期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
卷 1818, 期 4, 页码 1108-1114出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2011.11.007
关键词
Transmembrane protein; Quality control; Autophagy; Membrane chaperone; Protein folding
资金
- NIGMS NIH HHS [R01 GM056981-13, R01 GM056981] Funding Source: Medline
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. (C) 2011 Elsevier B.V. All rights reserved.
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