메뉴 건너뛰기




Volumn 290, Issue 1, 2006, Pages

Role of tethering factors in secretory membrane traffic

Author keywords

Membrane tethering

Indexed keywords

RAB PROTEIN; REGULATOR PROTEIN; SNARE PROTEIN; MEMBRANE PROTEIN;

EID: 33644816187     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00293.2005     Document Type: Review
Times cited : (151)

References (156)
  • 1
    • 0034698202 scopus 로고    scopus 로고
    • Rab1 recruitment of p115 into a cis-SNARE complex: Programming budding COPII vesicles for fusion
    • Allan BB, Moyer BD, and Balch WE. Rab1 recruitment of p115 into a cis-SNARE complex: programming budding COPII vesicles for fusion. Science 289: 444-448, 2000.
    • (2000) Science , vol.289 , pp. 444-448
    • Allan, B.B.1    Moyer, B.D.2    Balch, W.E.3
  • 2
    • 0033552616 scopus 로고    scopus 로고
    • ER to Golgi transport: Requirement for p115 at a pre-Golgi VTC stage
    • Alvarez C, Fujita H, Hubbard A, and 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
  • 3
    • 0037910281 scopus 로고    scopus 로고
    • COPI recruitment is modulated by a Rab1b-dependent mechanism
    • Alvarez C, Garcia-Mata R, Brandon E, and Sztul E. COPI recruitment is modulated by a Rab1b-dependent mechanism. Mol Biol Cell 14: 2116-2127, 2003.
    • (2003) Mol Biol Cell , vol.14 , pp. 2116-2127
    • Alvarez, C.1    Garcia-Mata, R.2    Brandon, E.3    Sztul, E.4
  • 4
    • 0035951798 scopus 로고    scopus 로고
    • The p115-interactive proteins GM130 and giantin participate in endoplasmic reticulum-Golgi traffic
    • Alvarez C, Garcia-Mata R, Hauri HP, and Sztul E. The p115-interactive proteins GM130 and giantin participate in endoplasmic reticulum-Golgi traffic. J Biol Chem 276: 2693-2700, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 2693-2700
    • Alvarez, C.1    Garcia-Mata, R.2    Hauri, H.P.3    Sztul, E.4
  • 5
    • 0035914416 scopus 로고    scopus 로고
    • The coatomer-interacting protein Dsl1p is required for Golgi-to-endoplasmic reticulum retrieval in yeast
    • Andag U, Neumann T, and Schmitt HD. The coatomer-interacting protein Dsl1p is required for Golgi-to-endoplasmic reticulum retrieval in yeast. J Biol Chem 276: 39150-39160, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 39150-39160
    • Andag, U.1    Neumann, T.2    Schmitt, H.D.3
  • 6
    • 0032489878 scopus 로고    scopus 로고
    • Cargo selection by the COPII budding machinery during export from the ER
    • Aridor M, Weissman J, Bannykh S, Nuoffer C, and Balch WE. Cargo selection by the COPII budding machinery during export from the ER. J Cell Biol 141: 61-70, 1998.
    • (1998) J Cell Biol , vol.141 , pp. 61-70
    • Aridor, M.1    Weissman, J.2    Bannykh, S.3    Nuoffer, C.4    Balch, W.E.5
  • 7
    • 16344396080 scopus 로고    scopus 로고
    • A Rab requirement is not bypassed in SLY1-20 suppression
    • Ballew N, Liu Y, and Barlowe C. A Rab requirement is not bypassed in SLY1-20 suppression. Mol Biol Cell 16: 1839-1849, 2005.
    • (2005) Mol Biol Cell , vol.16 , pp. 1839-1849
    • Ballew, N.1    Liu, Y.2    Barlowe, C.3
  • 8
    • 0035150185 scopus 로고    scopus 로고
    • SNARE complexes: Is there sufficient complexity for vesicle targeting specificity?
    • Banfield DK. SNARE complexes: is there sufficient complexity for vesicle targeting specificity? Trends Biochem Sci 26: 67-68, 2001.
    • (2001) Trends Biochem Sci , vol.26 , pp. 67-68
    • Banfield, D.K.1
  • 9
    • 0030807931 scopus 로고    scopus 로고
    • Coupled ER to Golgi transport reconstituted with purified cytosolic proteins
    • Barlowe C. Coupled ER to Golgi transport reconstituted with purified cytosolic proteins. J Cell Biol 139: 1097-1108, 1997.
    • (1997) J Cell Biol , vol.139 , pp. 1097-1108
    • Barlowe, C.1
  • 10
    • 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, and 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
  • 11
    • 0030662715 scopus 로고    scopus 로고
    • GRASP65, a protein involved in the stacking of Golgi cisternae
    • Barr FA, Puype M, Vandekerckhove J, and Warren G. GRASP65, a protein involved in the stacking of Golgi cisternae. Cell 91: 253-262, 1997.
    • (1997) Cell , vol.91 , pp. 253-262
    • Barr, F.A.1    Puype, M.2    Vandekerckhove, J.3    Warren, G.4
  • 12
    • 0034161259 scopus 로고    scopus 로고
    • TRAPP stably associates with the Golgi and is required for vesicle docking
    • Barrowman J, Sacher M, and Ferro-Novick S. TRAPP stably associates with the Golgi and is required for vesicle docking. EMBO J 19: 862-869, 2000.
    • (2000) EMBO J , vol.19 , pp. 862-869
    • Barrowman, J.1    Sacher, M.2    Ferro-Novick, S.3
  • 13
    • 0033613967 scopus 로고    scopus 로고
    • Identification and characterization of golgin-84, a novel Golgi integral membrane protein with a cytoplasmic coiled-coil domain
    • Bascom RA, Srinivasan S, and Nussbaum RL. Identification and characterization of golgin-84, a novel Golgi integral membrane protein with a cytoplasmic coiled-coil domain. J Biol Chem 274: 2953-2962, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 2953-2962
    • Bascom, R.A.1    Srinivasan, S.2    Nussbaum, R.L.3
  • 14
    • 0842324801 scopus 로고    scopus 로고
    • The mechanisms of vesicle budding and fusion
    • Bonifacino JS and Glick BS. The mechanisms of vesicle budding and fusion. Cell 116: 153-166, 2004.
    • (2004) Cell , vol.116 , pp. 153-166
    • Bonifacino, J.S.1    Glick, B.S.2
  • 15
    • 0036151862 scopus 로고    scopus 로고
    • Molecular determinants of exocytosis
    • Bruns D and Jahn R. Molecular determinants of exocytosis. Pflügers Arch 443: 333-338, 2002.
    • (2002) Pflügers Arch , vol.443 , pp. 333-338
    • Bruns, D.1    Jahn, R.2
  • 16
    • 0032522377 scopus 로고    scopus 로고
    • Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins
    • Cao X, Ballew N, and Barlowe C. Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins. EMBO J 17: 2156-2165, 1998.
    • (1998) EMBO J , vol.17 , pp. 2156-2165
    • Cao, X.1    Ballew, N.2    Barlowe, C.3
  • 17
    • 0025286486 scopus 로고
    • Purification of three related peripheral membrane proteins needed for vesicular transport
    • Clary DO and Rothman JE. Purification of three related peripheral membrane proteins needed for vesicular transport. J Biol Chem 265: 10109-10117, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 10109-10117
    • Clary, D.O.1    Rothman, J.E.2
  • 18
    • 0013468039 scopus 로고    scopus 로고
    • Vps51p mediates the association of the GARP (Vps52/53/54) complex with the late Golgi t-SNARE Tlg1p
    • Conibear E, Cleck JN, and Stevens TH. Vps51p mediates the association of the GARP (Vps52/53/54) complex with the late Golgi t-SNARE Tlg1p. Mol Biol Cell 14: 1610-1623, 2003.
