4.6 Review

Ubiquitin ligases, critical mediators of endoplasmic reticulum-associated degradation

Journal

SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY
Volume 18, Issue 6, Pages 770-779

Publisher

ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.semcdb.2007.09.002

Keywords

endoplasmic reticulum-associated degradation; ubiquitin protein ligase (E3); proteasome; Saccharomyces cerevisiae

Funding

  1. Intramural NIH HHS [Z01 BC009392-13] Funding Source: Medline

Ask authors/readers for more resources

Endoplasmic reticulum-associated degradation (ERAD) represents the primary means of quality control within the secretory pathway. Critical to this process are ubiquitin protein ligases (E3s) which, together with ubiquitin conjugating enzymes (E2s), mediate the ubiquitylation of proteins targeted for degradation from the ER. In this chapter we review our knowledge of both Saccharomyces cerevisiae and mammalian ERAD ubiquitin ligases. We focus on recent insights into these E3s, their associated proteins and potential mechanisms of action. Published by Elsevier Ltd.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.6
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available