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Giraudo C.G., Maccioni H.J. Endoplasmic reticulum export of glycosyltransferases depends on interaction of a cytoplasmic dibasic motif with Sar1. Mol Biol Cell. 14:2003;3753-3766
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Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles
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This structure-based alanine-scanning mutagenesis of the Sec24p subunit of COPII coat finds a mutant that shows a severe defect in the packaging of SNARE molecules and some but not all cargoes in an in vitro budding assay. This reveals that Sec24p has several independent binding sites. Interestingly, cargo proteins that share the same class of ER exit signals are not necessarily affected to a similar extent.
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Miller E.A., Beilharz T.H., Malkus P.N., Lee M.C., Hamamoto S., Orci L., Schekman R. Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Cell. 114:2003;497-509 This structure-based alanine-scanning mutagenesis of the Sec24p subunit of COPII coat finds a mutant that shows a severe defect in the packaging of SNARE molecules and some but not all cargoes in an in vitro budding assay. This reveals that Sec24p has several independent binding sites. Interestingly, cargo proteins that share the same class of ER exit signals are not necessarily affected to a similar extent.
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Miller, E.A.1
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Shimoni Y., Kurihara T., Ravazzola M., Orci L., Schekman R. Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae. J Cell Biol. 151:2000;973-984
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Shimoni, Y.1
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SNARE selectivity of the COPII coat
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The mechanism of SNARE complex binding to the Sec23p-Sec24p complex is analyzed by three assays: a biochemical binding assay of each SNARE molecule and Sec23p-Sec24p complex, X-ray crystallography analysis following the formation of co-crystal complexes with Sec24p, and usage of an alanine-substituted mutant form of SNARE protein. These sets of experiments not only identify the individual binding sites of each SNARE molecules with distinct Sec24 binding sites, but also demonstrate that SNARE assembly promotes efficient recognition by the Sec23p-Sec24p complex by exposing a hidden binding motif on Sed5p.
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Mossessova E., Bickford L.C., Goldberg J. SNARE selectivity of the COPII coat. Cell. 114:2003;483-495 The mechanism of SNARE complex binding to the Sec23p-Sec24p complex is analyzed by three assays: a biochemical binding assay of each SNARE molecule and Sec23p-Sec24p complex, X-ray crystallography analysis following the formation of co-crystal complexes with Sec24p, and usage of an alanine-substituted mutant form of SNARE protein. These sets of experiments not only identify the individual binding sites of each SNARE molecules with distinct Sec24 binding sites, but also demonstrate that SNARE assembly promotes efficient recognition by the Sec23p-Sec24p complex by exposing a hidden binding motif on Sed5p.
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Mossessova, E.1
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Reconstitution of coat protein complex II (COPII) vesicle formation from cargo-reconstituted proteoliposomes reveals the potential role of GTP hydrolysis by Sar1p in protein sorting
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Sato K., Nakano A. Reconstitution of coat protein complex II (COPII) vesicle formation from cargo-reconstituted proteoliposomes reveals the potential role of GTP hydrolysis by Sar1p in protein sorting. J Biol Chem. 279:2004;1330-1335
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Sato, K.1
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Belden W.J., Barlowe C. Role of Erv29p in collecting soluble secretory proteins into ER-derived transport vesicles. Science. 294:2001;1528-1531
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The Emp24 complex recruits a specific cargo molecule into endoplasmic-reticulum-derived vesicles
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Muniz M., Nuoffer C., Hauri H.P., Riezman H. The Emp24 complex recruits a specific cargo molecule into endoplasmic-reticulum-derived vesicles. J Cell Biol. 148:2000;925-930
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Muniz, M.1
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Muniz M., Morsomme P., Riezman H. Protein sorting upon exit from the endoplasmic reticulum. Cell. 104:2001;313-320
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The Rab GTPase Ypt1p and tethering factors couple protein sorting at the ER to vesicle targeting to the Golgi apparatus
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In this paper, ER-localized tethering factors, Uso1p, Ypt1p and the Sec34/35 complex, are shown using an in vitro assay to be involved in the sorting of GPI-proteins and non-GPI-proteins upon exit from ER. By contrast, the TRAPP complex that is part of the Golgi-localized tethering machinery is not necessary for ER cargo sorting. The sorting defects of uso1-1 and ypt1-1 mutant cells, but not TRAPP mutant cells, were also observed in ER-derived vesicles purified from these cells.
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Morsomme P., Riezman H. The Rab GTPase Ypt1p and tethering factors couple protein sorting at the ER to vesicle targeting to the Golgi apparatus. Dev Cell. 2:2002;307-317 In this paper, ER-localized tethering factors, Uso1p, Ypt1p and the Sec34/35 complex, are shown using an in vitro assay to be involved in the sorting of GPI-proteins and non-GPI-proteins upon exit from ER. By contrast, the TRAPP complex that is part of the Golgi-localized tethering machinery is not necessary for ER cargo sorting. The sorting defects of uso1-1 and ypt1-1 mutant cells, but not TRAPP mutant cells, were also observed in ER-derived vesicles purified from these cells.
