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ERAD ubiquitin ligases
Author(s) -
Mehnert Martin,
Sommer Thomas,
Jarosch Ernst
Publication year - 2010
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.201000046
Subject(s) - endoplasmic reticulum associated protein degradation , endoplasmic reticulum , microbiology and biotechnology , ubiquitin , secretory pathway , biology , proteasome , cytoplasm , ubiquitin protein ligases , ubiquitin ligase , protein folding , unfolded protein response , biochemistry , golgi apparatus , gene
In eukaryotic cells terminally misfolded proteins of the secretory pathway are retarded in the endoplasmic reticulum (ER) and subsequently degraded in a ubiquitin‐proteasome‐dependent manner. This highly conserved process termed ER‐associated protein degradation (ERAD) ensures homeostasis in the secretory pathway by disposing faulty polypeptides and preventing their deleterious accumulation and eventual aggregation in the cell. The focus of this paper is the functional description of membrane‐bound ubiquitin ligases, which are involved in all critical steps of ERAD. In the end we want to speculate on how the modular architecture of these entities ensures the specificity of substrate selection and possibly accomplishes the transport of misfolded polypeptides from the ER into the cytoplasm.