메뉴 건너뛰기




Volumn 17, Issue 4, 2005, Pages 345-352

COPII-coated vesicles: Flexible enough for large cargo?

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; CHYLOMICRON; FIBRILLAR COLLAGEN; PROCOLLAGEN; SECRETORY PROTEIN; SMAD ANCHOR FOR RECEPTOR ACTIVATION; SMAD ANCHOR FOR RECEPTOR ACTIVATION 2 PROTEIN; UNCLASSIFIED DRUG;

EID: 22044441866     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2005.06.004     Document Type: Review
Times cited : (88)

References (55)
  • 2
    • 0030928782 scopus 로고    scopus 로고
    • Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI
    • S.J. Scales, R. Pepperkok, and T.E. Kreis Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI Cell 90 1997 1137 1148
    • (1997) Cell , vol.90 , pp. 1137-1148
    • Scales, S.J.1    Pepperkok, R.2    Kreis, T.E.3
  • 3
    • 0033538549 scopus 로고    scopus 로고
    • Vesicular tubular clusters between the ER and Golgi mediate concentration of soluble secretory proteins by exclusion from COPI-coated vesicles
    • J.A. Martinez-Menarguez, H.J. Geuze, J.W. Slot, and J. Klumperman Vesicular tubular clusters between the ER and Golgi mediate concentration of soluble secretory proteins by exclusion from COPI-coated vesicles Cell 98 1999 81 90
    • (1999) Cell , vol.98 , pp. 81-90
    • Martinez-Menarguez, J.A.1    Geuze, H.J.2    Slot, J.W.3    Klumperman, J.4
  • 5
    • 0027467609 scopus 로고
    • Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum
    • T. Yoshihisa, C. Barlowe, and R. Schekman 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
  • 8
    • 9144229521 scopus 로고    scopus 로고
    • GTP/GDP exchange by Sec12p enables COPII vesicle bud formation on synthetic liposomes
    • E. Futai, S. Hamamoto, L. Orci, and R. Schekman GTP/GDP exchange by Sec12p enables COPII vesicle bud formation on synthetic liposomes EMBO J 23 2004 4146 4155
    • (2004) EMBO J , vol.23 , pp. 4146-4155
    • Futai, E.1    Hamamoto, S.2    Orci, L.3    Schekman, R.4
  • 9
    • 0027500969 scopus 로고
    • SEC12 encodes a guanine-nucleotide-exchange factor essential for transport vesicle budding from the ER
    • C. Barlowe, and R. Schekman 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
  • 10
    • 15544367075 scopus 로고    scopus 로고
    • Dissection of COPII subunit-cargo assembly and disassembly kinetics during Sar1p-GTP hydrolysis
    • K. Sato, and A. Nakano Dissection of COPII subunit-cargo assembly and disassembly kinetics during Sar1p-GTP hydrolysis Nat Struct Mol Biol 12 2005 167 174
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 167-174
    • Sato, K.1    Nakano, A.2
  • 11
    • 0028803617 scopus 로고
    • Yeast SEC16 gene encodes a multidomain vesicle coat protein that interacts with Sec23p
    • P. Espenshade, R.E. Gimeno, E. Holzmacher, P. Teung, and C.A. Kaiser 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
  • 12
    • 0037112755 scopus 로고    scopus 로고
    • Cargo selection into COPII vesicles is driven by the Sec24p subunit
    • E. Miller, B. Antonny, S. Hamamoto, and R. Schekman Cargo selection into COPII vesicles is driven by the Sec24p subunit EMBO J 21 2002 6105 6113
    • (2002) EMBO J , vol.21 , pp. 6105-6113
    • Miller, E.1    Antonny, B.2    Hamamoto, S.3    Schekman, R.4
  • 13
    • 0043029286 scopus 로고    scopus 로고
    • SNARE selectivity of the COPII coat
    • E. Mossessova, L.C. Bickford, and J. Goldberg SNARE selectivity of the COPII coat Cell 114 2003 483 495
    • (2003) Cell , vol.114 , pp. 483-495
    • Mossessova, E.1    Bickford, L.C.2    Goldberg, J.3
  • 14
    • 0041526467 scopus 로고    scopus 로고
    • Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles
    • E.A. Miller, T.H. Beilharz, P.N. Malkus, M.C. Lee, S. Hamamoto, L. Orci, and R. Schekman Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles Cell 114 2003 497 509
    • (2003) Cell , vol.114 , pp. 497-509
    • Miller, E.A.1    Beilharz, T.H.2    Malkus, P.N.3    Lee, M.C.4    Hamamoto, S.5    Orci, L.6    Schekman, R.7
  • 16
    • 0141521617 scopus 로고    scopus 로고
