메뉴 건너뛰기




Volumn 10, Issue 4, 1998, Pages 477-482

Transport from the endoplasmic reticulum to the Golgi

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANE PROTEIN; COAT PROTEIN; MEMBRANE PROTEIN;

EID: 0032145891     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(98)80062-8     Document Type: Article
Times cited : (31)

References (57)
  • 5
    • 0028966452 scopus 로고
    • Human SEC13Rp functions in yeast and is located on transport vesicles budding from the endoplasmic reticulum
    • Shaywitz DA, Orci L, Ravazzola M, Swaroop A, Kaiser CA. Human SEC13Rp functions in yeast and is located on transport vesicles budding from the endoplasmic reticulum. J Cell Biol. 128:1995;769-777.
    • (1995) J Cell Biol , vol.128 , pp. 769-777
    • Shaywitz, D.A.1    Orci, L.2    Ravazzola, M.3    Swaroop, A.4    Kaiser, C.A.5
  • 8
    • 0028070987 scopus 로고
    • Vesicle fusion from yeast to man
    • Ferro-Novick S, Jahn R. Vesicle fusion from yeast to man. Nature. 370:1994;191-193.
    • (1994) Nature , vol.370 , pp. 191-193
    • Ferro-Novick, S.1    Jahn, R.2
  • 9
    • 0025277750 scopus 로고
    • Distinct sets of SEC genes govern transport vesicle formation and fusion early in the secretory pathway
    • Kaiser CA, Schekman R. Distinct sets of SEC genes govern transport vesicle formation and fusion early in the secretory pathway. Cell. 61:1990;723-733.
    • (1990) Cell , vol.61 , pp. 723-733
    • Kaiser, C.A.1    Schekman, R.2
  • 10
    • 0024299523 scopus 로고
    • Reconstitution of SEC gene product-dependent intercompartmental protein transport
    • Baker D, Hicke L, Rexach M, Schleyer M, Schekman R. Reconstitution of SEC gene product-dependent intercompartmental protein transport. Cell. 54:1988;335-344.
    • (1988) Cell , vol.54 , pp. 335-344
    • Baker, D.1    Hicke, L.2    Rexach, M.3    Schleyer, M.4    Schekman, R.5
  • 11
    • 0024094641 scopus 로고
    • Reconstitution of protein transport from the endoplasmic reticulum to the Golgi complex in yeast: The acceptor Golgi compartment is defective in the sec23 mutant
    • Ruohola H, Kabcenell AK, Ferro-Novick S. Reconstitution of protein transport from the endoplasmic reticulum to the Golgi complex in yeast: the acceptor Golgi compartment is defective in the sec23 mutant. J Cell Biol. 107:1988;1465-1476.
    • (1988) J Cell Biol , vol.107 , pp. 1465-1476
    • Ruohola, H.1    Kabcenell, A.K.2    Ferro-Novick, S.3
  • 12
    • 0025775567 scopus 로고
    • Distinct biochemical requirements for the budding, targeting, and fusion of ER-derived transport vesicles
    • Rexach MF, Schekman RW. Distinct biochemical requirements for the budding, targeting, and fusion of ER-derived transport vesicles. J Cell Biol. 114:1991;219-229.
    • (1991) J Cell Biol , vol.114 , pp. 219-229
    • Rexach, M.F.1    Schekman, R.W.2
  • 13
    • 0027454503 scopus 로고
    • The Sec13p complex and reconstitution of vesicle budding from the ER with purified cytosolic proteins
    • Salama NR, Yeung T, Schekman RW. The Sec13p complex and reconstitution of vesicle budding from the ER with purified cytosolic proteins. EMBO J. 12:1993;4073-4082.
    • (1993) EMBO J , vol.12 , pp. 4073-4082
    • Salama, N.R.1    Yeung, T.2    Schekman, R.W.3
  • 14
    • 0027500969 scopus 로고
    • SEC12 encodes a guanine-nucleotide-exchange factor essential for transport vesicle budding from the ER
    • Barlowe C, Schekman R. SEC12 encodes a guanine-nucleotide-exchange factor essential for transport vesicle budding from the ER. Nature. 365:1993;347-349.
