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THE MAMMALIAN UNFOLDED PROTEIN RESPONSE
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▪ Abstract In the endoplasmic reticulum (ER), secretory and transmembrane proteins fold into their native conformation and undergo posttranslational modifications important for their activity and structure. When protein folding in the ER is inhibited, signal transduction pathways, which increase the biosynthetic capacity and decrease the biosynthetic burden of the ER to maintain the homeostasis of this organelle, are activated. These pathways are called the unfolded protein response (UPR). In this review, we briefly summarize principles of protein folding and molecular chaperone function important for a mechanistic understanding of UPR-signaling events. We then discuss mechanisms of signal transduction employed by the UPR in mammals and our current understanding of the remodeling of cellular processes by the UPR. Finally, we summarize data that demonstrate that UPR signaling feeds into decision making in other processes previously thought to be unrelated to ER function, e.g., eukaryotic starvation responses and differentiation programs.
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The mitochondrial permeability transition pore and its role in cell death
CROMPTON, M. (1999) · Biochemical Journal · doi:10.1042/bj3410233 · Cited by 2,432
Harding, H. P., Zhang, Y., Bertolotti, A., Zeng, H., & Ron, D. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80330-5 · Cited by 2,021
ER Stress Induces Cleavage of Membrane-Bound ATF6 by the Same Proteases that Process SREBPs
Ye, J., Rawson, R. B., Komuro, R., Chen, X., Davé, U. P., Prywes, R., Brown, M. S., & Goldstein, J. L. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00133-7 · Cited by 1,871
Delépine, M., Nicolino, M., Barrett, T., Golamaully, M., Mark Lathrop, G., & Julier, C. (2000) · Nature Genetics · doi:10.1038/78085 · Cited by 813
Histone acetylation and deacetylation in yeast
Kurdistani, S. K., & Grunstein, M. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1075 · Cited by 677
Sriburi, R., Jackowski, S., Mori, K., & Brewer, J. W. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200406136 · Cited by 653
Yan, W., Frank, C. L., Korth, M. J., Sopher, B. L., Novoa, I., Ron, D., & Katze, M. G. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252341799 · Cited by 385
Research works printed but not linked: 175
- Selye H, 1985, Basal Facts, 7, 3
- 10.1016/j.devcel.2004.08.011 · DOI
- 10.1038/ncb0903-769 · DOI
- 10.1016/j.mrfmmm.2004.06.056 · DOI · Paper page
- Kaufman RJ, 1988, J. Biol. Chem., 263, 6352, 10.1016/S0021-9258(18)68793-9 · DOI · Paper page
- Dorner AJ, 1989, J. Biol. Chem., 264, 20602, 10.1016/S0021-9258(19)47105-6 · DOI · Paper page
- 10.1002/bit.10206 · DOI
- 10.1038/332462a0 · DOI · Paper page
- 10.1210/er.19.2.173 · doi:10.1210/er.19.2.173
- 10.1034/j.1600-0854.2000.011104.x · DOI · Paper page
- 10.1038/415092a · DOI · Paper page
- 10.1128/JVI.77.23.12617-12629.2003 · DOI
- 10.1007/BF00023606 · doi:10.1007/bf00023606
- 10.1105/tpc.11.10.1935 · doi:10.1105/tpc.11.10.1935
- 10.1038/16729 · DOI · Paper page
- 10.1016/S0092-8674(00)80835-1 · DOI · Paper page
- 10.1016/S0092-8674(00)81146-0 · DOI · Paper page
- 10.1038/43897 · doi:10.1038/43897
- 10.1038/47513 · DOI · Paper page
- 10.1016/S1097-2765(01)00265-9 · DOI · Paper page
- 10.1101/gad.992302 · DOI · Paper page
- 10.1016/0092-8674(90)90148-8 · DOI · Paper page
- 10.1016/0092-8674(77)90305-1 · DOI · Paper page
- 10.1101/gad.852300 · DOI
- 10.1128/MCB.21.3.916-927.2001 · DOI · Paper page
- 10.1073/pnas.202495299 · DOI
- 10.1038/sj.emboj.7600233 · DOI
- 10.1091/mbc.8.9.1805 · DOI · Paper page
- 10.1002/(SICI)1521-3773(19980420)37:7<868::AID-ANIE868>3.3.CO;2-8 · doi:10.1002/(sici)1521-3773(19980420)37:7<868::aid-anie868>3.3.co;2-8
- 10.1073/pnas.47.9.1309 · DOI · Paper page
- 10.1006/scdb.1999.0315 · DOI · Paper page
- 10.1016/0092-8674(75)90167-1 · DOI · Paper page
- 10.1074/jbc.M302117200 · DOI
- 10.1021/bi9530752 · DOI
- 10.1083/jcb.114.2.189 · DOI · Paper page
- 10.1074/jbc.270.30.18051 · DOI
- 10.1074/jbc.274.10.6203 · DOI · Paper page
- 10.1146/annurev.genet.35.102401.090313 · DOI · Paper page
- 10.1038/nrm1052 · DOI · Paper page
- 10.1074/jbc.M303395200 · DOI · Paper page
- 10.1126/science.1079181 · DOI · Paper page
- 10.1021/bi00116a015 · DOI · Paper page
- Weng S, 1993, J. Biol. Chem., 268, 25656, 10.1016/S0021-9258(19)74440-8 · DOI
- Trombetta SE, 1992, J. Biol. Chem., 267, 9236, 10.1016/S0021-9258(19)50413-6 · DOI · Paper page
- 10.1091/mbc.4.11.1109 · DOI · Paper page
- 10.1128/MCB.12.7.3288 · DOI · Paper page
- 10.1074/jbc.273.47.30903 · DOI
- 10.1006/scdb.1999.0320 · DOI · Paper page
- 10.1126/science.1092287 · DOI · Paper page
- 10.1093/emboj/17.20.5877 · DOI
- 10.1074/jbc.273.11.6009 · DOI · Paper page
- 10.1093/emboj/cdg378 · DOI
- 10.1083/jcb.147.7.1443 · DOI · Paper page
- 10.1006/scdb.1999.0318 · DOI · Paper page
- 10.1093/emboj/19.23.6440 · DOI · Paper page
- Hightower LE, Sadis SE, Takenaka IM. 1994. In The Biology of Heat Shock Proteins and Molecular Chaperones , ed.RI Morimoto, A Tissieres, C Georgopoulos, pp.197–207. Plainview, NY: Cold Spring Harbor Lab.
