopal S, Lowe M, Sztul E. Dissecting the role of the ARF guanine nucleotide exchange factor GBF1 in Golgi biogenesis and protein trafficking. J Cell Sci 120: 3929–3940, 2007.
    • (2007) J Cell Sci , vol.120 , pp. 3929-3940
    • Szul, T.1    Grabski, R.2    Lyons, S.3    Morohashi, Y.4    Shestopal, S.5    Lowe, M.6    Sztul, E.7
  • 57
    • 14044250981 scopus 로고    scopus 로고
    • Codon-optimized Gaussia luciferase cDNA for mammalian gene expression in culture and in vivo
    • Tannous BA, Kim DE, Fernandez JL, Weissleder R, Breakefield XO. Codon-optimized Gaussia luciferase cDNA for mammalian gene expression in culture and in vivo. Mol Ther 11: 435–443, 2005.
    • (2005) Mol Ther , vol.11 , pp. 435-443
    • Tannous, B.A.1    Kim, D.E.2    Fernandez, J.L.3    Weissleder, R.4    Breakefield, X.O.5
  • 59
    • 14544280217 scopus 로고    scopus 로고
    • Interaction of BIG2, a brefeldin A-inhibited guanine nucleotide-exchange protein, with exocyst protein Exo70
    • Xu KF, Shen X, Li H, Pacheco-Rodriguez G, Moss J, Vaughan M. Interaction of BIG2, a brefeldin A-inhibited guanine nucleotide-exchange protein, with exocyst protein Exo70. Proc Natl Acad Sci USA 102: 2784–2789, 2005.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 2784-2789
    • Xu, K.F.1    Shen, X.2    Li, H.3    Pacheco-Rodriguez, G.4    Moss, J.5    Vaughan, M.6
  • 60
    • 0034646458 scopus 로고    scopus 로고
    • Identification and localization of two brefeldin A-inhibited guanine nucleotide-exchange proteins for ADP-ribosylation factors in a macromolecular complex
    • Yamaji R, Adamik R, Takeda K, Togawa A, Pacheco-Rodriguez G, Ferrans VJ, Moss J, Vaughan M. Identification and localization of two brefeldin A-inhibited guanine nucleotide-exchange proteins for ADP-ribosylation factors in a macromolecular complex. Proc Natl Acad Sci USA 97: 2567–2572, 2000.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 2567-2572
    • Yamaji, R.1    Adamik, R.2    Takeda, K.3    Togawa, A.4    Pacheco-Rodriguez, G.5    Ferrans, V.J.6    Moss, J.7    Vaughan, M.8
  • 61
    • 33750328406 scopus 로고    scopus 로고
    • GBF1, a cis-Golgi and VTCs-localized ARF-GEF, is implicated in ERto- Golgi protein traffic
    • Zhao X, Claude A, Chun J, Shields DJ, Presley JF, Melancon P. GBF1, a cis-Golgi and VTCs-localized ARF-GEF, is implicated in ERto- Golgi protein traffic. J Cell Sci 119: 3743–3753, 2006.
    • (2006) J Cell Sci , vol.119 , pp. 3743-3753
    • Zhao, X.1    Claude, A.2    Chun, J.3    Shields, D.J.4    Presley, J.F.5    Melancon, P.6
  • 62
    • 0036151274 scopus 로고    scopus 로고
    • Localization of large ADP-ribosylation factor-guanine nucleotide exchange factors to different Golgi compartments: Evidence for distinct functions in protein traffic
    • Zhao X, Lasell TK, Melancon P. Localization of large ADP-ribosylation factor-guanine nucleotide exchange factors to different Golgi compartments: evidence for distinct functions in protein traffic. Mol Biol Cell 13: 119–133, 2002.
    • (2002) Mol Biol Cell , vol.13 , pp. 119-133
    • Zhao, X.1    Lasell, T.K.2    Melancon, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.