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PLoS Biol. 2011 Mar;9(3):e1001038. doi: 10.1371/journal.pbio.1001038. Epub 2011 Mar 29.

Ubiquitylation in ERAD: reversing to go forward?

Author information

  • 1Laboratory of Protein Dynamics and Signaling, National Cancer Institute, Frederick, Maryland, United States of America. tsaiyien@mail.nih.gov

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 processes are discussed.

Comment on

  • Enzymatic blockade of the ubiquitin-proteasome pathway. [PLoS Biol. 2011]
PMID:
21468305
[PubMed - indexed for MEDLINE]
PMCID:
PMC3066135
Free PMC Article

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