    • (2003) Mol Biol Cell , vol.14 , pp. 1610-1623
    • Conibear, E.1    Cleck, J.N.2    Stevens, T.H.3
  • 19
    • 0033972955 scopus 로고    scopus 로고
    • Vps52p, Vps53p, and Vps54p form a novel multisubunit complex required for protein sorting at the yeast late Golgi
    • Conibear E and Stevens TH. Vps52p, Vps53p, and Vps54p form a novel multisubunit complex required for protein sorting at the yeast late Golgi. Mol Biol Cell 11: 305-323, 2000.
    • (2000) Mol Biol Cell , vol.11 , pp. 305-323
    • Conibear, E.1    Stevens, T.H.2
  • 20
    • 12344320665 scopus 로고    scopus 로고
    • Mammalian GRIP domain proteins differ in their membrane binding properties and are recruited to distinct domains of the TGN
    • Derby MC, van Vliet C, Brown D, Luke MR, Lu L, Hong W, Slow JL, and Gleeson PA. Mammalian GRIP domain proteins differ in their membrane binding properties and are recruited to distinct domains of the TGN. J Cell Sci 117: 5865-5874, 2004.
    • (2004) J Cell Sci , vol.117 , pp. 5865-5874
    • Derby, M.C.1    Van Vliet, C.2    Brown, D.3    Luke, M.R.4    Lu, L.5    Hong, W.6    Slow, J.L.7    Gleeson, P.A.8
  • 21
    • 0037455546 scopus 로고    scopus 로고
    • The coiled-coil membrane protein golgin-84 is a novel Rab effector required for Golgi ribbon formation
    • Diao A, Rahman D, Pappin DJ, Lucocq J, and Lowe M. The coiled-coil membrane protein golgin-84 is a novel Rab effector required for Golgi ribbon formation. J Cell Biol 160: 201-212, 2003.
    • (2003) J Cell Biol , vol.160 , pp. 201-212
    • Diao, A.1    Rahman, D.2    Pappin, D.J.3    Lucocq, J.4    Lowe, M.5
  • 22
    • 0042744682 scopus 로고    scopus 로고
    • What is the role of SNARE proteins in membrane fusion?
    • Duman JG and Forte JG. What is the role of SNARE proteins in membrane fusion? Am J Physiol Cell Physiol 285: C237-C249, 2003.
    • (2003) Am J Physiol Cell Physiol , vol.285
    • Duman, J.G.1    Forte, J.G.2
  • 23
    • 0033034407 scopus 로고    scopus 로고
    • Mixed and non-cognate SNARE complexes. Characterization of assembly and biophysical properties
    • Fasshauer D, Antonin W, Subraniam V, and Jahn R. Mixed and non-cognate SNARE complexes. Characterization of assembly and biophysical properties. J Biol Chem 274: 15440-15446, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 15440-15446
    • Fasshauer, D.1    Antonin, W.2    Subraniam, V.3    Jahn, R.4
  • 24
    • 0032548828 scopus 로고    scopus 로고
    • Sec3p is a spatial landmark for polarized secretion in budding yeast
    • Finger FP, Hughes TE, and Novick P. Sec3p is a spatial landmark for polarized secretion in budding yeast. Cell 92: 559-571, 1998.
    • (1998) Cell , vol.92 , pp. 559-571
    • Finger, F.P.1    Hughes, T.E.2    Novick, P.3
  • 25
    • 0038602702 scopus 로고    scopus 로고
    • Structural basis of the interaction between RalA and Sec5, a subunit of the sec6/8 complex
    • Fukai S, Matern HT, Jagatu JR, Scheller RH, and Bunger AT. Structural basis of the interaction between RalA and Sec5, a subunit of the sec6/8 complex. EMBO J 22: 3267-3278, 2003.
    • (2003) EMBO J , vol.22 , pp. 3267-3278
    • Fukai, S.1    Matern, H.T.2    Jagatu, J.R.3    Scheller, R.H.4    Bunger, A.T.5
  • 26
    • 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, and 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
  • 27
    • 0242417632 scopus 로고    scopus 로고
    • The membrane-tethering protein p115 interacts with GBF1, an ARF guanine-nucleotide-exchange factor
    • Garcia-Mata R and Sztul E. The membrane-tethering protein p115 interacts with GBF1, an ARF guanine-nucleotide-exchange factor. EMBO Rep 4: 320-325, 2003.
    • (2003) EMBO Rep , vol.4 , pp. 320-325
    • Garcia-Mata, R.1    Sztul, E.2
  • 30
    • 0036855657 scopus 로고    scopus 로고
    • CASP, the alternatively spliced product of the gene encoding the CCAAT-displacement protein transcription factor, is a Golgi membrane protein related to giantin
    • Gillingham AK, Pfeifer AC, and Munro S. CASP, the alternatively spliced product of the gene encoding the CCAAT-displacement protein transcription factor, is a Golgi membrane protein related to giantin. Mol Biol Cell 13: 3761-3774, 2002.
    • (2002) Mol Biol Cell , vol.13 , pp. 3761-3774
    • Gillingham, A.K.1    Pfeifer, A.C.2    Munro, S.3
  • 31
    • 7244248570 scopus 로고    scopus 로고
    • The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to recruit the golgin Rud3p to the cis-Golgi
    • Gillingham AK, Tong AH, Boone C, and Munro S. The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to recruit the golgin Rud3p to the cis-Golgi. J Cell Biol 167: 281-292, 2004.
    • (2004) J Cell Biol , vol.167 , pp. 281-292
    • Gillingham, A.K.1    Tong, A.H.2    Boone, C.3    Munro, S.4
  • 32
    • 0031567602 scopus 로고    scopus 로고
    • High-affinity binding of the yeast cis-Golgi t-SNARE, Sed5p, to wild-type and mutant Sly1p, a modulator of transport vesicle docking
    • Grabowski R and Gallwitz D. High-affinity binding of the yeast cis-Golgi t-SNARE, Sed5p, to wild-type and mutant Sly1p, a modulator of transport vesicle docking. FEBS Lett 411: 169-172, 1997.
    • (1997) FEBS Lett , vol.411 , pp. 169-172
    • Grabowski, R.1    Gallwitz, D.2
  • 33
    • 0032577562 scopus 로고    scopus 로고
    • Sec6/8 complex is recruited to cell-cell contacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells
    • Grindstaff KK, Yeaman C, and Nelson WJ. Sec6/8 complex is recruited to cell-cell contacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells. Cell 93: 731-740, 1998.
    • (1998) Cell , vol.93 , pp. 731-740
    • Grindstaff, K.K.1    Yeaman, C.2    Nelson, W.J.3
  • 34
    • 0033558093 scopus 로고    scopus 로고
    • The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis
    • Guo W, Roth D, Walch-Solimena C, and Novick P. The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis. EMBO J 18: 1071-1080, 1999.
    • (1999) EMBO J , vol.18 , pp. 1071-1080
    • Guo, W.1    Roth, D.2    Walch-Solimena, C.3    Novick, P.4
  • 35
    • 0035067186 scopus 로고    scopus 로고
    • Spatial regulation of the exocyst complex by Rho1 GTPase
    • Guo W, Tamanoi F, and Novick P. Spatial regulation of the exocyst complex by Rho1 GTPase. Nat Cell Biol 3: 353-360, 2001.
    • (2001) Nat Cell Biol , vol.3 , pp. 353-360
    • Guo, W.1    Tamanoi, F.2    Novick, P.3
  • 37
    • 0032498542 scopus 로고    scopus 로고
    • Cell-free transport to distinct Golgi cisternae is compartment specific and ARF independent
    • Happe S and Weidman P. Cell-free transport to distinct Golgi cisternae is compartment specific and ARF independent. J Cell Biol 140: 511-523, 1998.