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Dev Cell
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Morsomme, P.1
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The ER v-SNAREs are required for GPI-anchored protein sorting from other secretory proteins upon exit from the ER
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This paper reports that the sorting in the ER of GPI-proteins from non-GPI-proteins depends on v-SNAREs, Bos1p, Bet1p and Sec22p, but not on the t-SNARE Sed5p. The immunoelectron microscopic analysis also demonstrates that proper segregation of these cargo proteins occurs in sec18 mutant cells, but not in bos1-1 mutant cells.
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Morsomme P., Prescianotto-Baschong C., Riezman H. The ER v-SNAREs are required for GPI-anchored protein sorting from other secretory proteins upon exit from the ER. J Cell Biol. 162:2003;403-412 This paper reports that the sorting in the ER of GPI-proteins from non-GPI-proteins depends on v-SNAREs, Bos1p, Bet1p and Sec22p, but not on the t-SNARE Sed5p. The immunoelectron microscopic analysis also demonstrates that proper segregation of these cargo proteins occurs in sec18 mutant cells, but not in bos1-1 mutant cells.
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Morsomme, P.1
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Lipid rafts function in biosynthetic delivery of proteins to the cell surface in yeast
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Bagnat M., Keranen S., Shevchenko A., Simons K. Lipid rafts function in biosynthetic delivery of proteins to the cell surface in yeast. Proc Natl Acad Sci USA. 97:2000;3254-3259
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Imaging of procollagen transport reveals COPI-dependent cargo sorting during ER-to-Golgi transport in mammalian cells
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Stephens D.J., Pepperkok R. Imaging of procollagen transport reveals COPI-dependent cargo sorting during ER-to-Golgi transport in mammalian cells. J Cell Sci. 115:2002;1149-1160
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Stephens, D.J.1
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ER-to-Golgi carriers arise through direct en bloc protrusion and multistage maturation of specialized ER exit domains
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Mironov A.A., Mironov A.A. Jr., Beznoussenko G.V., Trucco A., Lupetti P., Smith J.D., Geerts W.J., Koster A.J., Burger K.N., Martone M.E., et al. ER-to-Golgi carriers arise through direct en bloc protrusion and multistage maturation of specialized ER exit domains. Dev Cell. 5:2003;583-594
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Mironov Jr., A.A.2
Beznoussenko, G.V.3
Trucco, A.4
Lupetti, P.5
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Koster, A.J.8
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Inositol-deacylation of glycosylphosphatidylinositol-anchored proteins is mediated by mammalian PGAP1 and yeast Bst1p
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Tanaka S, Maeda Y, Tashima Y, Kinoshita T: Inositol-deacylation of glycosylphosphatidylinositol-anchored proteins is mediated by mammalian PGAP1 and yeast Bst1p. J Biol Chem 2004.
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Tanaka, S.1
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Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding
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Vashist S., Kim W., Belden W.J., Spear E.D., Barlowe C., Ng D.T. Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding. J Cell Biol. 155:2001;355-368
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For whom the bell tolls: Protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection
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Kostova Z., Wolf D.H. For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection. EMBO J. 22:2003;2309-2317
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Trombetta E.S., Parodi A.J. Quality control and protein folding in the secretory pathway. Annu Rev Cell Dev Biol. 19:2003;649-676
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Degradation of endoplasmic reticulum (ER) quality control substrates requires transport between the ER and Golgi
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Caldwell S.R., Hill K.J., Cooper A.A. Degradation of endoplasmic reticulum (ER) quality control substrates requires transport between the ER and Golgi. J Biol Chem. 276:2001;23296-23303
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Taxis C., Vogel F., Wolf D.H. ER-golgi traffic is a prerequisite for efficient ER degradation. Mol Biol Cell. 13:2002;1806-1818
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Haynes C.M., Caldwell S., Cooper A.A. An HRD/DER-independent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transport. J Cell Biol. 158:2002;91-101
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Voeltz G.K., Rolls M.M., Rapoport T.A. Structural organization of the endoplasmic reticulum. EMBO Rep. 3:2002;944-950
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Pfeffer S. Membrane domains in the secretory and endocytic pathways. Cell. 112:2003;507-517
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Geuze H.J., Murk J.L., Stroobants A.K., Griffith J.M., Kleijmeer M.J., Koster A.J., Verkleij A.J., Distel B., Tabak H.F. Involvement of endoplasmic reticulum in peroxisome formation. Mol Biol Cell. 14:2003;2900-2907
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Stephens D.J. De novo formation, fusion and fission of mammalian COPII-coated endoplasmic reticulum exit sites. EMBO Rep. 4:2003;210-217
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Bevis B.J., Hammond A.T., Reinke C.A., Glick B.S. De novo formation of transitional ER sites and Golgi structures in Pichia pastoris. Nat Cell Biol. 4:2002;750-756
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