    • (1993) Nature , vol.365 , pp. 347-349
    • Barlowe, C.1    Schekman, R.2
  • 15
    • 0027467609 scopus 로고
    • Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum
    • Yoshihisa T, Barlowe C, Schekman R. Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum. Science. 259:1993;1466-1468.
    • (1993) Science , vol.259 , pp. 1466-1468
    • Yoshihisa, T.1    Barlowe, C.2    Schekman, R.3
  • 16
    • 0028089202 scopus 로고
    • Inhibition of GTP hydrolysis by Sar1p causes accumulation of vesicles that are a functional intermediate of the ER-to-Golgi transport in yeast
    • Oka T, Nakano A. Inhibition of GTP hydrolysis by Sar1p causes accumulation of vesicles that are a functional intermediate of the ER-to-Golgi transport in yeast. J Cell Biol. 124:1994;425-434.
    • (1994) J Cell Biol , vol.124 , pp. 425-434
    • Oka, T.1    Nakano, A.2
  • 17
    • 0028803617 scopus 로고
    • Yeast SEC16 gene encodes a multidomain vesicle coat protein that interacts with Sec23p
    • Espenshade P, Gimeno RE, Holzmacher E, Teung P, Kaiser CA. Yeast SEC16 gene encodes a multidomain vesicle coat protein that interacts with Sec23p. J Cell Biol. 131:1995;311-324.
    • (1995) J Cell Biol , vol.131 , pp. 311-324
    • Espenshade, P.1    Gimeno, R.E.2    HolzMacHer, E.3    Teung, P.4    Kaiser, C.A.5
  • 18
    • 0031017668 scopus 로고    scopus 로고
    • Selective packaging of cargo molecules into endoplasmic reticulum-derived COPII vesicles
    • Campbell JL, Schekman R. Selective packaging of cargo molecules into endoplasmic reticulum-derived COPII vesicles. Proc Natl Acad Sci USA. 94:1997;837-842.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 837-842
    • Campbell, J.L.1    Schekman, R.2
  • 19
    • 0029905137 scopus 로고    scopus 로고
    • COPII coat subunit interactions: Sec24p and Sec23p bind to adjacent regions of Sec16p
    • Gimeno RE, Espenshade P, Kaiser CA. COPII coat subunit interactions: Sec24p and Sec23p bind to adjacent regions of Sec16p. Mol Biol Cell. 7:1996;1815-1823.
    • (1996) Mol Biol Cell , vol.7 , pp. 1815-1823
    • Gimeno, R.E.1    Espenshade, P.2    Kaiser, C.A.3
  • 20
    • 0030771853 scopus 로고    scopus 로고
    • COPII subunit interactions in the assembly of the vesicle coat
    • of outstanding interest. A combination of two-hybrid assays and binding studies are used to map contacts among COPII subunits. Independent domains of Sec16p that bind to Sec24p or Sec31p as well as domains of Sec31p that bind Sec13p, Sec23p or Sec24p are defined.
    • Shaywitz DA, Espenshade PJ, Gimeno RE, Kaiser CA. COPII subunit interactions in the assembly of the vesicle coat. of outstanding interest J Biol Chem. 272:1997;25413-25416 A combination of two-hybrid assays and binding studies are used to map contacts among COPII subunits. Independent domains of Sec16p that bind to Sec24p or Sec31p as well as domains of Sec31p that bind Sec13p, Sec23p or Sec24p are defined.
    • (1997) J Biol Chem , vol.272 , pp. 25413-25416
    • Shaywitz, D.A.1    Espenshade, P.J.2    Gimeno, R.E.3    Kaiser, C.A.4
  • 21
    • 18344405156 scopus 로고    scopus 로고
    • COPII-coated vesicle formation reconstituted with purified coat proteins and chemically-defined liposomes
    • of outstanding interest. The first in vitro reconstitution of vesicle budding using completely defined components. Purified Sar1p, Sec23p/Sec24p, and Sec31p/Sec13p will co-assemble on liposomes that contain acidic phospholipids. The heterogeneous vesicles that form are morphologically similar to native coatomer protein II (COPII) vesicles.
