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Volumn 294, Issue 6, 2008, Pages

Depletion of β-COP reveals a role for COP-I in compartmentalization of secretory compartments and in biosynthetic transport of caveolin-1

Author keywords

Coatomer; Endoplasmic reticulum Golgi intermediate compartment; Golgi; Recycling endosome; Trans Golgi network

Indexed keywords

BREFELDIN A; CAVEOLIN 1; COP I PROTEIN; CYCLOHEXIMIDE; SMALL INTERFERING RNA; TRANSFERRIN; UNCLASSIFIED DRUG; CAV1 PROTEIN, HUMAN; COAT PROTEIN COMPLEX I; COATOMER PROTEIN; G PROTEIN, VESICULAR STOMATITIS VIRUS; MEMBRANE PROTEIN; VIRUS ENVELOPE PROTEIN;

EID: 47249163819     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00010.2008     Document Type: Article
Times cited : (49)

References (81)
  • 1
    • 0028971172 scopus 로고
    • Sequential coupling between COPII and COPI vesicle coats in endoplasmic reticulum to Golgi transport
    • Aridor M, Bannykh SI, Rowe T, Balch WE. Sequential coupling between COPII and COPI vesicle coats in endoplasmic reticulum to Golgi transport. J Cell Biol 131: 875-893, 1995.
    • (1995) J Cell Biol , vol.131 , pp. 875-893
    • Aridor, M.1    Bannykh, S.I.2    Rowe, T.3    Balch, W.E.4
  • 2
    • 0021673303 scopus 로고
    • Direct visualization of protein transport and processing in the living cell by microinjection of specific antibodies
    • Arnheiter H, Dubois-Dalcq M, Lazzarini RA. Direct visualization of protein transport and processing in the living cell by microinjection of specific antibodies. Cell 39: 99-109, 1984.
    • (1984) Cell , vol.39 , pp. 99-109
    • Arnheiter, H.1    Dubois-Dalcq, M.2    Lazzarini, R.A.3
  • 3
    • 0024822838 scopus 로고
    • Using temperature-sensitive mutants of VSV to study membrane protein biogenesis
    • Bergmann JE. Using temperature-sensitive mutants of VSV to study membrane protein biogenesis. Methods Cell Biol 32: 85-110, 1989.
    • (1989) Methods Cell Biol , vol.32 , pp. 85-110
    • Bergmann, J.E.1
  • 4
    • 33750344792 scopus 로고    scopus 로고
    • Coatomer, the coat protein of COPI transport vesicles, discriminates endoplasmic reticulum residents from p24 proteins
    • Bethune J, Kol M, Hoffmann J, Reckmann I, Brugger B, Wieland F. Coatomer, the coat protein of COPI transport vesicles, discriminates endoplasmic reticulum residents from p24 proteins. Mol Cell Biol 26: 8011-8021, 2006.
    • (2006) Mol Cell Biol , vol.26 , pp. 8011-8021
    • Bethune, J.1    Kol, M.2    Hoffmann, J.3    Reckmann, I.4    Brugger, B.5    Wieland, F.6
  • 5
    • 0842324801 scopus 로고    scopus 로고
    • The mechanisms of vesicle budding and fusion
    • Bonifacino JS, 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
  • 6
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • Bonifacino JS, Traub LM. Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu Rev Biochem 72: 395-447, 2003.
    • (2003) Annu Rev Biochem , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 7
    • 0035826727 scopus 로고    scopus 로고
    • SNARE proteins are highly enriched in lipid rafts in PC12 cells: Implications for the spatial control of exocytosis
    • Chamberlain LH, Burgoyne RD, Gould GW. SNARE proteins are highly enriched in lipid rafts in PC12 cells: implications for the spatial control of exocytosis. Proc Natl Acad Sci USA 98: 5619-5624, 2001.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 5619-5624
    • Chamberlain, L.H.1    Burgoyne, R.D.2    Gould, G.W.3
  • 10
    • 4644224284 scopus 로고    scopus 로고
    • Role of caveolae and caveolins in health and disease
    • Cohen AW, Hnasko R, Schubert W, Lisanti MP. Role of caveolae and caveolins in health and disease. Physiol Rev 84: 1341-1379, 2004.