    • (1998) J Cell Biol , vol.140 , pp. 511-523
    • Happe, S.1    Weidman, P.2
  • 38
    • 0037183696 scopus 로고    scopus 로고
    • The NH2-terminal domain of Golgin-160 contains both Golgi and nuclear targeting information
    • Hicks SW and Machamer CE. The NH2-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
  • 39
    • 20544435937 scopus 로고    scopus 로고
    • Golgi structure in stress sensing and apoptosis
    • Hicks SW and Machamer CE. Golgi structure in stress sensing and apoptosis. Biochim Biophys Acta 1744: 406-414, 2005.
    • (2005) Biochim Biophys Acta , vol.1744 , pp. 406-414
    • Hicks, S.W.1    Machamer, C.E.2
  • 41
    • 23844556932 scopus 로고    scopus 로고
    • SNAREs and traffic
    • Hong W. SNAREs and traffic. Biochim Biophys Acta 1744: 493-517, 2005.
    • (2005) Biochim Biophys Acta , vol.1744 , pp. 493-517
    • Hong, W.1
  • 43
    • 19644372736 scopus 로고    scopus 로고
    • p115 interacts with the GLUT4 vesicle protein, IRAP, and plays a critical role in insulin-stimulated GLUT4 translocation
    • Hosaka T, Brooks CC, Presman E, Kim SK, Zhang Z, Breen M, Gross DN, Sztul E, and Pilch PF. p115 interacts with the GLUT4 vesicle protein, IRAP, and plays a critical role in insulin-stimulated GLUT4 translocation. Mol Biol Cell 16: 2282-2290, 2005.
    • (2005) Mol Biol Cell , vol.16 , pp. 2282-2290
    • Hosaka, T.1    Brooks, C.C.2    Presman, E.3    Kim, S.K.4    Zhang, Z.5    Breen, M.6    Gross, D.N.7    Sztul, E.8    Pilch, P.F.9
  • 45
    • 0033526005 scopus 로고    scopus 로고
    • GMAP-210, a cis-Golgi network-associated protein, is a minus end microtubule-binding protein
    • Infante C, Ramos-Morales F, Fedriani C, Bornens M, and Rios RM. GMAP-210, a cis-Golgi network-associated protein, is a minus end microtubule-binding protein. J Cell Biol 145: 83-98, 1999.
    • (1999) J Cell Biol , vol.145 , pp. 83-98
    • Infante, C.1    Ramos-Morales, F.2    Fedriani, C.3    Bornens, M.4    Rios, R.M.5
  • 46
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • Jahn R and Sudhof TC. Membrane fusion and exocytosis. Annu Rev Biochem 68: 863-911, 1999.
    • (1999) Annu Rev Biochem , vol.68 , pp. 863-911
    • Jahn, R.1    Sudhof, T.C.2
  • 47
    • 0037147148 scopus 로고    scopus 로고
    • Crystal structure of SEDL and its implications for a genetic disease spondyloepiphyseal dysplasia tarda
    • Jang SB, Kim YG, Cho YS, Suh PG, Kim KH, and Oh BH. Crystal structure of SEDL and its implications for a genetic disease spondyloepiphyseal dysplasia tarda. J Biol Chem 277: 49863-49869, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 49863-49869
    • Jang, S.B.1    Kim, Y.G.2    Cho, Y.S.3    Suh, P.G.4    Kim, K.H.5    Oh, B.H.6
  • 48
    • 0031800716 scopus 로고    scopus 로고
    • A high copy suppressor screen reveals genetic interactions between BET3 and a new gene. Evidence for a novel complex in ER-to-Golgi transport
    • Jiang Y, Scarpa A, Zhang L, Stone S, Feliciano E, and Ferro-Novick S. A high copy suppressor screen reveals genetic interactions between BET3 and a new gene. Evidence for a novel complex in ER-to-Golgi transport. Genetics 149: 833-841, 1998.
    • (1998) Genetics , vol.149 , pp. 833-841
    • Jiang, Y.1    Scarpa, A.2    Zhang, L.3    Stone, S.4    Feliciano, E.5    Ferro-Novick, S.6
  • 49
    • 0033638091 scopus 로고    scopus 로고
    • The TRAPP complex is a nucleotide exchanger for Ypt1 and Ypt31/32
    • Jones S, Newman C, Liu F, and Segev N. The TRAPP complex is a nucleotide exchanger for Ypt1 and Ypt31/32. Mol Biol Cell 11: 4403-4411, 2000.
    • (2000) Mol Biol Cell , vol.11 , pp. 4403-4411
    • Jones, S.1    Newman, C.2    Liu, F.3    Segev, N.4
  • 50
    • 0242493310 scopus 로고    scopus 로고
    • Identification of mouse Vps16 and biochemical characterization of mammalian class C Vps complex
    • Kim BY, Ueda M, Kominami E, Agawa K, Kohsaka S, and Azakawa C. Identification of mouse Vps16 and biochemical characterization of mammalian class C Vps complex. Biochem Biophys Res Commun 311: 577-582, 2003.
    • (2003) Biochem Biophys Res Commun , vol.311 , pp. 577-582
    • Kim, B.Y.1    Ueda, M.2    Kominami, E.3    Agawa, K.4    Kohsaka, S.5    Azakawa, C.6
  • 51
    • 0032882140 scopus 로고    scopus 로고
    • High-copy suppressor analysis reveals a physical interaction between Sec34p and Sec35p, a protein implicated in vesicle docking
    • Kim DW, Sacher M, Scarpa A, Quinn AM, and Ferro-Novick S. High-copy suppressor analysis reveals a physical interaction between Sec34p and Sec35p, a protein implicated in vesicle docking. Mol Biol Cell 10: 3317-3329, 1999.
    • (1999) Mol Biol Cell , vol.10 , pp. 3317-3329
    • Kim, D.W.1    Sacher, M.2    Scarpa, A.3    Quinn, A.M.4    Ferro-Novick, S.5
  • 53
    • 0022455528 scopus 로고
    • Three types of low density lipoprotein receptor-deficient mutant have pleiotropic defects in the synthesis of N-linked, O-linked, and lipid-linked carbohydrate chains
    • Kingsley DM, Kozarsky KF, Segal M, and Krieger M. Three types of low density lipoprotein receptor-deficient mutant have pleiotropic defects in the synthesis of N-linked, O-linked, and lipid-linked carbohydrate chains. J Cell Biol 102: 1576-1585, 1986.
    • (1986) J Cell Biol , vol.102 , pp. 1576-1585
    • Kingsley, D.M.1    Kozarsky, K.F.2    Segal, M.3    Krieger, M.4
  • 54
    • 0033535542 scopus 로고    scopus 로고
    • A novel Golgi-localisation domain shared by a class of coiled-coil peripheral membrane proteins
    • Kjer-Nielsen L, Teasdale RD, van Vliet C, and Gleeson PA. A novel Golgi-localisation domain shared by a class of coiled-coil peripheral membrane proteins. Curr Biol 9: 385-388, 1999.
    • (1999) Curr Biol , vol.9 , pp. 385-388
    • Kjer-Nielsen, L.1    Teasdale, R.D.2    Van Vliet, C.3    Gleeson, P.A.4
  • 55
  • 56
    • 0042672956 scopus 로고    scopus 로고
    • A novel role for dp115 in the organization of tER sites in Drosophila
    • Kondylis V and Rabouille C. A novel role for dp115 in the organization of tER sites in Drosophila. J Cell Biol 162: 185-198, 2003.
    • (2003) J Cell Biol , vol.162 , pp. 185-198
    • Kondylis, V.1    Rabouille, C.2
  • 57
    • 0034423410 scopus 로고    scopus 로고
    • Transmembrane transforming growth factor-α tethers to the PDZ domain-containing, Golgi membrane-associated protein p59/GRASP55
    • Kuo A, Zhong C, Lane WS, and Derynck R. Transmembrane transforming growth factor-α tethers to the PDZ domain-containing, Golgi membrane-associated protein p59/GRASP55. EMBO J 19: 6427-6439, 2000.
