Adaptation of endoplasmic reticulum exit sites to acute and chronic increases in cargo load
dc.contributor.author | Farhan, Hesso | en_US |
dc.contributor.author | Weiss, Matthias | en_US |
dc.contributor.author | Tani, Katsuko | en_US |
dc.contributor.author | Kaufman, Randal J | en_US |
dc.contributor.author | Hauri, Hans‐peter | en_US |
dc.date.accessioned | 2014-01-08T20:35:06Z | |
dc.date.available | 2014-01-08T20:35:06Z | |
dc.date.issued | 2008-08-06 | en_US |
dc.identifier.citation | Farhan, Hesso; Weiss, Matthias; Tani, Katsuko; Kaufman, Randal J; Hauri, Hans‐peter (2008). "Adaptation of endoplasmic reticulum exit sites to acute and chronic increases in cargo load." The EMBO Journal 27(15): 2043-2054. <http://hdl.handle.net/2027.42/102229> | en_US |
dc.identifier.issn | 0261-4189 | en_US |
dc.identifier.issn | 1460-2075 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/102229 | |
dc.publisher | John Wiley & Sons, Ltd | en_US |
dc.subject.other | Secretory Pathway | en_US |
dc.subject.other | Phosphatidylinositol‐4 Kinase IIIα | en_US |
dc.subject.other | COPII | en_US |
dc.subject.other | Unfolded Protein Response | en_US |
dc.subject.other | Sec16 | en_US |
dc.title | Adaptation of endoplasmic reticulum exit sites to acute and chronic increases in cargo load | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.identifier.pmid | 18650939 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/102229/1/emboj2008136.pdf | |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/102229/2/emboj2008136-sup-0001.pdf | |
dc.identifier.doi | 10.1038/emboj.2008.136 | en_US |
dc.identifier.source | The EMBO Journal | en_US |
dc.identifier.citedreference | Sato M, Sato K, Nakano A ( 2002 ) Evidence for the intimate relationship between vesicle budding from the ER and the unfolded protein response. Biochem Biophys Res Commun 296: 560 – 567 | en_US |
dc.identifier.citedreference | Iinuma T, Shiga A, Nakamot K, O‧Brien MB, Aridor M, Arimitsu N, Tagaya M, Tani K ( 2007 ) Mammalian Sec16/p250 plays a role in membrane traffic from the endoplasmic reticulum. J Biol Chem 282: 17632 – 17639 | en_US |
dc.identifier.citedreference | Lee AH, Chu GC, Iwakoshi NN, Glimcher LH ( 2005 ) XBP‐1 is required for biogenesis of cellular secretory machinery of exocrine glands. EMBO J 24: 4368 – 4380 | en_US |
dc.identifier.citedreference | Lee K, Tirasophon W, Shen X, Michalak M, Prywes R, Okada T, Yoshida H, Mori K, Kaufman RJ ( 2002 ) IRE1‐mediated nonconventional mRNA splicing and S2P‐mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response. Genes Dev 16: 452 – 466 | en_US |
dc.identifier.citedreference | Lee MC, Miller EA, Goldberg J, Orci L, Schekman R ( 2004 ) Bi‐directional protein transport between the ER and Golgi. Annu Rev Cell Dev Biol 20: 87 – 123 | en_US |
dc.identifier.citedreference | Lin JH, Li H, Yasumura D, Cohen HR, Zhang C, Panning B, Shokat KM, Lavail MM, Walter P ( 2007 ) IRE1 signaling affects cell fate during the unfolded protein response. Science 318: 944 – 949 | en_US |
dc.identifier.citedreference | Lippincott‐Schwartz J, Yuan LC, Bonifacino JS, Klausner RD ( 1989 ) Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi to ER. Cell 56: 801 – 813 | en_US |
dc.identifier.citedreference | Mancias JD, Goldberg J ( 2007 ) The transport signal on Sec22 for packaging into COPII‐coated vesicles is a conformational epitope. Mol Cell 26: 403 – 414 | en_US |
dc.identifier.citedreference | Matsuoka K, Orci L, Amherdt M, Bednarek SY, Hamamoto S, Schekman R, Yeung T ( 1998 ) COPII‐coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes. Cell 93: 263 – 275 | en_US |
dc.identifier.citedreference | Mezzacasa A, Helenius A ( 2002 ) The transitional ER defines a boundary for quality control in the secretion of tsO45 VSVG glycoprotein. Traffic 3: 833 – 849 | en_US |
dc.identifier.citedreference | Nishimura N, Bannykh S, Slabough S, Matteson J, Altschuler Y, Hahn K, Balch WE ( 1999 ) A di‐acidic (DXE) code directs concentration of cargo during export from the endoplasmic reticulum. J Biol Chem 274: 15937 – 15946 | en_US |
dc.identifier.citedreference | Ron D, Walter P ( 2007 ) Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 8: 519 – 529 | en_US |
dc.identifier.citedreference | Schröder M, Kaufman RJ ( 2005 ) The mammalian unfolded protein response. Annu Rev Biochem 74: 739 – 789 | en_US |
dc.identifier.citedreference | Shaffer AL, Shapiro‐Shelef M, Iwakoshi NN, Lee AH, Qian SB, Zhao H, Yu X, Yang L, Tan BK, Rosenwald A, Hurt EM, Petroulakis E, Sonenberg N, Yewdell JW, Calame K, Glimcher LH, Staudt LM ( 2004 ) XBP1, downstream of Blimp‐1, expands the secretory apparatus and other organelles, and increases protein synthesis in plasma cell differentiation. Immunity 21: 81 – 93 | en_US |
