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Volumn 8, Issue 6, 1998, Pages

Vesicle transport: More work for the Rabs?

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EID: 0032510397     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/s0960-9822(98)70124-1     Document Type: Short Survey
Times cited : (20)

References (26)
  • 1
    • 0027525103 scopus 로고
    • Friends and family: The role of the Rab GTPases in vesicular traffic
    • Novick PJ, Brennwald P: Friends and family: the role of the Rab GTPases in vesicular traffic. Cell 1993, 75:597-601.
    • (1993) Cell , vol.75 , pp. 597-601
    • Novick, P.J.1    Brennwald, P.2
  • 3
    • 0031001794 scopus 로고    scopus 로고
    • t-SNARE activation through transient interaction with a Rab-like guanosine triphosphatase
    • Lupashin W, Waters MG: t-SNARE activation through transient interaction with a Rab-like guanosine triphosphatase. Science 1997, 276:1255-1258.
    • (1997) Science , vol.276 , pp. 1255-1258
    • Lupashin, W.1    Waters, M.G.2
  • 4
    • 0030796026 scopus 로고    scopus 로고
    • SNAREs and NSF in targeted membrane fusion
    • Hay JC, Scheller RH: SNAREs and NSF in targeted membrane fusion. Curr Opin Cell Biol 1997, 9:505-512.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 505-512
    • Hay, J.C.1    Scheller, R.H.2
  • 5
    • 0030860083 scopus 로고    scopus 로고
    • The diversity of Rab proteins in vesicle transport
    • Novick P, Zerial M: The diversity of Rab proteins in vesicle transport. Curr Opin Cell Biol 1997, 9:496-504.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 496-504
    • Novick, P.1    Zerial, M.2
  • 10
    • 0028065120 scopus 로고
    • Guanine nucleotide dissociation inhibitor is essential for Rab1 function in budding from the endoplasmic reticulum and transport through the Golgi stack
    • Peter F, Nuoffer C, Pind SN, Balch WE: Guanine nucleotide dissociation inhibitor is essential for Rab1 function in budding from the endoplasmic reticulum and transport through the Golgi stack. J Cell Biol 1994, 126:1393-1406.
    • (1994) J Cell Biol , vol.126 , pp. 1393-1406
    • Peter, F.1    Nuoffer, C.2    Pind, S.N.3    Balch, W.E.4
  • 11
    • 0030022944 scopus 로고    scopus 로고
    • Cytoplasmic domain of rhodopsin is essential for post-Golgi vesicle formation in a retinal cell-free system
    • Deretic D, Puleo-Scheppke B, Trippe C: Cytoplasmic domain of rhodopsin is essential for post-Golgi vesicle formation in a retinal cell-free system. J Biol Chem 1996, 271:2279-2286.
    • (1996) J Biol Chem , vol.271 , pp. 2279-2286
    • Deretic, D.1    Puleo-Scheppke, B.2    Trippe, C.3
  • 12
    • 0030720512 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase is required for the formation of constitutive transport vesicles from the TGN
    • Jones SM, Howell KE: Phosphatidylinositol 3-kinase is required for the formation of constitutive transport vesicles from the TGN. J Cell Biol 1997, 139:339-350.
    • (1997) J Cell Biol , vol.139 , pp. 339-350
    • Jones, S.M.1    Howell, K.E.2
  • 13
    • 0027240379 scopus 로고
    • A cytosolic complex of p62 and rab6 associates with TGN38/41 and is involved in budding of exocytic vesicles from the trans-Golgi network
    • Jones SM, Crosby JR, Salamero J, Howell KE: A cytosolic complex of p62 and rab6 associates with TGN38/41 and is involved in budding of exocytic vesicles from the trans-Golgi network. J Cell Biol 1993, 122:775-788.
    • (1993) J Cell Biol , vol.122 , pp. 775-788
    • Jones, S.M.1    Crosby, J.R.2    Salamero, J.3    Howell, K.E.4
  • 15
    • 0028224561 scopus 로고
    • Lysosome biogenesis requires Rab9 function and receptor recycling from endosomes to the trans Golgi network
    • Riederer MA, Soldati T, Shapiro AD, Lin J, Pfeffer S: Lysosome biogenesis requires Rab9 function and receptor recycling from endosomes to the trans Golgi network. J Cell Biol 1994, 125:573-582.
    • (1994) J Cell Biol , vol.125 , pp. 573-582
    • Riederer, M.A.1    Soldati, T.2    Shapiro, A.D.3    Lin, J.4    Pfeffer, S.5
  • 16
    • 0029804680 scopus 로고    scopus 로고
    • Two GTPase isoforms, Ypt31 p and Ypt32p, are essential for Golgi function in yeast
    • Benli M, Do̊ring F, Robinson DG, Yang X, Gallwitz D: Two GTPase isoforms, Ypt31 p and Ypt32p, are essential for Golgi function in yeast. EMBO J 1996, 15:6460-6475.