    • Endoplasmic reticulum export of glycosyltransferases depends on interaction of a cytoplasmic dibasic motif with Sar1
    • C.G. Giraudo, and H.J. Maccioni Endoplasmic reticulum export of glycosyltransferases depends on interaction of a cytoplasmic dibasic motif with Sar1 Mol Biol Cell 14 2003 3753 3766
    • (2003) Mol Biol Cell , vol.14 , pp. 3753-3766
    • Giraudo, C.G.1    MacCioni, H.J.2
  • 17
    • 0034646666 scopus 로고    scopus 로고
    • Evidence for overlapping and distinct functions in protein transport of coat protein Sec24p family members
    • R. Peng, A. De Antoni, and D. Gallwitz Evidence for overlapping and distinct functions in protein transport of coat protein Sec24p family members J Biol Chem 275 2000 11521 11528
    • (2000) J Biol Chem , vol.275 , pp. 11521-11528
    • Peng, R.1    De Antoni, A.2    Gallwitz, D.3
  • 18
    • 0027365851 scopus 로고
    • Molecular analysis of SAR1-related cDNAs from a mouse pituitary cell line
    • K.A. Shen, C.M. Hammond, and H.P. Moore Molecular analysis of SAR1-related cDNAs from a mouse pituitary cell line FEBS Lett 335 1993 380 385
    • (1993) FEBS Lett , vol.335 , pp. 380-385
    • Shen, K.A.1    Hammond, C.M.2    Moore, H.P.3
  • 22
    • 0010182347 scopus 로고    scopus 로고
    • Mammalian homologues of yeast sec31p. An ubiquitously expressed form is localized to endoplasmic reticulum (ER) exit sites and is essential for ER-Golgi transport
    • B.L. Tang, T. Zhang, D.Y. Low, E.T. Wong, H. Horstmann, and W. Hong Mammalian homologues of yeast sec31p. An ubiquitously expressed form is localized to endoplasmic reticulum (ER) exit sites and is essential for ER-Golgi transport J Biol Chem 275 2000 13597 13604
    • (2000) J Biol Chem , vol.275 , pp. 13597-13604
    • Tang, B.L.1    Zhang, T.2    Low, D.Y.3    Wong, E.T.4    Horstmann, H.5    Hong, W.6
  • 26
    • 0033991176 scopus 로고    scopus 로고
    • A proposed model for the assembly of chylomicrons
    • M.M. Hussain A proposed model for the assembly of chylomicrons Atherosclerosis 148 2000 1 15
    • (2000) Atherosclerosis , vol.148 , pp. 1-15
    • Hussain, M.M.1
  • 27
    • 0035085155 scopus 로고    scopus 로고
    • Very-low-density lipoprotein assembly and secretion
    • G.S. Shelness, and J.A. Sellers Very-low-density lipoprotein assembly and secretion Curr Opin Lipidol 12 2001 151 157
    • (2001) Curr Opin Lipidol , vol.12 , pp. 151-157
    • Shelness, G.S.1    Sellers, J.A.2
  • 28
    • 0027200620 scopus 로고
    • Molecular cloning of an apolipoprotein B messenger RNA editing protein
    • B. Teng, C.F. Burant, and N.O. Davidson Molecular cloning of an apolipoprotein B messenger RNA editing protein Science 260 1993 1816 1819
    • (1993) Science , vol.260 , pp. 1816-1819
    • Teng, B.1    Burant, C.F.2    Davidson, N.O.3
  • 29
    • 0035083798 scopus 로고    scopus 로고
    • Molecular mechanisms of apolipoprotein B mRNA editing
    • S. Anant, and N.O. Davidson Molecular mechanisms of apolipoprotein B mRNA editing Curr Opin Lipidol 12 2001 159 165
    • (2001) Curr Opin Lipidol , vol.12 , pp. 159-165
    • Anant, S.1    Davidson, N.O.2
  • 30
    • 0037124084 scopus 로고    scopus 로고
    • Complexity in the secretory pathway: The assembly and secretion of apolipoprotein B-containing lipoproteins
    • E.A. Fisher, and H.N. Ginsberg Complexity in the secretory pathway: the assembly and secretion of apolipoprotein B-containing lipoproteins J Biol Chem 277 2002 17377 17380
    • (2002) J Biol Chem , vol.277 , pp. 17377-17380
    • Fisher, E.A.1    Ginsberg, H.N.2
  • 35
    • 0037656344 scopus 로고    scopus 로고
    • Mutations in a Sar1 GTPase of COPII vesicles are associated with lipid absorption disorders
    • B. Jones, E.L. Jones, S.A. Bonney, H.N. Patel, A.R. Mensenkamp, S. Eichenbaum-Voline, M. Rudling, U. Myrdal, G. Annesi, and S. Naik Mutations in a Sar1 GTPase of COPII vesicles are associated with lipid absorption disorders Nat Genet 34 2003 29 31 Defects in the human SARA2 gene (coding for Sar1b) are shown to be associated with Anderson's disease and chylomicron retention disease.
