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Semin Cell Dev Biol. 2007 Dec;18(6):751-61. Epub 2007 Sep 8.

The activities and function of molecular chaperones in the endoplasmic reticulum.

Author information

1
Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, United States. teb20@pitt.edu

Abstract

Most proteins in the secretory pathway are translated, folded, and subjected to quality control at the endoplasmic reticulum (ER). These processes must be flexible enough to process diverse protein conformations, yet specific enough to recognize when a protein should be degraded. Molecular chaperones are responsible for this decision making process. ER associated chaperones assist in polypeptide translocation, protein folding, and ER associated degradation (ERAD). Nevertheless, we are only beginning to understand how chaperones function, how they are recruited to specific substrates and assist in folding/degradation, and how unique chaperone classes make quality control "decisions".

PMID:
17964199
PMCID:
PMC2175536
DOI:
10.1016/j.semcdb.2007.09.001
[Indexed for MEDLINE]
Free PMC Article

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