    • Matsuoka K, Orci L, Amherdt M, Bednarek SY, Hamamoto S, Schekman R, Yeung T. COPII-coated vesicle formation reconstituted with purified coat proteins and chemically-defined liposomes. of outstanding interest Cell. 93:1998;263-275 The first in vitro reconstitution of vesicle budding using completely defined components. Purified Sar1p, Sec23p/Sec24p, and Sec31p/Sec13p will co-assemble on liposomes that contain acidic phospholipids. The heterogeneous vesicles that form are morphologically similar to native coatomer protein II (COPII) vesicles.
    • (1998) Cell , vol.93 , pp. 263-275
    • Matsuoka, K.1    Orci, L.2    Amherdt, M.3    Bednarek, S.Y.4    Hamamoto, S.5    Schekman, R.6    Yeung, T.7
  • 22
    • 0028142838 scopus 로고
    • Ceramide synthesis enhances transport of GPI-anchored proteins to the Golgi apparatus in yeast
    • Horvath A, Sutterlin C, Manning-Krieg U, Movva NR, Riezman H. Ceramide synthesis enhances transport of GPI-anchored proteins to the Golgi apparatus in yeast. EMBO J. 13:1994;3687-3695.
    • (1994) EMBO J , vol.13 , pp. 3687-3695
    • Horvath, A.1    Sutterlin, C.2    Manning-Krieg, U.3    Movva, N.R.4    Riezman, H.5
  • 23
    • 0031038655 scopus 로고    scopus 로고
    • Suppressor gene analysis reveals an essential role for sphingolipids in transport of glycosylphosphatidylinositol-anchored proteins in Saccharomyces cerevisiae
    • Skrzypek M, Lester RL, Dickson RC. Suppressor gene analysis reveals an essential role for sphingolipids in transport of glycosylphosphatidylinositol-anchored proteins in Saccharomyces cerevisiae. J Bacteriol. 179:1997;1513-1520.
    • (1997) J Bacteriol , vol.179 , pp. 1513-1520
    • Skrzypek, M.1    Lester, R.L.2    Dickson, R.C.3
  • 24
    • 0029094253 scopus 로고
    • A quality control in the secretory pathway
    • Hammond C, Helenius A. A quality control in the secretory pathway. Curr Opin Cell Biol. 7:1995;523-529.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 523-529
    • Hammond, C.1    Helenius, A.2
  • 25
    • 23444432144 scopus 로고
    • Vesicular stomatitis virus glycoprotein is sorted and concentrated during export from the endoplasmic reticulum
    • Balch WE, McCaffery JM, Plutner H, Farquhar MG. Vesicular stomatitis virus glycoprotein is sorted and concentrated during export from the endoplasmic reticulum. Cell. 76:1994;841-852.
    • (1994) Cell , vol.76 , pp. 841-852
    • Balch, W.E.1    McCaffery, J.M.2    Plutner, H.3    Farquhar, M.G.4
  • 27
    • 0030812940 scopus 로고    scopus 로고
    • A di-acidic signal required for selective export from the endoplasmic reticulum
    • of special interest. The motif Asp - X - Glu within the carboxy-terminal cytosolic tail of the VSVG protein is shown to be important for efficient transport from the endoplasmic reticulum to the Golgi.
    • Nishimura N, Balch WE. A di-acidic signal required for selective export from the endoplasmic reticulum. of special interest Science. 277:1997;556-558 The motif Asp - X - Glu within the carboxy-terminal cytosolic tail of the VSVG protein is shown to be important for efficient transport from the endoplasmic reticulum to the Golgi.
    • (1997) Science , vol.277 , pp. 556-558
    • Nishimura, N.1    Balch, W.E.2
  • 28
    • 0029796074 scopus 로고    scopus 로고
    • Bimodal interaction of coatomer with the p24 family of putative cargo receptors
    • Fiedler K, Veit M, Stamnes MA, Rothman JE. Bimodal interaction of coatomer with the p24 family of putative cargo receptors. Science. 273:1996;1396-1399.