    • (2003) Nat Genet , vol.34 , pp. 29-31
    • Jones, B.1    Jones, E.L.2    Bonney, S.A.3    Patel, H.N.4    Mensenkamp, A.R.5    Eichenbaum-Voline, S.6    Rudling, M.7    Myrdal, U.8    Annesi, G.9    Naik, S.10
  • 36
    • 1842452932 scopus 로고    scopus 로고
    • The intracellular transport of chylomicrons requires the small GTPase, Sar1b
    • C.C. Shoulders, D.J. Stephens, and B. Jones The intracellular transport of chylomicrons requires the small GTPase, Sar1b Curr Opin Lipidol 15 2004 191 197
    • (2004) Curr Opin Lipidol , vol.15 , pp. 191-197
    • Shoulders, C.C.1    Stephens, D.J.2    Jones, B.3
  • 37
    • 0037439881 scopus 로고    scopus 로고
    • COPII proteins are required for Golgi fusion but not for endoplasmic reticulum budding of the pre-chylomicron transport vesicle
    • S.A. Siddiqi, F.S. Gorelick, J.T. Mahan, and C.M. Mansbach II COPII proteins are required for Golgi fusion but not for endoplasmic reticulum budding of the pre-chylomicron transport vesicle J Cell Sci 116 2003 415 427 Formation of ER-derived pre-chylomicron transport vesicles (PCTVs) is reconstituted in an in vitro system. COPII is seen to be dispensable for generation of PCTVs, but is necessary for budding of PCTVs that can subsequently fuse with Golgi membranes.
    • (2003) J Cell Sci , vol.116 , pp. 415-427
    • Siddiqi, S.A.1    Gorelick, F.S.2    Mahan, J.T.3    Mansbach II, C.M.4
  • 38
    • 0346220266 scopus 로고    scopus 로고
    • Apolipoprotein B100 exit from the endoplasmic reticulum (ER) is COPII-dependent, and its lipidation to very low density lipoprotein occurs post-ER
    • V. Gusarova, J.L. Brodsky, and E.A. Fisher Apolipoprotein B100 exit from the endoplasmic reticulum (ER) is COPII-dependent, and its lipidation to very low density lipoprotein occurs post-ER J Biol Chem 278 2003 48051 48058 A reconstitution of the ApoB-100 vesicle budding reaction from ER membranes in vitro. ApoB-100 exit from ER membranes depends upon functional COPII, but the size of lipoprotein entering vesicles is likely to be small, because full lipidation is shown to occur downstream of COPII-dependent events.
