Journal article
Orchestration of secretory protein folding by ER chaperones
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, v 1833(11), pp 2410-2424
01 Nov 2013
PMID: 23507200
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
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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Details
- Title
- Orchestration of secretory protein folding by ER chaperones
- Creators
- Tali Gidalevitz - Drexel UniversityFred Stevens - Argonne National LaboratoryYair Argon - Children's Hospital of Philadelphia
- Publication Details
- BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, v 1833(11), pp 2410-2424
- Publisher
- Elsevier
- Number of pages
- 15
- Grant note
- T32GM007748 / NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Institute of General Medical Sciences (NIGMS) R01AG018001 / NATIONAL INSTITUTE ON AGING; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Institute on Aging (NIA) AG18001; GM07748 / NIH; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biology
- Web of Science ID
- WOS:000323400000004
- Scopus ID
- 2-s2.0-84880633059
- Other Identifier
- 991019167814604721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology
- Cell Biology