    • (1996) Science , vol.273 , pp. 1396-1399
    • Fiedler, K.1    Veit, M.2    Stamnes, M.A.3    Rothman, J.E.4
  • 29
    • 0032559651 scopus 로고    scopus 로고
    • Gp25L/emp24/p24 protein family members of the cis-Golgi network bind both COP I and II coatomer
    • of special interest. Paired phenylalanine residues within the cytosolic tail of p24 proteins are shown to be necessary for their efficient transport out of the endoplasmic reticulum. Peptides containing this motif are shown to bind to the Sec23p/Sec24p complex in mammalian cell extracts.
    • Dominguez M, Dejgaard K, Fullekrug J, Dahan S, Fazel A, Paccaud JP, Thomas DY, Bergeron JJ, Nilsson T. gp25L/emp24/p24 protein family members of the cis-Golgi network bind both COP I and II coatomer. of special interest J Cell Biol. 140:1998;751-765 Paired phenylalanine residues within the cytosolic tail of p24 proteins are shown to be necessary for their efficient transport out of the endoplasmic reticulum. Peptides containing this motif are shown to bind to the Sec23p/Sec24p complex in mammalian cell extracts.
    • (1998) J Cell Biol , vol.140 , pp. 751-765
    • Dominguez, M.1    Dejgaard, K.2    Fullekrug, J.3    Dahan, S.4    Fazel, A.5    Paccaud, J.P.6    Thomas, D.Y.7    Bergeron, J.J.8    Nilsson, T.9
  • 30
    • 0031450221 scopus 로고    scopus 로고
    • The recycling of ERGIC-53 in the early secretory pathway. ERGIC-53 carries a cytosolic endoplasmic reticulum-exit determinant interacting with COPII
    • of special interest. Similar to the case described in [29], paired Phe residues in the cytosolic tail of ERGIC-53 are shown to be important for transport out of the endoplasmic reticulum. Peptides based on the tail sequence are also shown to bind to the mammalian Sec23p/Sec24p complex.
    • Kappeler F, Klopfenstein DR, Foguet M, Paccaud JP, Hauri HP. The recycling of ERGIC-53 in the early secretory pathway. ERGIC-53 carries a cytosolic endoplasmic reticulum-exit determinant interacting with COPII. of special interest J Biol Chem. 272:1997;31801-31808 Similar to the case described in [29], paired Phe residues in the cytosolic tail of ERGIC-53 are shown to be important for transport out of the endoplasmic reticulum. Peptides based on the tail sequence are also shown to bind to the mammalian Sec23p/Sec24p complex.
    • (1997) J Biol Chem , vol.272 , pp. 31801-31808
    • Kappeler, F.1    Klopfenstein, D.R.2    Foguet, M.3    Paccaud, J.P.4    Hauri, H.P.5
  • 31
    • 0032495477 scopus 로고    scopus 로고
    • COPII-cargo interactions direct protein sorting into ER-derived transport vesicles
    • of outstanding interest. This paper describes the first isolation of a complex containing both coatomer protein II (COPII) coat proteins and vesicle cargo proteins. Yeast Sar1p stimulates assembly of Sec23p/Sec24p onto microsomal membranes. On detergent solubilization of the membrane both integral membrane and soluble proteins are associated with this pre-budding complex.
    • Kuehn MJ, Herrmann JM, Schekman R. COPII-cargo interactions direct protein sorting into ER-derived transport vesicles. of outstanding interest Nature. 391:1998;187-190 This paper describes the first isolation of a complex containing both coatomer protein II (COPII) coat proteins and vesicle cargo proteins. Yeast Sar1p stimulates assembly of Sec23p/Sec24p onto microsomal membranes. On detergent solubilization of the membrane both integral membrane and soluble proteins are associated with this pre-budding complex.
