Publication Date:
2009-03-28
Description:
As proteins travel through the endoplasmic reticulum (ER), a quality-control system retains newly synthesized polypeptides and supports their maturation. Only properly folded proteins are released to their designated destinations. Proteins that cannot mature are left to accumulate, impairing the function of the ER. To maintain homeostasis, the protein-quality-control system singles out aberrant polypeptides and delivers them to the cytosol, where they are destroyed by the proteasome. The importance of this pathway is evident from the growing list of pathologies associated with quality-control defects in the ER.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hirsch, Christian -- Gauss, Robert -- Horn, Sabine C -- Neuber, Oliver -- Sommer, Thomas -- England -- Nature. 2009 Mar 26;458(7237):453-60. doi: 10.1038/nature07962.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Delbruck Center for Molecular Medicine, Robert-Rossle-Strasse 10, 13125 Berlin, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19325625" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
Endoplasmic Reticulum/chemistry/*metabolism
;
Homeostasis
;
Humans
;
Intracellular Membranes/metabolism
;
Proteasome Endopeptidase Complex/metabolism
;
Protein Folding
;
Protein Processing, Post-Translational
;
Proteins/*chemistry/*metabolism
;
*Ubiquitination
Print ISSN:
0028-0836
Electronic ISSN:
1476-4687
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
,
Natural Sciences in General
,
Physics
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