    • (2004) Physiol Rev , vol.84 , pp. 1341-1379
    • Cohen, A.W.1    Hnasko, R.2    Schubert, W.3    Lisanti, M.P.4
  • 12
    • 0031425955 scopus 로고    scopus 로고
    • Inhibition of endosome function in CHO cells bearing a temperature-sensitive defect in the coatomer (COPI) component epsilon-COP
    • Daro E, Sheff D, Gomez M, Kreis T, Mellman I. Inhibition of endosome function in CHO cells bearing a temperature-sensitive defect in the coatomer (COPI) component epsilon-COP. J Cell Biol 139: 1747-1759, 1997.
    • (1997) J Cell Biol , vol.139 , pp. 1747-1759
    • Daro, E.1    Sheff, D.2    Gomez, M.3    Kreis, T.4    Mellman, I.5
  • 13
    • 0027953550 scopus 로고
    • Dominant inhibitory mutants of ARF1 block endoplasmic reticulum to Golgi transport and trigger disassembly of the Golgi apparatus
    • Dascher C, Balch WE. Dominant inhibitory mutants of ARF1 block endoplasmic reticulum to Golgi transport and trigger disassembly of the Golgi apparatus. J Biol Chem 269: 1437-1448, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 1437-1448
    • Dascher, C.1    Balch, W.E.2
  • 15
    • 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, 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
  • 16
    • 0025674154 scopus 로고
    • Dissociation of a 110-kD peripheral membrane protein from the Golgi apparatus is an early event in brefeldin A action
    • Donaldson JG, Lippincott-Schwartz J, Bloom GS, Kreis TE, Klausner RD. Dissociation of a 110-kD peripheral membrane protein from the Golgi apparatus is an early event in brefeldin A action. J Cell Biol 111: 2295-2306, 1990.
    • (1990) J Cell Biol , vol.111 , pp. 2295-2306
    • Donaldson, J.G.1    Lippincott-Schwartz, J.2    Bloom, G.S.3    Kreis, T.E.4    Klausner, R.D.5
  • 17
    • 0027414646 scopus 로고
    • Caveolae and sorting in the trans-Golgi network of epithelial cells
    • Dupree P, Parton RG, Raposo G, Kurzchalia TV, Simons K. Caveolae and sorting in the trans-Golgi network of epithelial cells. EMBO J 12: 1597-1605, 1993.
    • (1993) EMBO J , vol.12 , pp. 1597-1605
    • Dupree, P.1    Parton, R.G.2    Raposo, G.3    Kurzchalia, T.V.4    Simons, K.5
  • 18
    • 33749649546 scopus 로고    scopus 로고
    • Caveolae internalization regulates integrin-dependent signaling pathways
    • Echarri A, Del Pozo MA. Caveolae internalization regulates integrin-dependent signaling pathways. Cell Cycle 5: 2179-2182, 2006.
    • (2006) Cell Cycle , vol.5 , pp. 2179-2182
    • Echarri, A.1    Del Pozo, M.A.2
  • 19
    • 0038050371 scopus 로고    scopus 로고
    • Cisternal maturation and vesicle transport: Join the band wagon (Review)!
    • Elsner M, Hashimoto H, Nilsson T. Cisternal maturation and vesicle transport: join the band wagon (Review)! Mol Membr Biol 20: 221-229, 2003.
    • (2003) Mol Membr Biol , vol.20 , pp. 221-229
    • Elsner, M.1    Hashimoto, H.2    Nilsson, T.3
  • 20
    • 0034254166 scopus 로고    scopus 로고
    • COP I domains required for coatomer integrity, and novel interactions with ARF and ARF-GAP
    • Eugster A, Frigerio G, Dale M, Duden R. COP I domains required for coatomer integrity, and novel interactions with ARF and ARF-GAP. EMBO J 19: 3905-3917, 2000.
    • (2000) EMBO J , vol.19 , pp. 3905-3917
    • Eugster, A.1    Frigerio, G.2    Dale, M.3    Duden, R.4
  • 21
    • 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: 1396-1399, 1996.
    • (1996) Science , vol.273 , pp. 1396-1399
    • Fiedler, K.1    Veit, M.2    Stamnes, M.A.3    Rothman, J.E.4
  • 22
    • 33846130922 scopus 로고    scopus 로고
    • Involvement of specific COPI subunits in protein sorting from the late endosome to the vacuole in yeast
    • Gabriely G, Kama R, Gerst JE. Involvement of specific COPI subunits in protein sorting from the late endosome to the vacuole in yeast. Mol Cell Biol 27: 526-540, 2007.