    • (1998) Nature , vol.391 , pp. 187-190
    • Kuehn, M.J.1    Herrmann, J.M.2    Schekman, R.3
  • 32
    • 0032489878 scopus 로고    scopus 로고
    • Cargo selection by the COPII budding machinery during export from the ER
    • of outstanding interest. A parallel study to that described in reference [31] that employs both coatomer protein II (COPII) subunits and microsomal membranes that are derived from mammalian cells. The integral membrane protein VSVG can be extracted from membranes in association with Sar1p and Sec23p/Sec24p.
    • Aridor M, Weissman J, Bannykh S, Nuoffer C, Balch WE. Cargo selection by the COPII budding machinery during export from the ER. of outstanding interest J Cell Biol. 141:1998;61-70 A parallel study to that described in reference [31] that employs both coatomer protein II (COPII) subunits and microsomal membranes that are derived from mammalian cells. The integral membrane protein VSVG can be extracted from membranes in association with Sar1p and Sec23p/Sec24p.
    • (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
  • 33
    • 0028964475 scopus 로고
    • The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi
    • Schimmoller F, Singer-Kruger B, Schroder S, Kruger U, Barlowe C, Riezman H. The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi. EMBO J. 14:1995;1329-1339.
    • (1995) EMBO J , vol.14 , pp. 1329-1339
    • Schimmoller, F.1    Singer-Kruger, B.2    Schroder, S.3    Kruger, U.4    Barlowe, C.5    Riezman, H.6
  • 34
    • 0029910214 scopus 로고    scopus 로고
    • Erv25p, a component of COPII-coated vesicles, forms a complex with Emp24p that is required for efficient endoplasmic reticulum to Golgi transport
    • Belden WJ, Barlowe C. Erv25p, a component of COPII-coated vesicles, forms a complex with Emp24p that is required for efficient endoplasmic reticulum to Golgi transport. J Biol Chem. 271:1996;26939-26946.
    • (1996) J Biol Chem , vol.271 , pp. 26939-26946
    • Belden, W.J.1    Barlowe, C.2
  • 35
    • 0030015550 scopus 로고    scopus 로고
    • Genes that control the fidelity of endoplasmic reticulum to Golgi transport identified as suppressors of vesicle budding mutations
    • Elrod-Erickson MJ, Kaiser CA. Genes that control the fidelity of endoplasmic reticulum to Golgi transport identified as suppressors of vesicle budding mutations. Mol Biol Cell. 7:1996;1043-1058.
    • (1996) Mol Biol Cell , vol.7 , pp. 1043-1058
    • Elrod-Erickson, M.J.1    Kaiser, C.A.2
  • 36
    • 0030955328 scopus 로고    scopus 로고
    • ER-to-Golgi transport visualized in living cells
    • of outstanding interest. This paper describes the transport of pre-Golgi structures in living cells. The authors show that the ER-to-Golgi transport intermediate is not a small vesicle.
    • Presley JF, Cole NB, Schroer TA, Hirschberg K, Zaal KJM, Lippincott-Schwartz J. ER-to-Golgi transport visualized in living cells. of outstanding interest Nature. 389:1997;81-85 This paper describes the transport of pre-Golgi structures in living cells. The authors show that the ER-to-Golgi transport intermediate is not a small vesicle.
    • (1997) Nature , vol.389 , pp. 81-85
    • Presley, J.F.1    Cole, N.B.2    Schroer, T.A.3    Hirschberg, K.4    Zaal, K.J.M.5    Lippincott-Schwartz, J.6
  • 37
    • 0030928782 scopus 로고    scopus 로고
    • Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI
    • of outstanding interest. The findings presented here indicate that coatomer proteins COPII and COPI act sequentially in the transport of pre-Golgi structures.
    • Scales SJ, Pepperkok R, Kreis TE. Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI. of outstanding interest Cell. 90:1997;1137-1148 The findings presented here indicate that coatomer proteins COPII and COPI act sequentially in the transport of pre-Golgi structures.
    • (1997) Cell , vol.90 , pp. 1137-1148
    • Scales, S.J.1    Pepperkok, R.2    Kreis, T.E.3
  • 38
    • 0016785996 scopus 로고
    • Intracellular aspects of the processing of protein synthesis
    • Palade GE. Intracellular aspects of the processing of protein synthesis. Science. 189:1975;347-358.
