Simultaneous induction of the four subunits of the TRAP complex by ER stress accelerates ER degradation
dc.contributor.author | Nagasawa, Koji | en_US |
dc.contributor.author | Higashi, Toshio | en_US |
dc.contributor.author | Hosokawa, Nobuko | en_US |
dc.contributor.author | Kaufman, Randal J | en_US |
dc.contributor.author | Nagata, Kazuhiro | en_US |
dc.date.accessioned | 2014-01-08T20:34:43Z | |
dc.date.available | 2014-01-08T20:34:43Z | |
dc.date.issued | 2007-05 | en_US |
dc.identifier.citation | Nagasawa, Koji; Higashi, Toshio; Hosokawa, Nobuko; Kaufman, Randal J; Nagata, Kazuhiro (2007). "Simultaneous induction of the four subunits of the TRAP complex by ER stress accelerates ER degradation." EMBO reports 8(5): 483-489. <http://hdl.handle.net/2027.42/102129> | en_US |
dc.identifier.issn | 1469-221X | en_US |
dc.identifier.issn | 1469-3178 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/102129 | |
dc.publisher | John Wiley & Sons, Ltd | en_US |
dc.subject.other | UPR | en_US |
dc.subject.other | Sec61 Translocon | en_US |
dc.subject.other | ERAD | en_US |
dc.subject.other | XBP1/IRE1α Pathway | en_US |
dc.subject.other | TRAP Complex | en_US |
dc.title | Simultaneous induction of the four subunits of the TRAP complex by ER stress accelerates ER degradation | 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 | 17380188 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/102129/1/embor7400933-sup-0003.pdf | |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/102129/2/embor7400933-sup-0007.pdf | |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/102129/3/embor7400933-sup-0002.pdf | |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/102129/4/embor7400933-sup-0006.pdf | |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/102129/5/embor7400933-sup-0001.pdf | |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/102129/6/embor7400933-sup-0008.pdf | |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/102129/7/embor7400933-sup-0005.pdf | |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/102129/8/embor7400933-sup-0009.pdf | |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/102129/9/embor7400933-sup-0004.pdf | |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/102129/10/embor7400933.pdf | |
dc.identifier.doi | 10.1038/sj.embor.7400933 | en_US |
dc.identifier.source | EMBO reports | en_US |
dc.identifier.citedreference | Sifers RN, Brashears‐Macatee S, Kidd VJ, Muensch H, Woo SL ( 1988 ) A frameshift mutation results in a truncated α1‐antitrypsin that is retained within the rough endoplasmic reticulum. J Biol Chem 263: 7330 – 7335 | en_US |
dc.identifier.citedreference | Ellgaard L, Helenius A ( 2003 ) Quality control in the endoplasmic reticulum. Nat Rev Mol Cell Biol 4: 181 – 191 | en_US |
dc.identifier.citedreference | Fons RD, Bogert BA, Hegde RS ( 2003 ) Substrate‐specific function of the translocon‐associated protein complex during translocation across the ER membrane. J Cell Biol 160: 529 – 539 | en_US |
dc.identifier.citedreference | Hartmann E, Gorlich D, Kostka S, Otto A, Kraft R, Knespel S, Burger E, Rapoport TA, Prehn S ( 1993 ) A tetrameric complex of membrane proteins in the endoplasmic reticulum. Eur J Biochem 214: 375 – 381 | en_US |
dc.identifier.citedreference | Hosokawa N, Wada I, Hasegawa K, Yorihuzi T, Tremblay LO, Herscovics A, Nagata K ( 2001 ) A novel ER α‐mannosidase‐like protein accelerates ER‐associated degradation. EMBO Rep 2: 415 – 422 | en_US |