    • (2000) EMBO J , vol.19 , pp. 6427-6439
    • Kuo, A.1    Zhong, C.2    Lane, W.S.3    Derynck, R.4
  • 58
    • 0033594080 scopus 로고    scopus 로고
    • Golgi structure in three dimensions: Functional insights from the normal rat kidney cell
    • Ladinsky MS, Mastronarde DN, McIntosh JR, Howell KE, and Staehlin LA. Golgi structure in three dimensions: functional insights from the normal rat kidney cell. J Cell Biol 144: 1135-1149, 1999.
    • (1999) J Cell Biol , vol.144 , pp. 1135-1149
    • Ladinsky, M.S.1    Mastronarde, D.N.2    McIntosh, J.R.3    Howell, K.E.4    Staehlin, L.A.5
  • 59
    • 0034723203 scopus 로고    scopus 로고
    • The amino-terminal domain of the Golgi protein giantin interacts directly with the vesicle-tethering protein p115
    • Lesa GM, Seemann J, Shorter J, Vandekerckhove J, and Warren G. The amino-terminal domain of the Golgi protein giantin interacts directly with the vesicle-tethering protein p115. J Biol Chem 275: 2831-2836, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 2831-2836
    • Lesa, G.M.1    Seemann, J.2    Shorter, J.3    Vandekerckhove, J.4    Warren, G.5
  • 60
    • 0030864380 scopus 로고    scopus 로고
    • CASP, a novel, highly conserved alternative-splicing product of the CDP/cut/cux gene, lacks cut-repeat and homeo DNA-binding domains, and interacts with full-length CDP in vitro
    • Lievens PM, Tufarelli C, Donady JJ, Stagg A, and Neufeld EJ. CASP, a novel, highly conserved alternative-splicing product of the CDP/cut/cux gene, lacks cut-repeat and homeo DNA-binding domains, and interacts with full-length CDP in vitro. Gene 197: 73-81, 1997.
    • (1997) Gene , vol.197 , pp. 73-81
    • Lievens, P.M.1    Tufarelli, C.2    Donady, J.J.3    Stagg, A.4    Neufeld, E.J.5
  • 62
    • 0027244942 scopus 로고
    • Giantin, a novel conserved Golgi membrane protein containing a cytoplasmic domain of at least 350 kDa
    • Linstedt AD and Hauri HP. Giantin, a novel conserved Golgi membrane protein containing a cytoplasmic domain of at least 350 kDa. Mol Biol Cell 4: 679-693, 1993.
    • (1993) Mol Biol Cell , vol.4 , pp. 679-693
    • Linstedt, A.D.1    Hauri, H.P.2
  • 63
    • 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, and 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
  • 64
    • 0033638380 scopus 로고    scopus 로고
    • Exocyst is involved in cystogenesis and tubulogenesis and acts by modulating synthesis and delivery of basolateral plasma membrane and secretory proteins
    • Lipschutz JH, Guo W, O'Brien LE, Nguyen YH, Novick P, and Mostov KE. Exocyst is involved in cystogenesis and tubulogenesis and acts by modulating synthesis and delivery of basolateral plasma membrane and secretory proteins. Mol Biol Cell 11: 4259-4275, 2000.
    • (2000) Mol Biol Cell , vol.11 , pp. 4259-4275
    • Lipschutz, J.H.1    Guo, W.2    O'Brien, L.E.3    Nguyen, Y.H.4    Novick, P.5    Mostov, K.E.6
  • 65
    • 0001647625 scopus 로고    scopus 로고
    • Exocytosis: The many masters of the exocyst
    • Lipschutz JH and Mostov KE. Exocytosis: the many masters of the exocyst. Curr Biol 12: R212-R214, 2002.
    • (2002) Curr Biol , vol.12
    • Lipschutz, J.H.1    Mostov, K.E.2
  • 66
    • 2642540241 scopus 로고    scopus 로고
    • The binary interacting network of the conserved oligomeric Golgi tethering complex
    • Loh E and Hong W. The binary interacting network of the conserved oligomeric Golgi tethering complex. J Biol Chem 279: 24640-24648, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 24640-24648
    • Loh, E.1    Hong, W.2
  • 67
    • 17244375812 scopus 로고    scopus 로고
    • Mammalian Bet3 functions as a cytosolic factor participating in transport from the ER to the Golgi apparatus
    • Loh E, Peter F, Subramaniam VN, and Hong W. Mammalian Bet3 functions as a cytosolic factor participating in transport from the ER to the Golgi apparatus. J Cell Sci 118: 1209-1222, 2005.
    • (2005) J Cell Sci , vol.118 , pp. 1209-1222
    • Loh, E.1    Peter, F.2    Subramaniam, V.N.3    Hong, W.4
  • 68
    • 0032498623 scopus 로고    scopus 로고
    • Isolation of functional Golgi-derived vesicles with a possible role in retrograde transport
    • Love HD, Lin CC, Short CS, and Osterman J. Isolation of functional Golgi-derived vesicles with a possible role in retrograde transport. J Cell Biol 140: 541-551, 1998.
    • (1998) J Cell Biol , vol.140 , pp. 541-551
    • Love, H.D.1    Lin, C.C.2    Short, C.S.3    Osterman, J.4
  • 69
    • 0030060309 scopus 로고    scopus 로고
    • The mammalian ARF-like protein 1 (Arl1) is associated with the Golgi complex
    • Lowe SL, Wong SH, and Hong W. The mammalian ARF-like protein 1 (Arl1) is associated with the Golgi complex. J Cell Sci 109: 209-20, 1996.
    • (1996) J Cell Sci , vol.109 , pp. 209-220
    • Lowe, S.L.1    Wong, S.H.2    Hong, W.3
  • 70
    • 0141856316 scopus 로고    scopus 로고
    • Interaction of Arl1-GTP with GRIP domains recruits autoantigens Golgin-97 and Golgin-245/p230 onto the Golgi
    • Lu L and Hong W. Interaction of Arl1-GTP with GRIP domains recruits autoantigens Golgin-97 and Golgin-245/p230 onto the Golgi. Mol Biol Cell 14: 3767-3781, 2003.
    • (2003) Mol Biol Cell , vol.14 , pp. 3767-3781
    • Lu, L.1    Hong, W.2
  • 71
    • 4644352428 scopus 로고    scopus 로고
    • Autoantigen Golgin-97, an effector of Arl1 GTPase, participates in traffic from the endosome to the trans-Golgi network
    • Lu L, Tai G, and Hong W. Autoantigen Golgin-97, an effector of Arl1 GTPase, participates in traffic from the endosome to the trans-Golgi network. Mol Biol Cell 15: 4426-4443, 2004.
    • (2004) Mol Biol Cell , vol.15 , pp. 4426-4443
    • Lu, L.1    Tai, G.2    Hong, W.3
  • 72
    • 0037423287 scopus 로고    scopus 로고
    • GRIP domain-mediated targeting of two new coiled-coil proteins, GCC88 and GCC185, to subcompartments of the trans-Golgi network
    • Luke MR, Kjer-Nielsen L, Brown DL, Stow JL, and Gleeson PA. GRIP domain-mediated targeting of two new coiled-coil proteins, GCC88 and GCC185, to subcompartments of the trans-Golgi network. J Biol Chem 278: 4216-4226, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 4216-4226
    • Luke, M.R.1    Kjer-Nielsen, L.2    Brown, D.L.3    Stow, J.L.4    Gleeson, P.A.5
  • 73
    • 0030960276 scopus 로고    scopus 로고
    • Predicting coiled-coil regions in proteins
    • Lupas A. Predicting coiled-coil regions in proteins. Curr Opin Struct Biol 7: 388-393, 1997.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 388-393
    • Lupas, A.1
  • 74
    • 0042266400 scopus 로고    scopus 로고
    • Death from within: Apoptosis and the secretory pathway
    • Maag RS, Hicks SW, and Machamer CE. Death from within: apoptosis and the secretory pathway. Curr Opin Cell Biol 15: 456-461, 2003.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 456-461
    • Maag, R.S.1    Hicks, S.W.2    Machamer, C.E.3
  • 75
    • 0038697678 scopus 로고    scopus 로고
    • Golgi disassembly in apoptosis: Cause or effect?