    • (2007) Mol Cell Biol , vol.27 , pp. 526-540
    • Gabriely, G.1    Kama, R.2    Gerst, J.E.3
  • 23
    • 0032509448 scopus 로고    scopus 로고
    • Molecular cloning, characterization, and dynamics of rat formiminotransferase cyclodeaminase, a Golgi-associated 58-kDa protein
    • Gao YS, Alvarez C, Nelson DS, Sztul E. Molecular cloning, characterization, and dynamics of rat formiminotransferase cyclodeaminase, a Golgi-associated 58-kDa protein. J Biol Chem 273: 33825-33834, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 33825-33834
    • Gao, Y.S.1    Alvarez, C.2    Nelson, D.S.3    Sztul, E.4
  • 24
    • 17344391184 scopus 로고    scopus 로고
    • ADP-ribosylation factor/COPI-dependent events at the endoplasmic reticulum-Golgi interface are regulated by the guanine nucleotide exchange factor GBF1
    • Garcia-Mata R, Szul T, Alvarez C, Sztul E. ADP-ribosylation factor/COPI-dependent events at the endoplasmic reticulum-Golgi interface are regulated by the guanine nucleotide exchange factor GBF1. Mol Biol Cell 14: 2250-2261, 2003.
    • (2003) Mol Biol Cell , vol.14 , pp. 2250-2261
    • Garcia-Mata, R.1    Szul, T.2    Alvarez, C.3    Sztul, E.4
  • 25
    • 0031027758 scopus 로고    scopus 로고
    • COPI-independent anterograde transport: Cargo-selective ER to Golgi protein transport in yeast COPI mutants
    • Gaynor EC, Emr SD. COPI-independent anterograde transport: cargo-selective ER to Golgi protein transport in yeast COPI mutants. J Cell Biol 136: 789-802, 1997.
    • (1997) J Cell Biol , vol.136 , pp. 789-802
    • Gaynor, E.C.1    Emr, S.D.2
  • 26
    • 0141920801 scopus 로고    scopus 로고
    • Mutations in COCH that result in non-syndromic autosomal dominant deafness (DFNA9) affect matrix deposition of cochlin
    • Grabski R, Szul T, Sasaki T, Timpl R, Mayne R, Hicks B, Sztul E. Mutations in COCH that result in non-syndromic autosomal dominant deafness (DFNA9) affect matrix deposition of cochlin. Hum Genet 113: 406-416, 2003.
    • (2003) Hum Genet , vol.113 , pp. 406-416
    • Grabski, R.1    Szul, T.2    Sasaki, T.3    Timpl, R.4    Mayne, R.5    Hicks, B.6    Sztul, E.7
  • 27
    • 0028984235 scopus 로고
    • Immunocytochemical localization of beta-COP to the ER-Golgi boundary and the TGN
    • Griffiths G, Pepperkok R, Locker JK, Kreis TE. Immunocytochemical localization of beta-COP to the ER-Golgi boundary and the TGN. J Cell Sci 108: 2839-2856, 1995.
    • (1995) J Cell Sci , vol.108 , pp. 2839-2856
    • Griffiths, G.1    Pepperkok, R.2    Locker, J.K.3    Kreis, T.E.4
  • 28
    • 0030812588 scopus 로고    scopus 로고
    • Functional dissection of COP-I subunits in the biogenesis of multivesicular endosomes
    • Gu F, Aniento F, Parton RG, Gruenberg J. Functional dissection of COP-I subunits in the biogenesis of multivesicular endosomes. J Cell Biol 139: 1183-1195, 1997.
    • (1997) J Cell Biol , vol.139 , pp. 1183-1195
    • Gu, F.1    Aniento, F.2    Parton, R.G.3    Gruenberg, J.4
  • 29
    • 17544372313 scopus 로고    scopus 로고
    • A single point mutation in epsilon-COP results in temperature-sensitive, lethal defects in membrane transport in a Chinese hamster ovary cell mutant
    • Guo Q, Penman M, Trigatti BL, Krieger M. A single point mutation in epsilon-COP results in temperature-sensitive, lethal defects in membrane transport in a Chinese hamster ovary cell mutant. J Biol Chem 271: 11191-11196, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 11191-11196
    • Guo, Q.1    Penman, M.2    Trigatti, B.L.3    Krieger, M.4
  • 30
    • 0028264318 scopus 로고
    • Disruptions in Golgi structure and membrane traffic in a conditional lethal mammalian cell mutant are corrected by epsilon-COP
    • Guo Q, Vasile E, Krieger M. Disruptions in Golgi structure and membrane traffic in a conditional lethal mammalian cell mutant are corrected by epsilon-COP. J Cell Biol 125: 1213-1224, 1994.