dc.identifier.citedreference | Shugrue CA, Kolen ER, Peters H, Czernik A, Kaiser C, Matovcik L, Hubbard AL, Gorelick F ( 1999 ) Identification of the putative mammalian orthologue of Sec31P, a component of the COPII coat. J Cell Sci 112: 4547 – 4556 | en_US |
dc.identifier.citedreference | Sriburi R, Bommiasamy H, Buldak GL, Robbins GR, Frank M, Jackowski S, Brewer JW ( 2007 ) Coordinate regulation of phospholipid biosynthesis and secretory pathway gene expression in XBP‐1(S)‐induced endoplasmic reticulum biogenesis. J Biol Chem 282: 7024 – 7034 | en_US |
dc.identifier.citedreference | Stephens DJ ( 2003 ) De novo formation, fusion and fission of mammalian COPII‐coated endoplasmic reticulum exit sites. EMBO Rep 4: 210 – 217 | en_US |
dc.identifier.citedreference | Travers KJ, Patil CK, Wodicka L, Lockhart DJ, Weissman JS, Walter P ( 2000 ) Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER‐associated degradation. Cell 101: 249 – 258 | en_US |
dc.identifier.citedreference | Watson P, Townley AK, Koka P, Palmer KJ, Stephens DJ ( 2006 ) Sec16 defines endoplasmic reticulum exit sites and is required for secretory cargo export in mammalian cells. Traffic 7: 1678 – 1687 | en_US |
dc.identifier.citedreference | Wendeler MW, Paccaud JP, Hauri HP ( 2007 ) Role of Sec24 isoforms in selective export of membrane proteins from the endoplasmic reticulum. EMBO Rep 8: 258 – 264 | en_US |
dc.identifier.citedreference | Wong K, Meyers R, Cantley LC ( 1997 ) Subcellular localization of phosphatidylinositol 4‐kinase isoforms. J Biol Chem 272: 13236 – 13241 | en_US |
dc.identifier.citedreference | Zhang K, Wong HN, Song B, Miller CN, Scheuner D, Kaufman RJ ( 2005 ) The unfolded protein response sensor IRE1alpha is required at 2 distinct steps in B cell lymphopoiesis. J Clin Invest 115: 268 – 281 | en_US |
dc.identifier.citedreference | Acosta‐Alvear D, Zhou Y, Blais A, Tsikitis M, Lents NH, Arias C, Lennon CJ, Kluger Y, Dynlacht BD ( 2007 ) XBP1 controls diverse cell type‐ and condition‐specific transcriptional regulatory networks. Mol Cell 27: 53 – 66 | en_US |
dc.identifier.citedreference | Bevis BJ, Hammond AT, Reinke CA, Glick BS ( 2002 ) De novo formation of transitional ER sites and Golgi structures in Pichia pastoris. Nat Cell Biol 4: 750 – 756 | en_US |
dc.identifier.citedreference | Bhattacharyya D, Glick BS ( 2007 ) Two mammalian Sec16 homologues have nonredundant functions in endoplasmic reticulum (ER) export and transitional ER organization. Mol Biol Cell 18: 839 – 849 | en_US |
dc.identifier.citedreference | Bi X, Corpina RA, Goldberg J ( 2002 ) Structure of the Sec23/24‐Sar1 pre‐budding complex of the COPII vesicle coat. Nature 419: 271 – 277 | en_US |
dc.identifier.citedreference | Blumental‐Perry A, Haney CJ, Weixel KM, Watkins SC, Weisz OA, Aridor M ( 2006 ) Phosphatidylinositol 4‐phosphate formation at ER exit sites regulates ER export. Dev Cell 11: 671 – 682 | en_US |
dc.identifier.citedreference | Diao A, Rahman D, Pappin DJ, Lucocq J, Lowe M ( 2003 ) The coiled‐coil membrane protein golgin‐84 is a novel rab effector required for Golgi ribbon formation. J Cell Biol 160: 201 – 212 | en_US |
dc.identifier.citedreference | Doms RW, Russand G, Yewdell JW ( 1989 ) Brefeldin A redistributes resident and itinerant Golgi proteins to the endoplasmic reticulum. J Cell Biol 109: 61 – 72 | en_US |
dc.identifier.citedreference | Farhan H, Reiterer V, Korkhov VM, Schmid JA, Freissmuth M, Sitte HH ( 2007 ) Concentrative export from the endoplasmic reticulum of the gamma‐aminobutyric acid transporter 1 requires binding to SEC24D. J Biol Chem 282: 7679 – 7689 | en_US |
dc.identifier.citedreference | Forster R, Weiss M, Zimmermann T, Reynaud EG, Verissimo F, Stephens DJ, Pepperkok R ( 2006 ) Secretory cargo regulates the turnover of COPII subunits at single ER exit sites. Curr Biol 16: 173 – 179 | en_US |
dc.identifier.citedreference | Gimeno RE, Espenshade P, Kaiser CA ( 1996 ) COPII coat subunit interactions: Sec24p and Sec23p bind to adjacent regions of Sec16p. Mol Biol Cell 7: 1815 – 1823 | en_US |
dc.identifier.citedreference | Guo Y, Linstedt AD ( 2006 ) COPII–Golgi protein interactions regulate COPII coat assembly and Golgi size. J Cell Biol 174: 53 – 63 | en_US |
dc.identifier.citedreference | Hanton SL, Chatre L, Renna L, Matheson LA, Brandizzi F ( 2007 ) De novo formation of plant endoplasmic reticulum export sites is membrane cargo induced and signal mediated. Plant Physiol 143: 1640 – 1650 | en_US |
dc.identifier.citedreference | Heinzer S, Wörz S, Kalla C, Rohr K, Weiss M ( 2008 ) A model for the self‐organization of exit sites in the endoplasmic reticulum. J Cell Sci 121: 55 – 64 | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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