    • (2003) J Biol Chem , vol.278 , pp. 48051-48058
    • Gusarova, V.1    Brodsky, J.L.2    Fisher, E.A.3
  • 39
    • 2942590588 scopus 로고    scopus 로고
    • Vesicular trafficking of hepatic apolipoprotein B100 and its maturation to very-low-density lipoprotein particles; Studies from cells and cell-free systems
    • J.L. Brodsky, V. Gusarova, and E.A. Fisher Vesicular trafficking of hepatic apolipoprotein B100 and its maturation to very-low-density lipoprotein particles; studies from cells and cell-free systems Trends Cardiovasc Med 14 2004 127 132
    • (2004) Trends Cardiovasc Med , vol.14 , pp. 127-132
    • Brodsky, J.L.1    Gusarova, V.2    Fisher, E.A.3
  • 40
    • 0034680777 scopus 로고    scopus 로고
    • Kinase signaling initiates coat complex II (COPII) recruitment and export from the mammalian endoplasmic reticulum
    • M. Aridor, and W.E. Balch Kinase signaling initiates coat complex II (COPII) recruitment and export from the mammalian endoplasmic reticulum J Biol Chem 275 2000 35673 35676
    • (2000) J Biol Chem , vol.275 , pp. 35673-35676
    • Aridor, M.1    Balch, W.E.2
  • 41
    • 0037087610 scopus 로고    scopus 로고
    • Imaging of procollagen transport reveals COPI-dependent cargo sorting during ER-to-Golgi transport in mammalian cells
    • D.J. Stephens, and R. Pepperkok Imaging of procollagen transport reveals COPI-dependent cargo sorting during ER-to-Golgi transport in mammalian cells J Cell Sci 115 2002 1149 1160
    • (2002) J Cell Sci , vol.115 , pp. 1149-1160
    • Stephens, D.J.1    Pepperkok, R.2
  • 42
    • 10744221460 scopus 로고    scopus 로고
    • ER-to-Golgi carriers arise through direct en bloc protrusion and multistage maturation of specialized ER exit domains
    • A.A. Mironov, A.A. Mironov Jr., G.V. Beznoussenko, A. Trucco, P. Lupetti, J.D. Smith, W.J. Geerts, A.J. Koster, K.N. Burger, and M.E. Martone ER-to-Golgi carriers arise through direct en bloc protrusion and multistage maturation of specialized ER exit domains Dev Cell 5 2003 583 594 The authors use EM and fluorescence microscopy to follow procollagen-I and VSV-G exit from the ER in vivo. Procollagen is seen to leave the ER in carriers that do not stain for VSV-G or COPII, and no COPII-associated vesicles are ever observed.
    • (2003) Dev Cell , vol.5 , pp. 583-594
    • Mironov, A.A.1    Mironov Jr., A.A.2    Beznoussenko, G.V.3    Trucco, A.4    Lupetti, P.5    Smith, J.D.6    Geerts, W.J.7    Koster, A.J.8    Burger, K.N.9    Martone, M.E.10
  • 43
    • 0035071569 scopus 로고    scopus 로고
    • Illuminating the secretory pathway: When do we need vesicles?
    • D.J. Stephens, and R. Pepperkok Illuminating the secretory pathway: when do we need vesicles? J Cell Sci 114 2001 1053 1059
    • (2001) J Cell Sci , vol.114 , pp. 1053-1059
    • Stephens, D.J.1    Pepperkok, R.2
  • 44
    • 0442292206 scopus 로고    scopus 로고
    • Biogenesis of ER-to-Golgi transport carriers: Complex roles of COPII in ER export
    • K.J. Palmer, and D.J. Stephens Biogenesis of ER-to-Golgi transport carriers: complex roles of COPII in ER export Trends Cell Biol 14 2004 57 61
    • (2004) Trends Cell Biol , vol.14 , pp. 57-61
    • Palmer, K.J.1    Stephens, D.J.2
  • 45
    • 3142624697 scopus 로고    scopus 로고
    • Differential ER exit in yeast and mammalian cells
    • R. Watanabe, and H. Riezman Differential ER exit in yeast and mammalian cells Curr Opin Cell Biol 16 2004 350 355
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 350-355
    • Watanabe, R.1    Riezman, H.2
  • 46
    • 0037296519 scopus 로고    scopus 로고
    • De novo formation, fusion and fission of mammalian COPII-coated endoplasmic reticulum exit sites
    • D.J. Stephens De novo formation, fusion and fission of mammalian COPII-coated endoplasmic reticulum exit sites EMBO Rep 4 2003 210 217
    • (2003) EMBO Rep , vol.4 , pp. 210-217
    • Stephens, D.J.1
  • 47
    • 0037113095 scopus 로고    scopus 로고
    • Ultrastructural characterization of endoplasmic reticulum-Golgi transport containers (EGTC)
    • H. Horstmann, C.P. Ng, B.L. Tang, and W. Hong Ultrastructural characterization of endoplasmic reticulum-Golgi transport containers (EGTC) J Cell Sci 115 2002 4263 4273
    • (2002) J Cell Sci , vol.115 , pp. 4263-4273
    • Horstmann, H.1    Ng, C.P.2    Tang, B.L.3    Hong, W.4
  • 48
    • 14044272872 scopus 로고    scopus 로고
    • Live imaging of bidirectional traffic from the ERGIC
    • H. Ben-Tekaya, K. Miura, R. Pepperkok, and H.P. Hauri Live imaging of bidirectional traffic from the ERGIC J Cell Sci 118 2005 357 367
    • (2005) J Cell Sci , vol.118 , pp. 357-367
    • Ben-Tekaya, H.1    Miura, K.2    Pepperkok, R.3    Hauri, H.P.4
  • 49
    • 12344277564 scopus 로고    scopus 로고
    • Coupling of ER exit to microtubules through direct interaction of COPII with dynactin
    • P. Watson, R. Forster, K.J. Palmer, R. Pepperkok, and D.J. Stephens Coupling of ER exit to microtubules through direct interaction of COPII with dynactin Nat Cell Biol 7 2005 48 55 A physical interaction between Sec23 and dynactin is established and shown to be important for ER exit. Thus, microtubules are involved very early in the secretory pathway.