    • (1994) J Cell Biol , vol.125 , pp. 1213-1224
    • Guo, Q.1    Vasile, E.2    Krieger, M.3
  • 31
    • 0032578522 scopus 로고    scopus 로고
    • A single binding site for dilysine retrieval motifs and p23 within the gamma subunit of coatomer
    • Harter C, Wieland FT. A single binding site for dilysine retrieval motifs and p23 within the gamma subunit of coatomer. Proc Natl Acad Sci USA 95: 11649-11654, 1998.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 11649-11654
    • Harter, C.1    Wieland, F.T.2
  • 33
    • 0036841790 scopus 로고    scopus 로고
    • Up-regulated caveolin-1 accentuates the metastasis capability of lung adenocarcinoma by inducing filopodia formation
    • Ho CC, Huang PH, Huang HY, Chen YH, Yang PC, Hsu SM. Up-regulated caveolin-1 accentuates the metastasis capability of lung adenocarcinoma by inducing filopodia formation. Am J Pathol 161: 1647-1656, 2002.
    • (2002) Am J Pathol , vol.161 , pp. 1647-1656
    • Ho, C.C.1    Huang, P.H.2    Huang, H.Y.3    Chen, Y.H.4    Yang, P.C.5    Hsu, S.M.6
  • 34
    • 0028169450 scopus 로고
    • Isolation of three classes of conditional lethal Chinese hamster ovary cell mutants with temperature-dependent defects in low density lipoprotein receptor stability and intracellular membrane transport
    • Hobbie L, Fisher AS, Lee S, Flint A, Krieger M. Isolation of three classes of conditional lethal Chinese hamster ovary cell mutants with temperature-dependent defects in low density lipoprotein receptor stability and intracellular membrane transport. J Biol Chem 269: 20958-20970, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 20958-20970
    • Hobbie, L.1    Fisher, A.S.2    Lee, S.3    Flint, A.4    Krieger, M.5
  • 35
    • 0346102461 scopus 로고    scopus 로고
    • Recognition of dileucine-based sorting signals from HIV-1 Nef and LIMP-II by the AP-1 gamma-sigma1 and AP-3 delta-sigma3 hemicomplexes
    • Janvier K, Kato Y, Boehm M, Rose JR, Martina JA, Kim BY, Venkatesan S, Bonifacino JS. Recognition of dileucine-based sorting signals from HIV-1 Nef and LIMP-II by the AP-1 gamma-sigma1 and AP-3 delta-sigma3 hemicomplexes. J Cell Biol 163: 1281-1290, 2003.
    • (2003) J Cell Biol , vol.163 , pp. 1281-1290
    • Janvier, K.1    Kato, Y.2    Boehm, M.3    Rose, J.R.4    Martina, J.A.5    Kim, B.Y.6    Venkatesan, S.7    Bonifacino, J.S.8
  • 36
    • 1342288875 scopus 로고    scopus 로고
    • Increased expression of caveolin-1 and microvessel density correlates with metastasis and poor prognosis in clear cell renal cell carcinoma
    • Joo HJ, Oh DK, Kim YS, Lee KB, Kim SJ. Increased expression of caveolin-1 and microvessel density correlates with metastasis and poor prognosis in clear cell renal cell carcinoma. BJU Int 93: 291-296, 2004.
    • (2004) BJU Int , vol.93 , pp. 291-296
    • Joo, H.J.1    Oh, D.K.2    Kim, Y.S.3    Lee, K.B.4    Kim, S.J.5
  • 37
    • 0037083622 scopus 로고    scopus 로고
    • Overexpression of caveolin-1 in esophageal squamous cell carcinoma correlates with lymph node metastasis and pathologic stage
    • Kato K, Hida Y, Miyamoto M, Hashida H, Shinohara T, Itoh T, Okushiba S, Kondo S, Katoh H. Overexpression of caveolin-1 in esophageal squamous cell carcinoma correlates with lymph node metastasis and pathologic stage. Cancer 94: 929-933, 2002.
