Format

Send to:

Choose Destination
See comment in PubMed Commons below
Traffic. 2012 Jan;13(1):19-24. doi: 10.1111/j.1600-0854.2011.01269.x. Epub 2011 Sep 13.

Ubiquitination of substrates by esterification.

Author information

  • 1Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, MO 63110, USA. xiwang@wustl.edu

Abstract

Post-translational modification by ubiquitination determines intracellular location and fate of numerous proteins, thus impacting a diverse array of physiologic functions. Past dogma has been that ubiquitin was only coupled to substrates by isopeptide bonds to internal lysine residues or less frequently peptide bonds to the N-terminus. Enigmatically, however, several proteins lacking lysines had been reported to retain ubiquitin-dependent fates. Resolution of this paradox was afforded by recent observations that ubiquitination of substrates can also occur on cysteine or serine and threonine residues by thio- or oxy-ester bond formation, respectively (collectively called esterification). Although chemically possible, these bonds were considered too labile to be of physiological relevance. In this review we discuss recent evidence for the ubiquitination of protein substrates by esterification and speculate on its mechanism and its physiological importance.

© 2011 John Wiley & Sons A/S.

PMID:
21883762
[PubMed - indexed for MEDLINE]
PMCID:
PMC3973488
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Blackwell Publishing Icon for PubMed Central
    Loading ...
    Write to the Help Desk