H2N2V1, Main, Exploration, bibRecord, 000845

Protein Folding in the Endoplasmic Reticulum

Identifieur interne : 000845 ( Main/Exploration ); précédent : 000844; suivant : 000846

Protein Folding in the Endoplasmic Reticulum

Auteurs : Ineke Braakman [Pays-Bas] ; Daniel N. Hebert [États-Unis]

Source :

Cold Spring Harbor Perspectives in Biology [ 1943-0264 ] ; 2013.

RBID : PMC:3632058

Abstract

In this article, we will cover the folding of proteins in the lumen of the endoplasmic reticulum (ER), including the role of three types of covalent modifications: signal peptide removal, N-linked glycosylation, and disulfide bond formation, as well as the function and importance of resident ER folding factors. These folding factors consist of classical chaperones and their cochaperones, the carbohydrate-binding chaperones, and the folding catalysts of the PDI and proline cis–trans isomerase families. We will conclude with the perspective of the folding protein: a comparison of characteristics and folding and exit rates for proteins that travel through the ER as clients of the ER machinery.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3632058

DOI: 10.1101/cshperspect.a013201
PubMed: 23637286
PubMed Central: 3632058

Affiliations:

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Protein Folding in the Endoplasmic Reticulum

Protein Folding in the Endoplasmic Reticulum

Source :

Abstract

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