- 10.1146/annurev.biochem.67.1.49 · DOI · Paper page
- 10.1073/pnas.262661199 · DOI · Paper page
- 10.1038/nsmb715 · DOI
- 10.1091/mbc.10.11.3787 · DOI · Paper page
- 10.1074/jbc.M110636200 · DOI · Paper page
- Wang Y, 2000, J. Biol. Chem., 275, 27013, 10.1016/S0021-9258(19)61473-0 · DOI · Paper page
- 10.1074/jbc.M010486200 · DOI · Paper page
- 10.1128/MCB.21.4.1239-1248.2001 · DOI · Paper page
- 10.1016/S1534-5807(02)00203-4 · DOI · Paper page
- 10.1074/jbc.M309804200 · DOI · Paper page
- 10.1002/jcb.20118 · DOI
- 10.1074/jbc.M112454200 · DOI
- 10.1074/jbc.M004454200 · DOI · Paper page
- 10.1038/35014014 · DOI · Paper page
- 10.1074/jbc.M300418200 · DOI
- 10.1074/jbc.M200903200 · DOI · Paper page
- 10.1101/gad.12.12.1812 · DOI · Paper page
- 10.1093/emboj/17.19.5708 · DOI · Paper page
- 10.1128/MCB.9.2.701 · DOI · Paper page
- 10.1016/S1097-2765(00)80034-9 · DOI · Paper page
- 10.1016/j.molcel.2004.06.038 · DOI · Paper page
- 10.1083/jcb.200302084 · DOI · Paper page
- 10.1038/sj.onc.1205340 · DOI
- 10.1096/fj.02-0657fje · DOI
- 10.1126/science.281.5381.1322 · DOI · Paper page
- 10.1128/MCB.20.3.929-935.2000 · DOI · Paper page
- 10.1073/pnas.94.21.11357 · DOI · Paper page
- 10.1016/0092-8674(93)90648-A · DOI · Paper page
- 10.1016/0092-8674(93)90521-Q · DOI · Paper page
- 10.1016/S0092-8674(00)80369-4 · DOI · Paper page
- 10.1126/science.1090031 · DOI · Paper page
- 10.1101/gad.839400 · DOI · Paper page
- 10.1016/S0092-8674(00)81360-4 · DOI · Paper page
- 10.1101/gad.964702 · DOI · Paper page
- 10.1016/S0092-8674(01)00611-0 · DOI · Paper page
- 10.1093/emboj/18.11.3119 · DOI · Paper page
- 10.1016/S0092-8674(00)81361-6 · DOI · Paper page
- 10.1128/MCB.10.3.1049 · doi:10.1128/mcb.10.3.1049
- 10.1126/science.8392224 · DOI
- 10.1128/MCB.11.11.5410 · doi:10.1128/mcb.11.11.5410
- Laski FA, 1983, J. Biol. Chem., 258, 11974, 10.1016/S0021-9258(17)44327-4 · doi:10.1016/s0021-9258(17)44327-4
- 10.1073/pnas.95.24.14136 · doi:10.1073/pnas.95.24.14136
- 10.1074/jbc.273.21.12685 · DOI · Paper page
- 10.1016/S0092-8674(01)00505-0 · DOI · Paper page
- 10.1128/MCB.2.3.241 · DOI
- 10.1073/pnas.050010197 · DOI · Paper page
- 10.1073/pnas.0307425100 · DOI
- 10.1073/pnas.1334037100 · DOI · Paper page
- 10.1002/j.1460-2075.1992.tb05323.x · DOI · Paper page
- 10.1016/S0022-2836(02)00322-4 · DOI
- 10.1074/jbc.275.5.3377 · DOI
- 10.1073/pnas.94.9.4289 · DOI
- 10.1111/j.1365-2443.2004.00704.x · DOI
- 10.1101/gad.8.7.796 · DOI · Paper page
- 10.1016/S0092-8674(00)00134-3 · DOI · Paper page
- 10.1016/S0092-8674(00)80217-2 · DOI · Paper page
- 10.1126/science.1084648 · DOI · Paper page
- 10.1038/ng1235 · DOI · Paper page
- 10.1128/MCB.18.4.1967 · doi:10.1128/mcb.18.4.1967
- 10.1091/mbc.E03-11-0851 · DOI · Paper page
- 10.1016/j.neuint.2004.01.003 · DOI
- 10.1128/MCB.23.20.7198-7209.2003 · DOI · Paper page
- 10.1073/pnas.220247197 · DOI · Paper page
- 10.1016/S0378-1119(02)01056-9 · DOI · Paper page