    • (1975) Science , vol.189 , pp. 347-358
    • Palade, G.E.1
  • 39
    • 0027165412 scopus 로고
    • β-COP is essential for transport of protein from the endoplasmic reticulum to the Golgi in vitro
    • Peter F, Plutner H, Kreis T, Balch WE. β-COP is essential for transport of protein from the endoplasmic reticulum to the Golgi in vitro. J Cell Biol. 122:1993;1155-1168.
    • (1993) J Cell Biol , vol.122 , pp. 1155-1168
    • Peter, F.1    Plutner, H.2    Kreis, T.3    Balch, W.E.4
  • 40
    • 0027241227 scopus 로고
    • Boslp, an integral membrane protein of the endoplasmic reticulum to Golgi transport vesicles, is required for their fusion competence
    • Lian JP, Ferro-Novick S. Boslp, an integral membrane protein of the endoplasmic reticulum to Golgi transport vesicles, is required for their fusion competence. Cell. 73:1993;735-745.
    • (1993) Cell , vol.73 , pp. 735-745
    • Lian, J.P.1    Ferro-Novick, S.2
  • 41
    • 0032579295 scopus 로고    scopus 로고
    • Role of vesicle-associated syntaxin 5 in the assembly of pre-Golgi intermediates
    • of special interest. The authors show that the vesicle pool of syntaxin 5 is required for the formation of VTCs and the delivery of cargo to the Golgi.
    • Rowe T, Dascher C, Bannykh S, Plutner H, Balch WE. Role of vesicle-associated syntaxin 5 in the assembly of pre-Golgi intermediates. of special interest Science. 279:1998;696-700 The authors show that the vesicle pool of syntaxin 5 is required for the formation of VTCs and the delivery of cargo to the Golgi.
    • (1998) Science , vol.279 , pp. 696-700
    • Rowe, T.1    Dascher, C.2    Bannykh, S.3    Plutner, H.4    Balch, W.E.5
  • 43
    • 0032549708 scopus 로고    scopus 로고
    • SNAREpins: Minimal machinery for membrane fusion
    • of special interest. Using an assay based on lipid mixing, SNARE proteins are shown by the authors of this paper to be sufficient to catalyze the fusion of chemically defined liposomes.
    • Weber T, Zemelman BV, McNew JA, Westermann B, Gmachl M, Parlati F, Söllner T, Rothman JE. SNAREpins: minimal machinery for membrane fusion. of special interest Cell. 92:1998;759-772 Using an assay based on lipid mixing, SNARE proteins are shown by the authors of this paper to be sufficient to catalyze the fusion of chemically defined liposomes.
    • (1998) Cell , vol.92 , pp. 759-772
    • Weber, T.1    Zemelman, B.V.2    McNew, J.A.3    Westermann, B.4    GMacHl, M.5    Parlati, F.6    Söllner, T.7    Rothman, J.E.8
  • 44
    • 0028030275 scopus 로고
    • Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis
    • Brennwald P, Kearns B, Champion K, Keränen S, Bankaitis V, Novick P. Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis. Cell. 79:1994;245-258.
    • (1994) Cell , vol.79 , pp. 245-258
    • Brennwald, P.1    Kearns, B.2    Champion, K.3    Keränen, S.4    Bankaitis, V.5    Novick, P.6
  • 45
    • 0028945592 scopus 로고
    • RbSec1A and B co-localize with Syntaxin 1 and SNAP-25 throughout the axon, but are not in a stable complex with syntaxin
    • Garcia EP, McPherson PS, Chilcote TJ, Takei K, DeCamilli P. rbSec1A and B co-localize with Syntaxin 1 and SNAP-25 throughout the axon, but are not in a stable complex with syntaxin. J Cell Biol. 129:1995;105-120.