    • (2002) Cancer , vol.94 , pp. 929-933
    • Kato, K.1    Hida, Y.2    Miyamoto, M.3    Hashida, H.4    Shinohara, T.5    Itoh, T.6    Okushiba, S.7    Kondo, S.8    Katoh, H.9
  • 38
    • 0030794182 scopus 로고    scopus 로고
    • Linking cargo to vesicle formation: Receptor tail interactions with coat proteins
    • Kirchhausen T, Bonifacino JS, Riezman H. Linking cargo to vesicle formation: receptor tail interactions with coat proteins. Curr Opin Cell Biol 9: 488-495, 1997.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 488-495
    • Kirchhausen, T.1    Bonifacino, J.S.2    Riezman, H.3
  • 39
    • 3142582011 scopus 로고    scopus 로고
    • Caveolins: Structure and function in signal transduction
    • Krajewska WM, Maslowska I. Caveolins: structure and function in signal transduction. Cell Mol Biol (Oxf) 9: 195-220, 2004.
    • (2004) Cell Mol Biol (Oxf) , vol.9 , pp. 195-220
    • Krajewska, W.M.1    Maslowska, I.2
  • 40
    • 0022550932 scopus 로고
    • Oligomerization is essential for transport of vesicular stomatitis viral glycoprotein to the cell surface
    • Kreis TE, Lodish HF. Oligomerization is essential for transport of vesicular stomatitis viral glycoprotein to the cell surface. Cell 46: 929-937, 1986.
    • (1986) Cell , vol.46 , pp. 929-937
    • Kreis, T.E.1    Lodish, H.F.2
  • 42
    • 0036791604 scopus 로고    scopus 로고
    • Caveolin-1 mutations (P132L and null) and the pathogenesis of breast cancer: Caveolin-1 (P132L) behaves in a dominant-negative manner and caveolin-1 (-/-) null mice show mammary epithelial cell hyperplasia
    • Lee H, Park DS, Razani B, Russell RG, Pestell RG, Lisanti MP. Caveolin-1 mutations (P132L and null) and the pathogenesis of breast cancer: caveolin-1 (P132L) behaves in a dominant-negative manner and caveolin-1 (-/-) null mice show mammary epithelial cell hyperplasia. Am J Pathol 161: 1357-1369, 2002.
    • (2002) Am J Pathol , vol.161 , pp. 1357-1369
    • Lee, H.1    Park, D.S.2    Razani, B.3    Russell, R.G.4    Pestell, R.G.5    Lisanti, M.P.6
  • 44
    • 0027244942 scopus 로고    scopus 로고
    • Linstedt AD, 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.
    • Linstedt AD, 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.
  • 45
    • 0029844218 scopus 로고    scopus 로고
    • In vivo assembly of coatomer, the COP-I coat precursor
    • Lowe M, Kreis TE. In vivo assembly of coatomer, the COP-I coat precursor. J Biol Chem 271: 30725-30730, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 30725-30730
    • Lowe, M.1    Kreis, T.E.2
  • 46
    • 30044439559 scopus 로고    scopus 로고
    • Cis-Golgi matrix proteins move directly to endoplasmic reticulum exit sites by association with tubules
    • Mardones GA, Snyder CM, Howell KE. Cis-Golgi matrix proteins move directly to endoplasmic reticulum exit sites by association with tubules. Mol Biol Cell 17: 525-538, 2006.
    • (2006) Mol Biol Cell , vol.17 , pp. 525-538
    • Mardones, G.A.1    Snyder, C.M.2    Howell, K.E.3
  • 47
    • 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
    • Martinez-Menarguez JA, Geuze HJ, Slot JW, Klumperman J. Vesicular tubular clusters between the ER and Golgi mediate concentration of soluble secretory proteins by exclusion from COPI-coated vesicles. Cell 98: 81-90, 1999.
    • (1999) Cell , vol.98 , pp. 81-90
    • Martinez-Menarguez, J.A.1    Geuze, H.J.2    Slot, J.W.3    Klumperman, J.4
  • 48
    • 0035969241 scopus 로고    scopus 로고
    • Evidence that the entire Golgi apparatus cycles in interphase HeLa cells: Sensitivity of Golgi matrix proteins to an ER exit block
    • Miles S, McManus H, Forsten KE, Storrie B. Evidence that the entire Golgi apparatus cycles in interphase HeLa cells: sensitivity of Golgi matrix proteins to an ER exit block. J Cell Biol 155: 543-555, 2001.
    • (2001) J Cell Biol , vol.155 , pp. 543-555
    • Miles, S.1    McManus, H.2    Forsten, K.E.3    Storrie, B.4
  • 49
    • 0032547807 scopus 로고    scopus 로고
    • The membrane transport factor TAP/p115 cycles between the Golgi and earlier secretory compartments and contains distinct domains required for its localization and function
    • Nelson DS, Alvarez C, Gao YS, Garcia-Mata R, Fialkowski E, Sztul E. The membrane transport factor TAP/p115 cycles between the Golgi and earlier secretory compartments and contains distinct domains required for its localization and function. J Cell Biol 143: 319-331, 1998.
