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Orchestration of secretory protein folding by ER chaperones
Journal article   Open access   Peer reviewed

Orchestration of secretory protein folding by ER chaperones

Tali Gidalevitz, Fred Stevens and Yair Argon
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, v 1833(11), pp 2410-2424
01 Nov 2013
PMID: 23507200
url
https://doi.org/10.1016/j.bbamcr.2013.03.007View
Published, Version of Record (VoR)Open Access (Publisher-Specific) Open

Abstract

Biochemistry & Molecular Biology Cell Biology Life Sciences & Biomedicine Science & Technology
The endoplasmic reticulum is a major compartment of protein biogenesis in the cell, dedicated to production of secretory, membrane and organelle proteins. The secretome has distinct structural and post-translational characteristics, since folding in the ER occurs in an environment that is distinct in terms of its ionic composition, dynamics and requirements for quality control. The folding machinery in the ER therefore includes chaperones and folding enzymes that introduce, monitor and react to disulfide bonds, glycans, and fluctuations of luminal calcium. We describe the major chaperone networks in the lumen and discuss how they have distinct modes of operation that enable cells to accomplish highly efficient production of the secretome. This article is part of a Special Issue entitled: Functional and structural diversity of endoplasmic reticulum. (c) 2013 Elsevier B.V. All rights reserved.

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Collaboration types
Domestic collaboration
Web of Science research areas
Biochemistry & Molecular Biology
Cell Biology
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