    • Machamer CE. Golgi disassembly in apoptosis: cause or effect? Trends Cell Biol 13: 279-281, 2003.
    • (2003) Trends Cell Biol , vol.13 , pp. 279-281
    • Machamer, C.E.1
  • 77
    • 13844317835 scopus 로고    scopus 로고
    • Golgin tethers define subpopulations of COPI vesicles
    • Malsam J, Satoh A, Pelletier L, and Warren G. Golgin tethers define subpopulations of COPI vesicles. Science 307: 1095-1098, 2005.
    • (2005) Science , vol.307 , pp. 1095-1098
    • Malsam, J.1    Satoh, A.2    Pelletier, L.3    Warren, G.4
  • 80
    • 0035794232 scopus 로고    scopus 로고
    • An essential cytoplasmic domain for the Golgi localization of coiled-coil proteins with a COOH-terminal membrane anchor
    • Misumi Y, Sohda M, Tashiro A, Sato H, and Ikehara Y. An essential cytoplasmic domain for the Golgi localization of coiled-coil proteins with a COOH-terminal membrane anchor. J Biol Chem 276: 6867-6873, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 6867-6873
    • Misumi, Y.1    Sohda, M.2    Tashiro, A.3    Sato, H.4    Ikehara, Y.5
  • 81
    • 0036200146 scopus 로고    scopus 로고
    • The Rab GTPase Ypt1p and tethering factors couple protein sorting at the ER to vesicle targeting to the Golgi apparatus
    • Morsomme P and Riezman H. The Rab GTPase Ypt1p and tethering factors couple protein sorting at the ER to vesicle targeting to the Golgi apparatus. Dev Cell 2: 307-317, 2002.
    • (2002) Dev Cell , vol.2 , pp. 307-317
    • Morsomme, P.1    Riezman, H.2
  • 83
    • 0035024551 scopus 로고    scopus 로고
    • Rab1 interaction with a GM130 effector complex regulates COPII vesicle cis-Golgi tethering
    • Moyer BD, Allan BB, and Balch WE. Rab1 interaction with a GM130 effector complex regulates COPII vesicle cis-Golgi tethering. Traffic 2: 268-276, 2001.
    • (2001) Traffic , vol.2 , pp. 268-276
    • Moyer, B.D.1    Allan, B.B.2    Balch, W.E.3
  • 84
    • 0033535585 scopus 로고    scopus 로고
    • The GRIP domain: A novel Golgi-targeting domain found in several coiled-coil proteins
    • Munro S and Nichols BJ. The GRIP domain: a novel Golgi-targeting domain found in several coiled-coil proteins. Curr Biol 9: 377-380, 1999.
    • (1999) Curr Biol , vol.9 , pp. 377-380
    • Munro, S.1    Nichols, B.J.2
  • 85
    • 0037421632 scopus 로고    scopus 로고
    • Mutations in the exocyst component Sec5 disrupt neuronal membrane traffic, but neurotransmitter release persists
    • Murthy M, Garza D, Scheller RH, and Schwarz TL. Mutations in the exocyst component Sec5 disrupt neuronal membrane traffic, but neurotransmitter release persists. Neuron 37: 433-447, 2003.
    • (2003) Neuron , vol.37 , pp. 433-447
    • Murthy, M.1    Garza, D.2    Scheller, R.H.3    Schwarz, T.L.4
  • 86
    • 0842301562 scopus 로고    scopus 로고
    • The exocyst component Sec5 is required for membrane traffic and polarity in the Drosophila ovary
    • Murthy M and Schwarz TL. The exocyst component Sec5 is required for membrane traffic and polarity in the Drosophila ovary. Development 131: 377-388, 2004.
    • (2004) Development , vol.131 , pp. 377-388
    • Murthy, M.1    Schwarz, T.L.2
  • 87
    • 0025805962 scopus 로고
    • A cytoskeleton-related gene, uso1, is required for intracellular protein transport in Saccharomyces cerevisiae
    • Nakajima H, Hirata A, Ogawa Y, Yonehara T, Yoda K, and Yamasaki M. A cytoskeleton-related gene, uso1, is required for intracellular protein transport in Saccharomyces cerevisiae. J Cell Biol 113: 245-260, 1991.
    • (1991) J Cell Biol , vol.113 , pp. 245-260
    • Nakajima, H.1    Hirata, A.2    Ogawa, Y.3    Yonehara, T.4    Yoda, K.5    Yamasaki, M.6
  • 88
    • 0030953187 scopus 로고    scopus 로고
    • The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner
    • Nakamura N, Lowe M, Levine TP, Rabouille C, and Warren G. The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner. Cell 89: 445-455, 1997.
    • (1997) Cell , vol.89 , pp. 445-455
    • Nakamura, N.1    Lowe, M.2    Levine, T.P.3    Rabouille, C.4    Warren, G.5
  • 90
    • 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, and 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
  • 91
    • 0035972762 scopus 로고    scopus 로고
    • Role of the multifunctional CDP/Cut/Cux homeodomain transcription factor in regulating differentiation, cell growth and development
    • Nepveu A. Role of the multifunctional CDP/Cut/Cux homeodomain transcription factor in regulating differentiation, cell growth and development. Gene 270: 1-15, 2001.
    • (2001) Gene , vol.270 , pp. 1-15
    • Nepveu, A.1
  • 93
    • 0035854711 scopus 로고    scopus 로고
    • The role of CDP in the negative regulation of CXCL1 gene expression
    • Nirodi C, Hart J, Phawan P, Moon NS, Nepveu A, and Richmond A. The role of CDP in the negative regulation of CXCL1 gene expression. J Biol Chem 276: 26122-26131, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 26122-26131
    • Nirodi, C.1    Hart, J.2    Phawan, P.3    Moon, N.S.4    Nepveu, A.5    Richmond, A.6
  • 94
    • 0032478142 scopus 로고    scopus 로고
    • Vesicles on strings: Morphological evidence for processive transport within the Golgi stack
    • Orci L, Perrelet A, and Rothman JE. Vesicles on strings: morphological evidence for processive transport within the Golgi stack. Proc Natl Acad Sci USA 95: 2279-2283, 1998.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 2279-2283
    • Orci, L.1    Perrelet, A.2    Rothman, J.E.3
  • 95
    • 0035038784 scopus 로고    scopus 로고
    • Stoichiometry and kinetics of transport vesicle fusion with Golgi membranes
    • Ostermann J. Stoichiometry and kinetics of transport vesicle fusion with Golgi membranes. EMBO Rep 2: 324-329, 2001.
    • (2001) EMBO Rep , vol.2 , pp. 324-329
    • Ostermann, J.1
  • 96
    • 0242266897 scopus 로고    scopus 로고
    • Structural basis for Arl1-dependent targeting of homodimeric GRIP domains to the Golgi apparatus
    • Panic B, Perisic O, Veprintsev DB, Williams RL, and Munro S. Structural basis for Arl1-dependent targeting of homodimeric GRIP domains to the Golgi apparatus. Mol Cell 12: 863-874, 2003.