- 10.1016/S1097-2765(00)00108-8 · DOI · Paper page
- 10.1016/S0092-8674(03)00345-3 · DOI · Paper page
- 10.1073/pnas.0400541101 · DOI · Paper page
- 10.1083/jcb.200408003 · DOI · Paper page
- 10.1093/nar/29.21.4341 · DOI
- 10.1146/annurev.pharmtox.43.100901.140229 · DOI · Paper page
- 10.1016/S1097-2765(03)00105-9 · DOI · Paper page
- 10.1002/j.1460-2075.1995.tb07256.x · DOI · Paper page
- 10.1074/jbc.M405616200 · DOI
- 10.1083/jcb.200308075 · DOI · Paper page
- 10.1074/jbc.M301107200 · DOI · Paper page
- 10.1128/MCB.23.4.1292-1303.2003 · DOI · Paper page
- 10.1074/jbc.M310535200 · DOI
- 10.1073/pnas.082483399 · doi:10.1073/pnas.082483399
- 10.1128/MCB.24.3.1365-1377.2004 · DOI · Paper page
- 10.1042/BJ20020391 · DOI · Paper page
- 10.1128/MCB.23.21.7448-7459.2003 · DOI · Paper page
- 10.2174/1389203013381189 · doi:10.2174/1389203013381189
- 10.1074/jbc.M313724200 · DOI
- 10.1111/j.1356-9597.2004.00735.x · DOI
- 10.1016/S1534-5807(03)00022-4 · DOI · Paper page
- 10.1247/csf.8.309 · DOI
- 10.1083/jcb.200112008 · DOI
- 10.1016/S0014-5793(99)00721-8 · doi:10.1016/s0014-5793(99)00721-8
- Chang HJ, 2002, Genetics, 162, 29, 10.1093/genetics/162.1.29 · DOI
- 10.1126/science.1096083 · DOI · Paper page
- 10.1371/journal.pbio.0020342 · DOI · Paper page
- 10.1172/JCI200215593 · doi:10.1172/jci200215593 · Paper page
- 10.1038/sj.emboj.7600106 · DOI · Paper page
- 10.1038/ncb1035 · DOI · Paper page
- 10.1074/jbc.M405195200 · DOI · Paper page
- 10.1128/MCB.22.11.3864-3874.2002 · DOI · Paper page
- 10.1172/JCI200214550 · DOI
- 10.1083/jcb.110.5.1501 · DOI · Paper page
- 10.1038/35085509 · DOI · Paper page
- 10.1038/ni907 · DOI · Paper page
- 10.1016/j.immuni.2004.06.010 · DOI · Paper page
- 10.1128/MCB.20.23.8684-8695.2000 · DOI
- 10.1128/MCB.20.7.2592-2603.2000 · DOI · Paper page
- 10.1016/j.tcb.2003.11.001 · DOI · Paper page
- 10.1126/science.1081208 · DOI · Paper page
- 10.1083/jcb.150.4.887 · DOI · Paper page
- 10.1074/jbc.M202726200 · DOI · Paper page
- 10.1042/0264-6021:3410233 · doi:10.1042/0264-6021:3410233 · Paper page
- 10.1038/sj.cdd.4401006 · DOI
- 10.1016/S0022-2836(02)00234-6 · DOI · Paper page
- 10.1128/MCB.21.4.1249-1259.2001 · DOI · Paper page
- 10.1074/jbc.M010677200 · DOI · Paper page
- 10.1074/jbc.270.15.8642 · DOI
- 10.1038/nm0502-485 · DOI · Paper page
- 10.3816/CLM.2002.n.011 · DOI
- Hurst HC, 1995, Protein Profile, 2, 101
- Hai T, 1999, Gene Expr., 7, 321
- 10.1016/S0378-1119(01)00551-0 · DOI · Paper page
- 10.1172/JCI200521848 · DOI · Paper page
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Metadata
- Authors
- Schröder, M., & Kaufman, R. J.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2005-06-01
- Volume
- 74
- Issue
- 1
- Pages
- 739-789
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2112286580
- Cited by
- 3,026
- References
- 7
- FWCI
- 8.58
- Type
- journal article
- Language
- en
- Open access
- green
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