Ubiquitin-specific protease 4 is inhibited by its ubiquitin-like domain |
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| Authors: | Luna-Vargas Mark P A Faesen Alex C van Dijk Willem J Rape Michael Fish Alexander Sixma Titia K |
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| Institution: | 1Division of Biochemistry and Center for Biomedical Genetics, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands;2Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 94720, USA |
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| Abstract: | 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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| Keywords: | regulation structure Ubl USP4 |
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