Coping with stress: cellular relaxation techniques

被引：31

作者：

Hirsch, Christian ^{[1
]}

Gauss, Robert ^{[1
]}

Sommer, Thomas ^{[1
]}

机构：

[1] Max Delbruck Ctr Mol Med, D-13125 Berlin, Germany

来源：

TRENDS IN CELL BIOLOGY | 2006年 / 16卷 / 12期

关键词：

D O I：

10.1016/j.tcb.2006.10.006

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Proteins damaged by stressors such as heat, oxidizing conditions or toxic agents are deleterious to cells and must be properly taken care of. Accordingly, misfolded proteins trigger a cellular stress response that aims to either repair defective polypeptides or eliminate faulty elements when salvage is not possible. This stress response provides time for additional stressor-specific pathways that adapt the cell to the changed environment if necessary. Recent studies have investigated how proteins that frustrate the folding machinery are recognized and cleared from the cell. Surprisingly, these clearance mechanisms are not restricted to the protein level. The stress response can also eliminate the mRNA of polypeptides that are refractory to folding.

引用

收藏

页码：657 / 663

页数：7

相关论文

共 65 条

[1] The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator [J].

Alberti, S ;

Böhse, K ;

Arndt, V ;

Schmitz, A ;

Höhfeld, J .

MOLECULAR BIOLOGY OF THE CELL, 2004, 15 (09) :4003-4010

[2] BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP [J].

Arndt, V ;

Daniel, C ;

Nastainczyk, W ;

Alberti, S ;

Höhfeld, J .

MOLECULAR BIOLOGY OF THE CELL, 2005, 16 (12) :5891-5900

[3] Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation [J].

Bays, NW ;

Gardner, RG ;

Seelig, LP ;

Joazeiro, CA ;

Hampton, RY .

NATURE CELL BIOLOGY, 2001, 3 (01) :24-29

[4] HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins [J].

Bays, NW ;

Wilhovsky, SK ;

Goradia, A ;

Hodgkiss-Harlow, K ;

Hampton, RY .

MOLECULAR BIOLOGY OF THE CELL, 2001, 12 (12) :4114-4128

[5] Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen [J].

Bhamidipati, A ;

Denic, V ;

Quan, EM ;

Weissman, JS .

MOLECULAR CELL, 2005, 19 (06) :741-751

[6] Role of Cue1p in ubiquitination and degradation at the ER surface [J].

Biederer, T ;

Volkwein, C ;

Sommer, T .

SCIENCE, 1997, 278 (5344) :1806-1809

[7] Role of the ubiquitin-selective CDC48UFD1/NPL4 chaperone (segregase) in ERAD of OLE1 and other substrates [J].

Braun, S ;

Matuschewski, K ;

Rape, M ;

Thoms, S ;

Jentsch, S .

EMBO JOURNAL, 2002, 21 (04) :615-621

[8] Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins [J].

Carvalho, Pedro ;

Goder, Veit ;

Rapoport, Tom A. .

CELL, 2006, 126 (02) :361-373

[9] On the mechanism of sensing unfolded protein in the endoplasmic reticulum [J].

Credle, JJ ;

Finer-Moore, JS ;

Papa, FR ;

Stroud, RM ;

Walter, P .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2005, 102 (52) :18773-18784

[10] Regulation of the cytoplasmic quality control protein degradation pathway by BAG2 [J].

Dai, Q ;

Qian, SB ;

Li, HH ;

McDonough, H ;

Borchers, C ;

Huang, D ;

Takayama, S ;

Younger, JM ;

Ren, HY ;

Cyr, DM ;

Patterson, C .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (46) :38673-38681

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