    • (1998) J Cell Biol , vol.143 , pp. 319-331
    • Nelson, D.S.1    Alvarez, C.2    Gao, Y.S.3    Garcia-Mata, R.4    Fialkowski, E.5    Sztul, E.6
  • 51
    • 0036094927 scopus 로고    scopus 로고
    • A distinct class of endosome mediates clathrin-independent endocytosis to the Golgi complex
    • Nichols BJ. A distinct class of endosome mediates clathrin-independent endocytosis to the Golgi complex. Nat Cell Biol 4: 374-378, 2002.
    • (2002) Nat Cell Biol , vol.4 , pp. 374-378
    • Nichols, B.J.1
  • 52
    • 0037101946 scopus 로고    scopus 로고
    • Vesicular transport: The core machinery of COPI recruitment and budding
    • Nickel W, Brugger B, Wieland FT. Vesicular transport: the core machinery of COPI recruitment and budding. J Cell Sci 115: 3235-3240, 2002.
    • (2002) J Cell Sci , vol.115 , pp. 3235-3240
    • Nickel, W.1    Brugger, B.2    Wieland, F.T.3
  • 54
    • 33645216741 scopus 로고    scopus 로고
    • Biogenesis of caveolae: A structural model for caveolin-induced domain formation
    • Parton RG, Hanzal-Bayer M, Hancock JF. Biogenesis of caveolae: a structural model for caveolin-induced domain formation. J Cell Sci 119: 787-796, 2006.
    • (2006) J Cell Sci , vol.119 , pp. 787-796
    • Parton, R.G.1    Hanzal-Bayer, M.2    Hancock, J.F.3
  • 55
    • 0032478277 scopus 로고    scopus 로고
    • Reversible dissociation of coatomer: Functional characterization of a beta/delta-coat protein subcomplex
    • Pavel J, Harter C, Wieland FT. Reversible dissociation of coatomer: functional characterization of a beta/delta-coat protein subcomplex. Proc Natl Acad Sci USA 95: 2140-2145, 1998.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 2140-2145
    • Pavel, J.1    Harter, C.2    Wieland, F.T.3
  • 56
    • 0035017308 scopus 로고    scopus 로고
    • Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER
    • Pelkmans L, Kartenbeck J, Helenius A. Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER. Nat Cell Biol 3: 473-483, 2001.
    • (2001) Nat Cell Biol , vol.3 , pp. 473-483
    • Pelkmans, L.1    Kartenbeck, J.2    Helenius, A.3
  • 57
    • 0027220591 scopus 로고
    • Beta-COP is essential for biosynthetic membrane transport from the endoplasmic reticulum to the Golgi complex in vivo
    • Pepperkok R, Scheel J, Horstmann H, Hauri HP, Griffiths G, Kreis TE. Beta-COP is essential for biosynthetic membrane transport from the endoplasmic reticulum to the Golgi complex in vivo. Cell 74: 71-82, 1993.
    • (1993) Cell , vol.74 , pp. 71-82
    • Pepperkok, R.1    Scheel, J.2    Horstmann, H.3    Hauri, H.P.4    Griffiths, G.5    Kreis, T.E.6
  • 58
    • 0027165412 scopus 로고
    • Beta-COP is essential for transport of protein from the endoplasmic reticulum to the Golgi in vitro
    • Peter F, Plutner H, Zhu H, Kreis TE, Balch WE. Beta-COP is essential for transport of protein from the endoplasmic reticulum to the Golgi in vitro. J Cell Biol 122: 1155-1167, 1993.
    • (1993) J Cell Biol , vol.122 , pp. 1155-1167
    • Peter, F.1    Plutner, H.2    Zhu, H.3    Kreis, T.E.4    Balch, W.E.5
  • 59
    • 16344368798 scopus 로고    scopus 로고
    • Cholesterol and fatty acids regulate dynamic caveolin trafficking through the Golgi complex and between the cell surface and lipid bodies
    • Pol A, Martin S, Fernandez MA, Ingelmo-Torres M, Ferguson C, Enrich C, Parton RG. Cholesterol and fatty acids regulate dynamic caveolin trafficking through the Golgi complex and between the cell surface and lipid bodies. Mol Biol Cell 16: 2091-2105, 2005.
