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The endoplasmic reticulum (ER) is a large, dynamic, and multifunctional organelle. ER protein homeostasis is essential for the coordination of its diverse functions and depends on ER-associated protein degradation (ERAD). The latter process selects target proteins in the lumen and membrane of the ER, promotes their ubiquitination, and facilitates their delivery into the cytosol for degradation by the proteasome. Originally characterized for a role in the degradation of misfolded proteins and rate-limiting enzymes of sterol biosynthesis, the many branches of ERAD now appear to control the levels of a wider range of substrates and influence more broadly the organization and functions of the ER, as well as its interactions with adjacent organelles. Here, we discuss recent mechanistic advances in our understanding of ERAD and of its consequences for the regulation of ER functions.

Original publication

DOI

10.15252/embj.2021109845

Type

Journal article

Journal

Embo j

Publication Date

15/03/2022

Volume

41

Keywords

ERAD, endoplasmic reticulum, protein degradation, protein quality control, ubiquitin ligase, Endoplasmic Reticulum, Endoplasmic Reticulum-Associated Degradation, Homeostasis, Proteolysis, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins