SUMO takes control of a ubiquitin-specific protease.
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ABSTRACT:
SUBMITTER: Mohideen F
PROVIDER: S-EPMC2753972 | biostudies-literature | 2008 Jun
REPOSITORIES: biostudies-literature
Publications
SUMO takes control of a ubiquitin-specific protease.
Mohideen Firaz F Lima Christopher D CD
Molecular cell 20080601 5
In this issue of Molecular Cell, Meulmeester et al. (2008) identify USP25 as a SUMO2/3-interacting protein and substrate. A USP25 SUMO interaction motif directs SUMO2/3 specificity, and SUMO modification diminishes USP25's ability to bind and degrade polyubiquitin chains. ...[more]
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Project description:USP4 is a member of the ubiquitin-specific protease (USP) family of deubiquitinating enzymes that has a role in spliceosome regulation. Here, we show that the crystal structure of the minimal catalytic domain of USP4 has the conserved USP-like fold with its typical ubiquitin-binding site. A ubiquitin-like (Ubl) domain inserted into the catalytic domain has autoregulatory function. This Ubl domain can bind to the catalytic domain and compete with the ubiquitin substrate, partially inhibiting USP4 activity against different substrates. Interestingly, other USPs, such as USP39, could relieve this inhibition.
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