    • (1995) J Cell Biol , vol.129 , pp. 105-120
    • Garcia, E.P.1    McPherson, P.S.2    Chilcote, T.J.3    Takei, K.4    Decamilli, P.5
  • 46
    • 0030990122 scopus 로고    scopus 로고
    • The yeast v-SNARE Vti1p mediates two vesicle transport pathways through interactions with the t-SNAREs Sed5p and Pepl2p
    • Fischer von Mollard G, Nothwehr FS, Stevens TH. The yeast v-SNARE Vti1p mediates two vesicle transport pathways through interactions with the t-SNAREs Sed5p and Pepl2p. J Cell Biol. 137:1997;1511-1524.
    • (1997) J Cell Biol , vol.137 , pp. 1511-1524
    • Fischer Von Mollard, G.1    Nothwehr, F.S.2    Stevens, T.H.3
  • 48
    • 0032080081 scopus 로고    scopus 로고
    • TRAPP, a highly conserved novel complex on the cis-Golgi that mediates vesicle docking and fusion
    • of outstanding interest. Describes a novel component of the secretory apparatus that is a candidate targeting complex for ER-to-Golgi transport vesicles.
    • Sacher M, Jiang Y, Barrowman J, Scarpa A, Burston J, Zhang L, Schieltz D, Yates JR III, Abeliovich H, Ferro-Novick S. TRAPP, a highly conserved novel complex on the cis-Golgi that mediates vesicle docking and fusion. of outstanding interest EMBO J. 17:1998;2494-2503 Describes a novel component of the secretory apparatus that is a candidate targeting complex for ER-to-Golgi transport vesicles.
    • (1998) EMBO J , vol.17 , pp. 2494-2503
    • Sacher, M.1    Jiang, Y.2    Barrowman, J.3    Scarpa, A.4    Burston, J.5    Zhang, L.6    Schieltz, D.7    Yates J.R. III8    Abeliovich, H.9    Ferro-Novick, S.10
  • 49
    • 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, 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. 149:1998;833-842.
    • (1998) Genetics , vol.149 , pp. 833-842
    • Jiang, Y.1    Scarpa, A.2    Zhang, L.3    Stone, S.4    Feliciano, E.5    Ferro-Novick, S.6
  • 50
    • 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. 139:1997;1097-1108.
    • (1997) J Cell Biol , vol.139 , pp. 1097-1108
    • Barlowe, C.1
  • 54
    • 0031001794 scopus 로고    scopus 로고
    • T-SNARE activation through transient interaction with a Rab-like guanosine triphosphatase
    • Lupashin VV, Waters MG. t-SNARE activation through transient interaction with a Rab-like guanosine triphosphatase. Science. 276:1997;1255-1258.
    • (1997) Science , vol.276 , pp. 1255-1258
    • Lupashin, V.V.1    Waters, M.G.2
  • 55
    • 0029932226 scopus 로고    scopus 로고
    • SNARE-mediated retrograde traffic from the Golgi complex to the endoplasmic reticulum
    • Lewis MJ, Pelham HRB. SNARE-mediated retrograde traffic from the Golgi complex to the endoplasmic reticulum. Cell. 85:1996;205-215.
    • (1996) Cell , vol.85 , pp. 205-215
    • Lewis, M.J.1    Pelham, H.R.B.2
  • 56
    • 0030911653 scopus 로고    scopus 로고
    • A novel SNARE complex implicated in vesicle fusion with the endoplasmic reticulum
    • Lewis MJ, Rayner JC, Pelham HRB. A novel SNARE complex implicated in vesicle fusion with the endoplasmic reticulum. EMBO J. 16:1997;3017-3024.
    • (1997) EMBO J , vol.16 , pp. 3017-3024
    • Lewis, M.J.1    Rayner, J.C.2    Pelham, H.R.B.3
  • 57
    • 0029843493 scopus 로고    scopus 로고
    • The exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisae
    • TerBush DR, Maurice T, Roth D, Novick P. The exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisae. EMBO J. 15:1996;6483-6494.
    • (1996) EMBO J , vol.15 , pp. 6483-6494
    • Terbush, D.R.1    Maurice, T.2    Roth, D.3    Novick, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.