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- Title
Ubiquitylation in ERAD: Reversing to Go Forward?
- Authors
Yien Che Tsai; Weissman, Allan M.
- Abstract
Proteins are co-translationally inserted into the endoplasmic reticulum (ER) where they undergo maturation. Homeostasis in the ER requires a highly sensitive and selective means of quality control. This occurs through ER-associated degradation (ERAD). This complex ubiquitin-proteasome-mediated process involves ubiquitin conjugating enzymes (E2) and ubiquitin ligases (E3), lumenal and cytosolic chaperones, and other proteins, including the AAA ATPase p97 (VCP; Cdc48 in yeast). Probing of processes involving proteasomal degradation has generally depended on proteasome inhibitors or knockdown of specific E2s or E3s. In this issue of PLoS Biology, Ernst et al. demonstrate the utility of expressing the catalytic domain of a viral deubiquitylating enzyme to probe the ubiquitin system. Convincing evidence is provided that deubiquitylation is integral to dislocation of ERAD substrates from the ER membrane. The implications of this work for understanding ERAD and the potential of expressing deubiquitylating enzyme domains for studying ubiquitin-mediated processesare discussed.
- Publication
PLoS Biology, 2011, Vol 9, Issue 3, p1
- ISSN
1544-9173
- Publication type
Academic Journal
- DOI
10.1371/journal.pbio.1001038