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Protein Sci. 2014 Apr;23(4):344-53. doi: 10.1002/pro.2415. Epub 2014 Feb 12.

Mechanisms for regulating deubiquitinating enzymes.

Author information

1
Department of Biophysics and Biophysical Chemistry and the Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, Maryland, 21205.

Abstract

Ubiquitination is a reversible post-translational modification that plays a dynamic role in regulating most eukaryotic processes. Deubiquitinating enzymes (DUBs), which hydrolyze the isopeptide or peptide linkages joining ubiquitin to substrate lysines or N-termini, therefore play a key role in ubiquitin signaling. Cells employ multiple mechanisms to regulate DUB activity and thus ensure the appropriate biological response. Recent structural studies have shed light on several different mechanisms by which DUB activity and specificity is regulated.

KEYWORDS:

DUB; UBL; deubiquitinating enzymes; ubiquitin

PMID:
24403057
PMCID:
PMC3970886
DOI:
10.1002/pro.2415
[Indexed for MEDLINE]
Free PMC Article

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