ERAD and how viruses exploit it

被引:58
作者
Byun, Hyewon
Gou, Yongqiang
Zook, Adam
Lozano, Mary M.
Dudley, Jaquelin P. [1 ,2 ]
机构
[1] Univ Texas Austin, Dept Mol Biosci, Ctr Infect Dis, Austin, TX 78712 USA
[2] Univ Texas Austin, Inst Cellular & Mol Biol, Austin, TX 78712 USA
关键词
ERAD; immune response; retrotranslocation; ubiquitination; proteasomal degradation; retrovirus; herpesvirus; polyomavirus; RETICULUM-ASSOCIATED DEGRADATION; PROTEIN DISULFIDE-ISOMERASE; MAMMALIAN ENDOPLASMIC-RETICULUM; TRANSMEMBRANE CONDUCTANCE REGULATOR; UBIQUITIN LIGASE COMPLEX; SIGNAL PEPTIDE PEPTIDASE; HEPATITIS-B-VIRUS; CLASS-I MOLECULES; QUALITY-CONTROL; CHOLERA-TOXIN;
D O I
10.3389/fmicb.2014.00330
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Endoplasmic reticulum (ER)-associated degradation (ERAD) is a universally important process among eukaryotic cells. ERAD is necessary to preserve cell integrity since the accumulation of defective proteins results in diseases associated with neurological dysfunction, cancer, and infections. This process involves recognition of misfolded or misassembled proteins that have been translated in association with ER membranes. Recognition of ERAD substrates leads to their extraction through the ER membrane (retrotranslocation or dislocation), ubiquitination, and destruction by cytosolic proteasomes. This review focuses on ERAD and its components as well as how viruses use this process to promote their replication and to avoid the immune response.
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页数:16
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