Signal integration in the endoplasmic reticulum unfolded protein response

被引：5210
作者：
Ron, David
Walter, Peter
机构：
[1] NYU, Sch Med, Kimmel Ctr Biol & Med, Skirball Inst, New York, NY 10016 USA
[2] Univ Calif San Francisco, Howard Hughes Med Inst, Dept Biochem & Biophys, San Francisco, CA 94158 USA
来源：
NATURE REVIEWS MOLECULAR CELL BIOLOGY | 2007年 / 8卷 / 07期
基金：
美国国家卫生研究院;
关键词：
D O I：
10.1038/nrm2199
中图分类号：
Q2 [细胞生物学];
学科分类号：
071009 ; 090102 ;
摘要：
The endoplasmic reticulum ( ER) responds to the accumulation of unfolded proteins in its lumen (ER stress) by activating intracellular signal transduction pathways-cumulatively called the unfolded protein response (UPR). Together, at least three mechanistically distinct arms of the UPR regulate the expression of numerous genes that function within the secretory pathway but also affect broad aspects of cell fate and the metabolism of proteins, amino acids and lipids. The arms of the UPR are integrated to provide a response that remodels the secretory apparatus and aligns cellular physiology to the demands imposed by ER stress.
引用
收藏
页码：519 / 529
页数：11
相关论文
共 100 条
[1]   Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response [J].
Bernales, Sebastian ;
McDonald, Kent L. ;
Walter, Peter .
PLOS BIOLOGY, 2006, 4 (12) :2311-2324
[2]   Intracellular signaling by the unfolded protein response [J].
Bernales, Sebastian ;
Papa, Feroz R. ;
Walter, Peter .
ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY, 2006, 22 :487-508
[3]   Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response [J].
Bertolotti, A ;
Zhang, YH ;
Hendershot, LM ;
Harding, HP ;
Ron, D .
NATURE CELL BIOLOGY, 2000, 2 (06) :326-332
[4]   ER stress-regulated translation increases tolerance to extreme hypoxia and promotes tumor growth [J].
Bi, MX ;
Naczki, C ;
Koritzinsky, M ;
Fels, D ;
Blais, J ;
Hu, NP ;
Harding, H ;
Novoa, I ;
Varia, M ;
Raleigh, J ;
Scheuner, D ;
Kaufman, RJ ;
Bell, J ;
Ron, D ;
Wouters, BG ;
Koumenis, C .
EMBO JOURNAL, 2005, 24 (19) :3470-3481
[5]   Perk-dependent translational regulation promotes tumor cell adaptation and angiogenesis in response to hypoxic stress [J].
Blais, Jaime D. ;
Addison, Christina L. ;
Edge, Robert ;
Falls, Theresa ;
Zhao, Huijun ;
Wary, Kishore ;
Koumenis, Costas ;
Harding, Heather P. ;
Ron, David ;
Holcik, Martin ;
Bell, John C. .
MOLECULAR AND CELLULAR BIOLOGY, 2006, 26 (24) :9517-9532
[6]   Activating transcription factor 4 is translationally regulated by hypoxic stress [J].
Blais, JD ;
Filipenko, V ;
Bi, MX ;
Harding, HP ;
Ron, D ;
Koumenis, C ;
Wouters, BG ;
Bell, JC .
MOLECULAR AND CELLULAR BIOLOGY, 2004, 24 (17) :7469-7482
[7]   A selective inhibitor-of eIF2α dephosphorylation protects cells from ER stress [J].
Boyce, M ;
Bryant, KF ;
Jousse, C ;
Long, K ;
Harding, HP ;
Scheuner, D ;
Kaufman, RJ ;
Ma, DW ;
Coen, DM ;
Ron, D ;
Yuan, JY .
SCIENCE, 2005, 307 (5711) :935-939
[8]   BIP AND SEC63P ARE REQUIRED FOR BOTH CO- AND POSTTRANSLATIONAL PROTEIN TRANSLOCATION INTO THE YEAST ENDOPLASMIC-RETICULUM [J].
BRODSKY, JL ;
GOECKELER, J ;
SCHEKMAN, R .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (21) :9643-9646
[9]   Growth arrest and DNA damage-inducible protein GADD34 targets protein phosphatase 1α to the endoplasmic reticulum and promotes dephosphorylation of the α subunit of eukaryotic translation initiation factor 2 [J].
Brush, MH ;
Weiser, DC ;
Shenolikar, S .
MOLECULAR AND CELLULAR BIOLOGY, 2003, 23 (04) :1292-1303
[10]   IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA [J].
Calfon, M ;
Zeng, HQ ;
Urano, F ;
Till, JH ;
Hubbard, SR ;
Harding, HP ;
Clark, SG ;
Ron, D .
NATURE, 2002, 415 (6867) :92-96
12345678910