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Mechanisms for regulating deubiquitinating enzymes.


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.

SUBMITTER: Wolberger C 

PROVIDER: S-EPMC3970886 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature

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Mechanisms for regulating deubiquitinating enzymes.

Wolberger Cynthia C  

Protein science : a publication of the Protein Society 20140212 4


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 mechanism  ...[more]

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