Ubiquitin-specific protease 4 is inhibited by its ubiquitin-like domain

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 ubiquiti...

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Detalles Bibliográficos
Autores principales: Luna-Vargas, Mark P A, Faesen, Alex C, van Dijk, Willem J, Rape, Michael, Fish, Alexander, Sixma, Titia K
Formato: Texto
Lenguaje:English
Publicado: European Molecular Biology Organization 2011
Materias:
Scientific Reports
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3077250/
https://www.ncbi.nlm.nih.gov/pubmed/21415856
http://dx.doi.org/10.1038/embor.2011.33
Descripción
Sumario: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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