dc.identifier.citedreference | Kalies KU, Allan S, Sergeyenko T, Kroger H, Romisch K ( 2005 ) The protein translocation channel binds proteasomes to the endoplasmic reticulum membrane. EMBO J 24: 2284 – 2293 | 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 unconventional 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 | Lilley BN, Ploegh HL ( 2004 ) A membrane protein required for dislocation of misfolded proteins from the ER. Nature 429: 834 – 840 | en_US |
dc.identifier.citedreference | Menetret JF, Hegde RS, Heinrich SU, Chandramouli P, Ludtke SJ, Rapoport TA, Akey CW ( 2005 ) Architecture of the ribosome‐channel complex derived from native membranes. J Mol Biol 348: 445 – 457 | en_US |
dc.identifier.citedreference | Meusser B, Hirsch C, Jarosch E, Sommer T ( 2005 ) ERAD: the long road to destruction. Nat Cell Biol 7: 766 – 772 | en_US |
dc.identifier.citedreference | Oda Y, Okada T, Yoshida H, Kaufman RJ, Nagata K, Mori K ( 2006 ) Derlin‐2 and Derlin‐3 are regulated by the mammalian unfolded protein response and are required for ER‐associated degradation. J Cell Biol 172: 383 – 393 | en_US |
dc.identifier.citedreference | Pilon M, Schekman R, Romisch K ( 1997 ) Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation. EMBO J 16: 4540 – 4548 | en_US |
dc.identifier.citedreference | Plemper RK, Bohmler S, Bordallo J, Sommer T, Wolf DH ( 1997 ) Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature 388: 891 – 895 | en_US |
dc.identifier.citedreference | Romisch K ( 2005 ) Endoplasmic reticulum‐associated degradation. Annu Rev Cell Dev Biol 21: 435 – 456 | en_US |
dc.identifier.citedreference | Rutkowski DT, Kaufman RJ ( 2004 ) A trip to the ER: coping with stress. Trends Cell Biol 14: 20 – 28 | en_US |
dc.identifier.citedreference | Shaffer AL et al ( 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 | Van den Berg B, Clemons Jr WM, Collinson I, Modis Y, Hartmann E, Harrison SC, Rapoport TA ( 2004 ) X‐ray structure of a protein‐conducting channel. Nature 427: 36 – 44 | en_US |
dc.identifier.citedreference | Wada I, Rindress D, Cameron PH, Ou WJ, Doherty II JJ, Louvard D, Bell AW, Dignard D, Thomas DY, Bergeron JJ ( 1991 ) SSRα and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane. J Biol Chem 266: 19599 – 19610 | en_US |
dc.identifier.citedreference | Wang L, Dobberstein B ( 1999 ) Oligomeric complexes involved in translocation of proteins across the membrane of the endoplasmic reticulum. FEBS Lett 457: 316 – 322 | en_US |
dc.identifier.citedreference | Ye Y, Shibata Y, Yun C, Ron D, Rapoport TA ( 2004 ) A membrane protein complex mediates retro‐translocation from the ER lumen into the cytosol. Nature 429: 841 – 847 | en_US |
dc.identifier.citedreference | Yoshida H, Matsui T, Hosokawa N, Kaufman RJ, Nagata K, Mori K ( 2003 ) A time‐dependent phase shift in the mammalian unfolded protein response. Dev Cell 4: 265 – 271 | en_US |
dc.identifier.citedreference | Yu H, Kaung G, Kobayashi S, Kopito RR ( 1997 ) Cytosolic degradation of T‐cell receptor α chains by the proteasome. J Biol Chem 272: 20800 – 20804 | en_US |
dc.identifier.citedreference | de Virgilio M, Weninger H, Ivessa NE ( 1998 ) Ubiquitination is required for the retro‐translocation of a short‐lived luminal endoplasmic reticulum glycoprotein to the cytosol for degradation by the proteasome. J Biol Chem 273: 9734 – 9743 | en_US |
dc.identifier.citedreference | Diatchenko L et al ( 1996 ) Suppression subtractive hybridization: a method for generating differentially regulated or tissue‐specific cDNA probes and libraries. Proc Natl Acad Sci USA 93: 6025 – 6030 | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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