    • (2005) Nat Cell Biol , vol.7 , pp. 48-55
    • Watson, P.1    Forster, R.2    Palmer, K.J.3    Pepperkok, R.4    Stephens, D.J.5
  • 50
    • 11244273061 scopus 로고    scopus 로고
    • Reconstitution of COPII vesicle fusion to generate a pre-Golgi intermediate compartment
    • D. Xu, and J.C. Hay Reconstitution of COPII vesicle fusion to generate a pre-Golgi intermediate compartment J Cell Biol 167 2004 997 1003 The authors reconstitute COPII vesicle budding and subsequent fusion to form an ERGIC-like compartment in vitro. COPII vesicles undergo homotypic fusion, and these new compartments are able to fuse with Golgi-derived COPI vesicles.
    • (2004) J Cell Biol , vol.167 , pp. 997-1003
    • Xu, D.1    Hay, J.C.2
  • 51
    • 0033917563 scopus 로고    scopus 로고
    • COPI-coated ER-to-Golgi transport complexes segregate from COPII in close proximity to ER exit sites
    • D.J. Stephens, N. Lin-Marq, A. Pagano, R. Pepperkok, and J.P. Paccaud COPI-coated ER-to-Golgi transport complexes segregate from COPII in close proximity to ER exit sites J Cell Sci 113 2000 2177 2185
    • (2000) J Cell Sci , vol.113 , pp. 2177-2185
    • Stephens, D.J.1    Lin-Marq, N.2    Pagano, A.3    Pepperkok, R.4    Paccaud, J.P.5
  • 53
    • 0037151098 scopus 로고    scopus 로고
    • +-ATPase Pma1p in the yeast endoplasmic reticulum
    • +-ATPase Pma1p in the yeast endoplasmic reticulum J Biol Chem 277 2002 22395 22401
    • (2002) J Biol Chem , vol.277 , pp. 22395-22401
    • Lee, M.C.1    Hamamoto, S.2    Schekman, R.3
  • 54
    • 14844314117 scopus 로고    scopus 로고
    • Uncoupled packaging of amyloid precursor protein and presenilin 1 into coat protein complex II vesicles
    • J. Kim, S. Hamamoto, M. Ravazzola, L. Orci, and R. Schekman Uncoupled packaging of amyloid precursor protein and presenilin 1 into coat protein complex II vesicles J Biol Chem 280 2005 7758 7768 In vitro reconstitution of mammalian COPII vesicle budding using purified components. The assay is used to study transport of the γ-secretase complex implicated in formation of plaques associated with Alzheimer's disease.
    • (2005) J Biol Chem , vol.280 , pp. 7758-7768
    • Kim, J.1    Hamamoto, S.2    Ravazzola, M.3    Orci, L.4    Schekman, R.5
  • 55
    • 0033615074 scopus 로고    scopus 로고
    • Segregation of COPI-rich and anterograde-cargo-rich domains in endoplasmic-reticulum-to-Golgi transport complexes
    • D.T. Shima, S.J. Scales, T.E. Kreis, and R. Pepperkok Segregation of COPI-rich and anterograde-cargo-rich domains in endoplasmic-reticulum-to-Golgi transport complexes Curr Biol 9 1999 821 824
    • (1999) Curr Biol , vol.9 , pp. 821-824
    • Shima, D.T.1    Scales, S.J.2    Kreis, T.E.3    Pepperkok, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.