    • (2005) Mol Biol Cell , vol.16 , pp. 2091-2105
    • Pol, A.1    Martin, S.2    Fernandez, M.A.3    Ingelmo-Torres, M.4    Ferguson, C.5    Enrich, C.6    Parton, R.G.7
  • 61
    • 0035661564 scopus 로고    scopus 로고
    • Golgi-to-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, Waters MG. Golgi-to-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
  • 62
    • 33745612093 scopus 로고    scopus 로고
    • Dynamic regulation of caveolin-1 trafficking in the germ line and embryo of Caenorhabditis elegans
    • Sato K, Sato M, Audhya A, Oegema K, Schweinsberg P, Grant BD. Dynamic regulation of caveolin-1 trafficking in the germ line and embryo of Caenorhabditis elegans. Mol Biol Cell 17: 3085-3094, 2006.
    • (2006) Mol Biol Cell , vol.17 , pp. 3085-3094
    • Sato, K.1    Sato, M.2    Audhya, A.3    Oegema, K.4    Schweinsberg, P.5    Grant, B.D.6
  • 63
    • 0030928782 scopus 로고    scopus 로고
    • Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI
    • 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. Cell 90: 1137-1148, 1997.
    • (1997) Cell , vol.90 , pp. 1137-1148
    • Scales, S.J.1    Pepperkok, R.2    Kreis, T.E.3
  • 64
    • 0029872276 scopus 로고    scopus 로고
    • Coat proteins and vesicle budding
    • Schekman R, Orci L. Coat proteins and vesicle budding. Science 271: 1526-1533, 1996.
    • (1996) Science , vol.271 , pp. 1526-1533
    • Schekman, R.1    Orci, L.2
  • 65
    • 0027328703 scopus 로고
    • ERGIC-53, a membrane protein of the ER-Golgi intermediate compartment, carries an ER retention motif
    • Schindler R, Itin C, Zerial M, Lottspeich F, Hauri HP. ERGIC-53, a membrane protein of the ER-Golgi intermediate compartment, carries an ER retention motif. Eur J Cell Biol 61: 1-9, 1993.
    • (1993) Eur J Cell Biol , vol.61 , pp. 1-9
    • Schindler, R.1    Itin, C.2    Zerial, M.3    Lottspeich, F.4    Hauri, H.P.5
  • 66
    • 0027284699 scopus 로고
    • Characterization of a novel 63 kDa membrane protein. Implications for the organization of the ER-to-Golgi pathway
    • Schweizer A, Ericsson M, Bachi T, Griffiths G, Hauri HP. Characterization of a novel 63 kDa membrane protein. Implications for the organization of the ER-to-Golgi pathway. J Cell Sci 104: 671-683, 1993.
    • (1993) J Cell Sci , vol.104 , pp. 671-683
    • Schweizer, A.1    Ericsson, M.2    Bachi, T.3    Griffiths, G.4    Hauri, H.P.5
  • 68
    • 0033615074 scopus 로고    scopus 로고
    • Segregation of COPI-rich and anterograde-cargo-rich domains in endoplasmic-reticulum-to-Golgi transport complexes
    • Shima DT, Scales SJ, Kreis TE, Pepperkok R. Segregation of COPI-rich and anterograde-cargo-rich domains in endoplasmic-reticulum-to-Golgi transport complexes. Curr Biol 9: 821-824, 1999.
    • (1999) Curr Biol , vol.9 , pp. 821-824
    • Shima, D.T.1    Scales, S.J.2    Kreis, T.E.3    Pepperkok, R.4
  • 69
    • 0032476574 scopus 로고    scopus 로고
    • Reconstitution of retrograde transport from the Golgi to the ER in vitro
    • Spang A, Schekman R. Reconstitution of retrograde transport from the Golgi to the ER in vitro. J Cell Biol 143: 589-599, 1998.
    • (1998) J Cell Biol , vol.143 , pp. 589-599
    • Spang, A.1    Schekman, R.2
  • 70
    • 0033917563 scopus 로고    scopus 로고
    • COPI-coated ER-to-Golgi transport complexes segregate from COPII in close proximity to ER exit sites
    • Stephens DJ, Lin-Marq N, Pagano A, Pepperkok R, Paccaud JP. COPI-coated ER-to-Golgi transport complexes segregate from COPII in close proximity to ER exit sites. J Cell Sci 113: 2177-2185, 2000.
