Coping with stress: cellular relaxation techniques.

Full Abstract

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.

Author information

Author/s: Hirsch, Christian (C); Gauss, Robert (R); Sommer, Thomas (T);

Affiliation: Max-Delbrück Center for Molecular Medicine, Robert-Rössle-Strasse 10, 13125 Berlin, Germany.

Journal and publication information

Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Review

Journal: Trends in cell biology (Trends Cell Biol), published in England. (Language: eng)

Reference: 2006-Dec; vol 16 (issue 12) : pp 657-63

Dates: Created 2006/12/01; Completed 2007/01/08; Revised 2008/08/15;

PMID: 17084628, status: MEDLINE (last retrieval date: 2/18/2009, IMS Date: 18 Feb 2009 00:00:00)

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

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MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Membrane Proteins - metabolism
Oxidative Stress - physiology
Proteasome Endopeptidase Complex - metabolism
Protein Folding
Protein-Serine-Threonine Kinases - metabolism
Proteins - metabolism
Signal Transduction - physiology
Ubiquitin-Protein Ligases - metabolism

Associated Chemicals: Heat-Shock Proteins (0) ; Membrane Proteins (0) ; Proteins (0) ; ERN2 protein, human (EC 2.7.1.-) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; Endoribonucleases (EC 3.1.-) ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; STUB1 protein, human (EC 6.3.2.19) ; Ubiquitin-Protein Ligases (EC 6.3.2.19)

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