    • (1996) EMBO J , vol.15 , pp. 6460-6475
    • Benli, M.1    Do̊ring, F.2    Robinson, D.G.3    Yang, X.4    Gallwitz, D.5
  • 17
    • 0030969912 scopus 로고    scopus 로고
    • Two new Ypt GTPases are required for exit from the Yeast trans-Golgi compartment
    • Jedd G, Mulholland J, Segev N: Two new Ypt GTPases are required for exit from the Yeast trans-Golgi compartment. J Cell Biol 1997, 137:563-580.
    • (1997) J Cell Biol , vol.137 , pp. 563-580
    • Jedd, G.1    Mulholland, J.2    Segev, N.3
  • 19
    • 0026658185 scopus 로고
    • The activity of Golgi transport vesicles depends on the presence of the N-ethylmaleimide-sensitive factor (NSF) and a soluble NSF attachment protein (α-SNAP) during vesicle formation
    • Wattenberg BW, Raub TJ, Hiebsch RR, Weidman PJ: The activity of Golgi transport vesicles depends on the presence of the N-ethylmaleimide-sensitive factor (NSF) and a soluble NSF attachment protein (α-SNAP) during vesicle formation. J Cell Biol 1992, 118:1321-1332.
    • (1992) J Cell Biol , vol.118 , pp. 1321-1332
    • Wattenberg, B.W.1    Raub, T.J.2    Hiebsch, R.R.3    Weidman, P.J.4
  • 20
    • 0028587687 scopus 로고
    • Isolation and characterisation of the principal ATPase associated with transitional endoplasmic reticulum of rat liver
    • Zhang L, Ashendel CL, Becker GW, Morré DJ: Isolation and characterisation of the principal ATPase associated with transitional endoplasmic reticulum of rat liver. J Cell Biol 1994, 127:1871-1883.
    • (1994) J Cell Biol , vol.127 , pp. 1871-1883
    • Zhang, L.1    Ashendel, C.L.2    Becker, G.W.3    Morré, D.J.4
  • 21
    • 0030222771 scopus 로고    scopus 로고
    • 2-domain proteins that regulate membrane traffic
    • 2-domain proteins that regulate membrane traffic. Neuron 1996, 17:379-388.
    • (1996) Neuron , vol.17 , pp. 379-388
    • Südhof, T.C.1    Rizo, J.2
  • 22
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
    • Söllner T, Bennett M K, Whiteheart SW, Scheller RH, Rothman JE: A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell 1993, 75:409-418.
    • (1993) Cell , vol.75 , pp. 409-418
    • Söllner, T.1    Bennett, M.K.2    Whiteheart, S.W.3    Scheller, R.H.4    Rothman, J.E.5
  • 23
    • 0028168590 scopus 로고
    • Synaptotagmin I is a high affinity receptor for clathrin AP-2: Implications for membrane recycling
    • Zhang JZ, Davletov BA, Südhof TC, Anderson RGW: Synaptotagmin I is a high affinity receptor for clathrin AP-2: implications for membrane recycling. Cell 1994, 78:751-760.
    • (1994) Cell , vol.78 , pp. 751-760
    • Zhang, J.Z.1    Davletov, B.A.2    Südhof, T.C.3    Anderson, R.G.W.4
  • 24
    • 0028828226 scopus 로고
    • Defective recycling of synaptic vesicles in synaptotagmin mutants of Caenorhabditis elegans
    • Jorgensen EM, Hartwieg E, Schuske K, Nonet ML, Jin Y, Horvitz HR: Defective recycling of synaptic vesicles in synaptotagmin mutants of Caenorhabditis elegans. Nature 1995, 378:196-199.
    • (1995) Nature , vol.378 , pp. 196-199
    • Jorgensen, E.M.1    Hartwieg, E.2    Schuske, K.3    Nonet, M.L.4    Jin, Y.5    Horvitz, H.R.6
  • 25
    • 0028832353 scopus 로고
    • Role of the C2B-domain of synaptotagmin in vesicular release and recycling as determined by specific antibody injection into the squid giant synapse preterminal
    • Fukuda M, Moreira JE, Lewis FM, Sugimori M, Niinobe M, Mikoshiba K, Llinas R: Role of the C2B-domain of synaptotagmin in vesicular release and recycling as determined by specific antibody injection into the squid giant synapse preterminal. Proc Natl Acad Sci USA 1995, 92:10708-10712.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10708-10712
    • Fukuda, M.1    Moreira, J.E.2    Lewis, F.M.3    Sugimori, M.4    Niinobe, M.5    Mikoshiba, K.6    Llinas, R.7
  • 26
    • 0028385277 scopus 로고
    • Implications of the SNARE hypothesis for intracellular membrane topology and dynamics
    • Rothman JE, Warren G: Implications of the SNARE hypothesis for intracellular membrane topology and dynamics. Curr Biol 1994, 4:220-223.
    • (1994) Curr Biol , vol.4 , pp. 220-223
    • Rothman, J.E.1    Warren, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.