| Mechanisms for quality control of misfolded transmembrane proteins. | |
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MedLine Citation:
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PMID: 22100602 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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To prevent the accumulation of misfolded and aggregated proteins, the cell has developed a complex network of cellular quality control (QC) systems to recognize misfolded proteins and facilitate their refolding or degradation. The cell faces numerous obstacles when performing quality control on transmembrane proteins. Transmembrane proteins have domains on both sides of a membrane and QC systems in distinct compartments must coordinate to monitor the folding status of the protein. Additionally, transmembrane domains can have very complex organization and QC systems must be able to monitor the assembly of transmembrane domains in the membrane. In this review, we will discuss the QC systems involved in repair and degradation of misfolded transmembrane proteins. Also, we will elaborate on the factors that recognize folding defects of transmembrane domains and what happens when misfolded transmembrane proteins escape QC and aggregate. This article is part of a Special Issue entitled: Protein Folding in Membranes. |
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Authors:
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Scott A Houck; Douglas M Cyr |
Publication Detail:
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Type: Journal Article; Review Date: 2011-11-11 |
Journal Detail:
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Title: Biochimica et biophysica acta Volume: 1818 ISSN: 0006-3002 ISO Abbreviation: Biochim. Biophys. Acta Publication Date: 2012 Apr |
Date Detail:
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Created Date: 2012-02-27 Completed Date: 2013-04-03 Revised Date: 2013-04-03 |
Medline Journal Info:
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Nlm Unique ID: 0217513 Medline TA: Biochim Biophys Acta Country: Netherlands |
Other Details:
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Languages: eng Pagination: 1108-14 Citation Subset: IM |
Copyright Information:
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Copyright © 2011 Elsevier B.V. All rights reserved. |
Affiliation:
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Department of Cell and Developmental Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27514, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Autophagy Humans Membrane Proteins / chemistry*, metabolism* Models, Biological Protein Folding* Protein Structure, Quaternary |
| Grant Support | |
ID/Acronym/Agency:
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R01 GM056981/GM/NIGMS NIH HHS; R01 GM056981-13/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Membrane Proteins |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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