    • (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
  • 71
    • 18244365900 scopus 로고    scopus 로고
    • Maintenance of Golgi apparatus structure in the face of continuous protein recycling to the endoplasmic reticulum: Making ends meet
    • Storrie B. Maintenance of Golgi apparatus structure in the face of continuous protein recycling to the endoplasmic reticulum: making ends meet. Int Rev Cytol 244: 69-94, 2005.
    • (2005) Int Rev Cytol , vol.244 , pp. 69-94
    • Storrie, B.1
  • 72
    • 0032517823 scopus 로고    scopus 로고
    • Recycling of golgi-resident glycosyltransferases through the ER reveals a novel pathway and provides an explanation for nocodazole-induced Golgi scattering
    • Storrie B, White J, Rottger S, Stelzer EH, Suganuma T, Nilsson T. Recycling of golgi-resident glycosyltransferases through the ER reveals a novel pathway and provides an explanation for nocodazole-induced Golgi scattering. J Cell Biol 143: 1505-1521, 1998.
    • (1998) J Cell Biol , vol.143 , pp. 1505-1521
    • Storrie, B.1    White, J.2    Rottger, S.3    Stelzer, E.H.4    Suganuma, T.5    Nilsson, T.6
  • 73
    • 24144431634 scopus 로고    scopus 로고
    • Assembly and trafficking of caveolar domains in the cell: Caveolae as stable, cargo-triggered, vesicular transporters
    • Tagawa A, Mezzacasa A, Hayer A, Longatti A, Pelkmans L, Helenius A. Assembly and trafficking of caveolar domains in the cell: caveolae as stable, cargo-triggered, vesicular transporters. J Cell Biol 170: 769-779, 2005.
    • (2005) J Cell Biol , vol.170 , pp. 769-779
    • Tagawa, A.1    Mezzacasa, A.2    Hayer, A.3    Longatti, A.4    Pelkmans, L.5    Helenius, A.6
  • 74
    • 0036151510 scopus 로고    scopus 로고
    • Caveolae are highly immobile plasma membrane microdomains, which are not involved in constitutive endocytic trafficking
    • Thomsen P, Roepstorff K, Stahlhut M, van Deurs B. Caveolae are highly immobile plasma membrane microdomains, which are not involved in constitutive endocytic trafficking. Mol Biol Cell 13: 238-250, 2002.
    • (2002) Mol Biol Cell , vol.13 , pp. 238-250
    • Thomsen, P.1    Roepstorff, K.2    Stahlhut, M.3    van Deurs, B.4
  • 76
    • 0025957468 scopus 로고
    • Coatomer': A cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles
    • Waters MG, Serafini T, Rothman JE. 'Coatomer': a cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles. Nature 349: 248-251, 1991.
    • (1991) Nature , vol.349 , pp. 248-251
    • Waters, M.G.1    Serafini, T.2    Rothman, J.E.3
  • 77
    • 0020121742 scopus 로고
    • The morphologic pathway of exocytosis of the vesicular stomatitis virus G protein in cultured fibroblasts
    • Wehland J, Willingham MC, Gallo MG, Pastan I. The morphologic pathway of exocytosis of the vesicular stomatitis virus G protein in cultured fibroblasts. Cell 28: 831-841, 1982.
    • (1982) Cell , vol.28 , pp. 831-841
    • Wehland, J.1    Willingham, M.C.2    Gallo, M.G.3    Pastan, I.4
  • 78
    • 0028875216 scopus 로고
    • Cytoplasmic coat proteins involved in endosome function
    • Whitney JA, Gomez M, Sheff D, Kreis TE, Mellman I. Cytoplasmic coat proteins involved in endosome function. Cell 83: 703-713, 1995.
    • (1995) Cell , vol.83 , pp. 703-713
    • Whitney, J.A.1    Gomez, M.2    Sheff, D.3    Kreis, T.E.4    Mellman, I.5
  • 81
    • 0033553388 scopus 로고    scopus 로고
    • GTP-dependent binding of ADP-ribosylation factor to coatomer in close proximity to the binding site for dilysine retrieval motifs and p23
    • Zhao L, Helms JB, Brunner J, Wieland FT. GTP-dependent binding of ADP-ribosylation factor to coatomer in close proximity to the binding site for dilysine retrieval motifs and p23. J Biol Chem 274: 14198-14203, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 14198-14203
    • Zhao, L.1    Helms, J.B.2    Brunner, J.3    Wieland, F.T.4


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