    • (2003) Mol Cell , vol.12 , pp. 863-874
    • Panic, B.1    Perisic, O.2    Veprintsev, D.B.3    Williams, R.L.4    Munro, S.5
  • 97
    • 20444393413 scopus 로고    scopus 로고
    • The golgin Lava lamp mediates dynein-based Golgi movements during Drosophila cellularization
    • Papoulas O, Hays TS, and Sisson JC. The golgin Lava lamp mediates dynein-based Golgi movements during Drosophila cellularization. Nat Cell Biol 7: 612-618, 2005.
    • (2005) Nat Cell Biol , vol.7 , pp. 612-618
    • Papoulas, O.1    Hays, T.S.2    Sisson, J.C.3
  • 98
    • 0036866606 scopus 로고    scopus 로고
    • Arf, Arl, Arp and Sar proteins: A family of GTP-binding proteins with a structural device for 'front-back' communication
    • Pasqualato S, Renault L, and Cherfils J. Arf, Arl, Arp and Sar proteins: a family of GTP-binding proteins with a structural device for 'front-back' communication. EMBO Rep 3: 1035-1041, 2002.
    • (2002) EMBO Rep , vol.3 , pp. 1035-1041
    • Pasqualato, S.1    Renault, L.2    Cherfils, J.3
  • 99
    • 0037071544 scopus 로고    scopus 로고
    • Sly1 protein bound to Golgi syntaxin Sed5p allows assembly and contributes to specificity of SNARE fusion complexes
    • Peng R and Gallwitz D. Sly1 protein bound to Golgi syntaxin Sed5p allows assembly and contributes to specificity of SNARE fusion complexes. J Cell Biol 157: 645-655, 2002.
    • (2002) J Cell Biol , vol.157 , pp. 645-655
    • Peng, R.1    Gallwitz, D.2
  • 100
    • 0037128212 scopus 로고    scopus 로고
    • CLIPR-59, a new trans-Golgi/TGN cytoplasmic linker protein belonging to the CLIP-170 family
    • Perez F, Pernet-Gallay K, Nizak C, Goodson HV, Kreis TE, and Goud B. CLIPR-59, a new trans-Golgi/TGN cytoplasmic linker protein belonging to the CLIP-170 family. J Cell Biol 156: 631-642, 2002.
    • (2002) J Cell Biol , vol.156 , pp. 631-642
    • Perez, F.1    Pernet-Gallay, K.2    Nizak, C.3    Goodson, H.V.4    Kreis, T.E.5    Goud, B.6
  • 101
    • 0036843024 scopus 로고    scopus 로고
    • The overexpression of GMAP-210 blocks anterograde and retrograde transport between the ER and the Golgi apparatus
    • Pernet-Gallay K, Antony C, Johannes L, Bornens M, Goud B, and Rios RM. The overexpression of GMAP-210 blocks anterograde and retrograde transport between the ER and the Golgi apparatus. Traffic 3: 822-832, 2002.
    • (2002) Traffic , vol.3 , pp. 822-832
    • Pernet-Gallay, K.1    Antony, C.2    Johannes, L.3    Bornens, M.4    Goud, B.5    Rios, R.M.6
  • 103
    • 1842613600 scopus 로고    scopus 로고
    • YSK1 is activated by the Golgi matrix protein GM130 and plays a role in cell migration through its substrate 14-3-3ζ
    • Preisinger C, Short B, De Corte V, Bruyneel E, Haas A, Kopajtich R, Gettermans J, and Barr A. YSK1 is activated by the Golgi matrix protein GM130 and plays a role in cell migration through its substrate 14-3-3ζ. J Cell Biol 164: 1009-1020, 2004.
    • (2004) J Cell Biol , vol.164 , pp. 1009-1020
    • Preisinger, C.1    Short, B.2    De Corte, V.3    Bruyneel, E.4    Haas, A.5    Kopajtich, R.6    Gettermans, J.7    Barr, A.8
  • 105
    • 0035889084 scopus 로고    scopus 로고
    • Evidence that Golgi structure depends on a p115 activity that is independent of the vesicle tether components giantin and GM130
    • Puthenveedu MA and Linstedt AD. Evidence that Golgi structure depends on a p115 activity that is independent of the vesicle tether components giantin and GM130. J Cell Biol 155: 227-238, 2001.
    • (2001) J Cell Biol , vol.155 , pp. 227-238
    • Puthenveedu, M.A.1    Linstedt, A.D.2
  • 106
    • 0842277809 scopus 로고    scopus 로고
    • Gene replacement reveals that p115/SNARE interactions are essential for Golgi biogenesis
    • Puthenveedu MA and Linstedt AD. Gene replacement reveals that p115/SNARE interactions are essential for Golgi biogenesis. Proc Natl Acad Sci USA 101: 1253-1256, 2004.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 1253-1256
    • Puthenveedu, M.A.1    Linstedt, A.D.2
  • 107
    • 0028930157 scopus 로고
    • Reassembly of Golgi stacks from mitotic Golgi fragments in a cell-free system
    • Rabouille C, Misteli T, Watson R, and Warren G. Reassembly of Golgi stacks from mitotic Golgi fragments in a cell-free system. J Cell Biol 129: 605-618, 1995.
    • (1995) J Cell Biol , vol.129 , pp. 605-618
    • Rabouille, C.1    Misteli, T.2    Watson, R.3    Warren, G.4
  • 108
    • 0035661564 scopus 로고    scopus 로고
    • Golgito-endoplasmic reticulum (ER) retrograde traffic in yeast requires Dsl1p, a component of the ER target site that interacts with a COPI coat subunit
    • Reilly BA, Kraynack BA, VanRheenen SM, and Waters MG. Golgito-endoplasmic reticulum (ER) retrograde traffic in yeast requires Dsl1p, a component of the ER target site that interacts with a COPI coat subunit. Mol Biol Cell 12: 3783-3796, 2001.
    • (2001) Mol Biol Cell , vol.12 , pp. 3783-3796
    • Reilly, B.A.1    Kraynack, B.A.2    VanRheenen, S.M.3    Waters, M.G.4
  • 109
    • 0028864441 scopus 로고
    • BET3 encodes a novel hydrophilic protein that acts in conjunction with yeast SNAREs
    • Rossi G, Kolstad K, Stone S, Pallnault F, and Ferro-Novick S. BET3 encodes a novel hydrophilic protein that acts in conjunction with yeast SNAREs. Mol Biol Cell 6: 1769-1780, 1995.
    • (1995) Mol Biol Cell , vol.6 , pp. 1769-1780
    • Rossi, G.1    Kolstad, K.2    Stone, S.3    Pallnault, F.4    Ferro-Novick, S.5
  • 110
    • 0037033044 scopus 로고    scopus 로고
    • Interaction with GM130 during HERG ion channel trafficking. Disruption by type 2 congenital long QT syndrome mutations. Human ether-à-go-go- related gene
    • Roti EC, Myers CD, Ayers RA, Boatman DE, Delfosse SA, Chan ER, Ackerman MJ, January CT, and Robertson GA. Interaction with GM130 during HERG ion channel trafficking. Disruption by type 2 congenital long QT syndrome mutations. Human ether-à-go-go-related gene. J Biol Chem 277: 47779-47785, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 47779-47785
    • Roti, E.C.1    Myers, C.D.2    Ayers, R.A.3    Boatman, D.E.4    Delfosse, S.A.5    Chan, E.R.6    Ackerman, M.J.7    January, C.T.8    Robertson, G.A.9
  • 113
    • 0035139779 scopus 로고    scopus 로고
    • Purification of TRAPP from Saccharomyces cerevisiae and identification of its mammalian counterpart
    • Sacher M and Ferro-Novick S. Purification of TRAPP from Saccharomyces cerevisiae and identification of its mammalian counterpart. Methods Enzymol 329: 234-241, 2001.
    • (2001) Methods Enzymol , vol.329 , pp. 234-241
    • Sacher, M.1    Ferro-Novick, S.2
  • 116
    • 0028816034 scopus 로고
    • p115 is a general vesicular transport factor related to the yeast endoplasmic reticulum to Golgi transport factor Uso1p
    • Sapperstein SK, Walter DM, Grosvenor AR, Heuser JE, and Waters MG. p115 is a general vesicular transport factor related to the yeast endoplasmic reticulum to Golgi transport factor Uso1p. Proc Natl Acad Sci USA 92: 522-526, 1995.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 522-526
    • Sapperstein, S.K.1    Walter, D.M.2    Grosvenor, A.R.3    Heuser, J.E.4    Waters, M.G.5
  • 117
    • 0013086419 scopus 로고    scopus 로고
    • Golgin-84 is a rab1 binding partner involved in golgi structure
    • Satoh A, Wang Y, Malsam J, Beard MB, and Warren G. Golgin-84 is a rab1 binding partner involved in golgi structure. Traffic 4: 153-161, 2003.
    • (2003) Traffic , vol.4 , pp. 153-161
    • Satoh, A.1    Wang, Y.2    Malsam, J.3    Beard, M.B.4    Warren, G.5
  • 118
    • 0037418580 scopus 로고    scopus 로고
    • Golgi recruitment of GRIP domain proteins by Arf-like GTPase 1 is regulated by Arf-like GTPase 3
    • Setty SR, Shin ME, Yoshino A, Marks MS, and Burd CG. Golgi recruitment of GRIP domain proteins by Arf-like GTPase 1 is regulated by Arf-like GTPase 3. Curr Biol 13: 401-404, 2003.
    • (2003) Curr Biol , vol.13 , pp. 401-404
    • Setty, S.R.1    Shin, M.E.2    Yoshino, A.3    Marks, M.S.4    Burd, C.G.5
  • 119
  • 120
    • 0037108473 scopus 로고    scopus 로고
    • The Rab6 GTPase regulates recruitment of the dynactin complex to Golgi membranes
    • Short B, Preisinger C, Schaletzky, Kopajtich R, and Barr FA. The Rab6 GTPase regulates recruitment of the dynactin complex to Golgi membranes. Curr Biol 12: 1792-1795, 2002.
    • (2002) Curr Biol , vol.12 , pp. 1792-1795
    • Short, B.1    Preisinger, C.2    Schaletzky3    Kopajtich, R.4    Barr, F.A.5
  • 121
    • 0036544571 scopus 로고    scopus 로고
    • Sequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115
    • Shorter J, Beard MB, Seeman J, Dirac-Svejstrup AB, and Warren G. Sequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115. J Cell Biol 157: 45-62, 2002.
    • (2002) J Cell Biol , vol.157 , pp. 45-62
    • Shorter, J.1    Beard, M.B.2    Seeman, J.3    Dirac-Svejstrup, A.B.4    Warren, G.5
  • 122
    • 0033568489 scopus 로고    scopus 로고
    • GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system
    • Shorter J, Watson R, Giannakou ME, Clarke M, Warren G, and Barr FA. GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system. EMBO J 18: 4949-4960, 1999.
    • (1999) EMBO J , vol.18 , pp. 4949-4960
    • Shorter, J.1    Watson, R.2    Giannakou, M.E.3    Clarke, M.4    Warren, G.5    Barr, F.A.6
  • 123
    • 0035503740 scopus 로고    scopus 로고
    • An effector of Ypt6p binds the SNARE Tlg1p and mediates selective fusion of vesicles with late Golgi membranes
    • Siniossoglou S and Pelham HR. An effector of Ypt6p binds the SNARE Tlg1p and mediates selective fusion of vesicles with late Golgi membranes. EMBO J 20: 5991-5998, 2001.
    • (2001) EMBO J , vol.20 , pp. 5991-5998
    • Siniossoglou, S.1    Pelham, H.R.2
  • 124
    • 0037073694 scopus 로고    scopus 로고
    • Vps51p links the VFT complex to the SNARE Tlg1p
    • Siniossoglou S and Pelham HR. Vps51p links the VFT complex to the SNARE Tlg1p. J Biol Chem 277: 48318-48324, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 48318-48324
    • Siniossoglou, S.1    Pelham, H.R.2
  • 125
    • 0035976927 scopus 로고    scopus 로고
    • Identification and characterization of a novel Golgi protein, GCP60, that interacts with the integral membrane protein giantin
    • Sohda M, Misumi Y, Yamamoto A, Yano A, Nakamura N, and Ikehara Y. Identification and characterization of a novel Golgi protein, GCP60, that interacts with the integral membrane protein giantin. J Biol Chem 276: 45298-45306, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 45298-45306
    • Sohda, M.1    Misumi, Y.2    Yamamoto, A.3    Yano, A.4    Nakamura, N.5    Ikehara, Y.6
  • 127
    • 0032734240 scopus 로고    scopus 로고
    • The yeast GRD20 gene is required for protein sorting in the trans-Golgi network/endosomal system and for polarization of the actin cytoskeleton
    • Spelbrink RG and Nothwehr SF. The yeast GRD20 gene is required for protein sorting in the trans-Golgi network/endosomal system and for polarization of the actin cytoskeleton. Mol Biol Cell 10: 4263-4281, 1999.
    • (1999) Mol Biol Cell , vol.10 , pp. 4263-4281
    • Spelbrink, R.G.1    Nothwehr, S.F.2
  • 128
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4A resolution
    • Sutton RB, Fasshauer D, Jahn R, and Brunger AT. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4A resolution. Nature 395: 347-353, 1998.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 129
    • 0037071543 scopus 로고    scopus 로고
    • The Sec34/Sec35p complex, a Ypt1p effector required for retrograde intra-Golgi trafficking, interacts with Golgi SNAREs and COPI vesicle coat proteins
    • Suvorova ES, Duden R, and Lupashin VV. The Sec34/Sec35p complex, a Ypt1p effector required for retrograde intra-Golgi trafficking, interacts with Golgi SNAREs and COPI vesicle coat proteins. J Cell Biol 157: 631-643, 2002.
    • (2002) J Cell Biol , vol.157 , pp. 631-643
    • Suvorova, E.S.1    Duden, R.2    Lupashin, V.V.3
  • 130
    • 0035933735 scopus 로고    scopus 로고
    • Identification of a human orthologue of Sec34p as a component of the cis-Golgi vesicle tethering machinery
    • Suvorova ES, Kurten RC, and Lupashin VV. Identification of a human orthologue of Sec34p as a component of the cis-Golgi vesicle tethering machinery. J Biol Chem 276: 22810-22818, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 22810-22818
    • Suvorova, E.S.1    Kurten, R.C.2    Lupashin, V.V.3
  • 131
    • 0029843493 scopus 로고    scopus 로고
    • The exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae
    • TerBush DR, Maurice T, Roth D, and Novick P. The exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae. EMBO J 15: 6483-6494, 1996.
    • (1996) EMBO J , vol.15 , pp. 6483-6494
    • TerBush, D.R.1    Maurice, T.2    Roth, D.3    Novick, P.4
  • 132
    • 0035158866 scopus 로고    scopus 로고
    • Selective formation of Sed5pcontaining SNARE complexes is mediated by combinatorial binding interactions
    • Tsui MM, Tai WC, and Banfield DK. Selective formation of Sed5pcontaining SNARE complexes is mediated by combinatorial binding interactions. Mol Biol Cell 12: 521-538, 2001.
    • (2001) Mol Biol Cell , vol.12 , pp. 521-538
    • Tsui, M.M.1    Tai, W.C.2    Banfield, D.K.3
  • 134
    • 0344393030 scopus 로고    scopus 로고
    • SNARE protein structure and function
    • Ungar D and Hughson. SNARE protein structure and function. Annu Rev Cell Dev Biol 19: 493-517, 2003.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 493-517
    • Ungar, D.1    Hughson2
  • 137
    • 0033571293 scopus 로고    scopus 로고
    • Sec34p, a protein required for vesicle tethering to the yeast Golgi apparatus, is in a complex with Sec35p
    • VanRheenen SM, Cao X, Lupashin VV, Barlowe C, and Waters MG. Sec34p, a protein required for vesicle tethering to the yeast Golgi apparatus, is in a complex with Sec35p. J Cell Biol 147: 729-742, 1999.
    • (1999) J Cell Biol , vol.147 , pp. 729-742
    • VanRheenen, S.M.1    Cao, X.2    Lupashin, V.V.3    Barlowe, C.4    Waters, M.G.5
  • 138
    • 0035016821 scopus 로고    scopus 로고
    • Dsl1p, an essential protein required for membrane traffic at the endoplasmic reticulum/Golgi interface in yeast
    • VanRheenen SM, Reilly BA, Chamberlain SJ, and Waters MG. Dsl1p, an essential protein required for membrane traffic at the endoplasmic reticulum/Golgi interface in yeast. Traffic 2: 212-231, 2001.
    • (2001) Traffic , vol.2 , pp. 212-231
    • VanRheenen, S.M.1    Reilly, B.A.2    Chamberlain, S.J.3    Waters, M.G.4
  • 139
    • 0013086420 scopus 로고    scopus 로고
    • Structural integrity of the Golgi is temperature sensitive in conditional-lethal mutants with no detectable GM130
    • Vasile E, Perez T, Nakmura N, and Krieger M. Structural integrity of the Golgi is temperature sensitive in conditional-lethal mutants with no detectable GM130. Traffic 4: 254-272, 2003.
    • (2003) Traffic , vol.4 , pp. 254-272
    • Vasile, E.1    Perez, T.2    Nakmura, N.3    Krieger, M.4
  • 140
    • 0035809910 scopus 로고    scopus 로고
    • The Golgi-associated hook3 protein is a member of a novel family of microtubule-binding proteins
    • Walenta JH, Didier AJ, Liu X, and Kramer H. The Golgi-associated hook3 protein is a member of a novel family of microtubule-binding proteins. J Cell Biol 152: 923-934, 2001.
    • (2001) J Cell Biol , vol.152 , pp. 923-934
    • Walenta, J.H.1    Didier, A.J.2    Liu, X.3    Kramer, H.4
  • 141
    • 0034676094 scopus 로고    scopus 로고
    • TRAPP stimulates guanine nucleotide exchange on Ypt1p
    • Wang W, Sacher M, and Ferro-Novick S. TRAPP stimulates guanine nucleotide exchange on Ypt1p. J Cell Biol 151: 289-296, 2000.
    • (2000) J Cell Biol , vol.151 , pp. 289-296
    • Wang, W.1    Sacher, M.2    Ferro-Novick, S.3
  • 143
    • 0026674071 scopus 로고
    • A novel 115-kD peripheral membrane protein is required for intercisternal transport in the Golgi stack
    • Waters MG, Clary DO, and Rothman JE. A novel 115-kD peripheral membrane protein is required for intercisternal transport in the Golgi stack. J Cell Biol 118: 1015-1026, 1992.
    • (1992) J Cell Biol , vol.118 , pp. 1015-1026
    • Waters, M.G.1    Clary, D.O.2    Rothman, J.E.3
  • 144
    • 0035489304 scopus 로고    scopus 로고
    • The Sec34/35 Golgi transport complex is related to the exocyst, defining a family of complexes involved in multiple steps of membrane traffic
    • Whyte JR and Munro S. The Sec34/35 Golgi transport complex is related to the exocyst, defining a family of complexes involved in multiple steps of membrane traffic. Developmental Cell 1: 527-537, 2001.
    • (2001) Developmental Cell , vol.1 , pp. 527-537
    • Whyte, J.R.1    Munro, S.2
  • 146
    • 0842269776 scopus 로고    scopus 로고
    • Structural basis for recruitment of GRIP domain golgin-245 by small GTPase Arl1
    • Wu M, Lu L, Hong W, and Song H. Structural basis for recruitment of GRIP domain golgin-245 by small GTPase Arl1. Nat Struct Mol Biol 11: 86-94, 2004.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 86-94
    • Wu, M.1    Lu, L.2    Hong, W.3    Song, H.4
  • 148
    • 0030050828 scopus 로고    scopus 로고
    • New mutants of Saccharomyces cerevisiae affected in the transport of proteins from the endoplasmic reticulum to the Golgi complex
    • Wuestehube LJ, Duden R, Eun A, Hamamoto S, Korn P, Ram R, and Scheckman R. New mutants of Saccharomyces cerevisiae affected in the transport of proteins from the endoplasmic reticulum to the Golgi complex. Genetics 142: 393-406, 1996.
    • (1996) Genetics , vol.142 , pp. 393-406
    • Wuestehube, L.J.1    Duden, R.2    Eun, A.3    Hamamoto, S.4    Korn, P.5    Ram, R.6    Scheckman, R.7
  • 149
    • 0036800355 scopus 로고    scopus 로고
    • GS15 forms a SNARE complex with syntaxin 5, GS28, and Ykt6 and is implicated in traffic in the early cisternae of the Golgi apparatus
    • Xu Y, Martin S, James DE, and Hong W. GS15 forms a SNARE complex with syntaxin 5, GS28, and Ykt6 and is implicated in traffic in the early cisternae of the Golgi apparatus. Mol Biol Cell 13: 3493-3507, 2002.
    • (2002) Mol Biol Cell , vol.13 , pp. 3493-3507
    • Xu, Y.1    Martin, S.2    James, D.E.3    Hong, W.4
  • 150
    • 0030010763 scopus 로고    scopus 로고
    • Uso1 protein is a dimer with two globular heads and a long coiled-coil tail
    • Yamakawa H, Seog DH, Yoda K, Yamasaki M, and Wakabayashi T. Uso1 protein is a dimer with two globular heads and a long coiled-coil tail. J Struct Biol 116: 356-365, 1996.
    • (1996) J Struct Biol , vol.116 , pp. 356-365
    • Yamakawa, H.1    Seog, D.H.2    Yoda, K.3    Yamasaki, M.4    Wakabayashi, T.5
  • 152
    • 1242284588 scopus 로고    scopus 로고
    • Mechanism of recruiting Sec6/8 (exocyst) complex to the apical junctional complex during polarization of epithelial cells
    • Yeaman C, Grindstaff KK, and Nelson WJ. Mechanism of recruiting Sec6/8 (exocyst) complex to the apical junctional complex during polarization of epithelial cells. J Cell Sci 117: 559-570, 2004.
    • (2004) J Cell Sci , vol.117 , pp. 559-570
    • Yeaman, C.1    Grindstaff, K.K.2    Nelson, W.J.3
  • 155
    • 14844310335 scopus 로고    scopus 로고
    • Cyclical regulation of the exocyst and cell polarity determinants for polarized cell growth
    • Zajac A, Sun X, Zhang J, and Guo W. Cyclical regulation of the exocyst and cell polarity determinants for polarized cell growth. Mol Biol Cell 16: 1500-1512, 2005.
    • (2005) Mol Biol Cell , vol.16 , pp. 1500-1512
    • Zajac, A.1    Sun, X.2    Zhang, J.3    Guo, W.4
  • 156
    • 14744272136 scopus 로고    scopus 로고
    • Cog3p depletion blocks vesicle-mediated Golgi retrograde trafficking in HeLa cells
    • Zolov SN and Lupashin VV. Cog3p depletion blocks vesicle-mediated Golgi retrograde trafficking in HeLa cells. J Cell Biol 168: 747-759, 2005.
    • (2005) J Cell Biol , vol.168 , pp. 747-759
    • Zolov, S.N.1    Lupashin, V.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.