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 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.
The ubiquitin‐specific protease Usp4 contains an autoinhibitory Ubl domain in its catalytic domain. Inhibition can be relieved by interaction with a non‐active USP, such as USP39.
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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Ubiquitin‐specific protease 4 is inhibited by its ubiquitin‐like domain ; volume:12 ; number:4 ; year:2011 ; pages:365-372 ; extent:8
EMBO reports / European Molecular Biology Organization ; 12, Heft 4 (2011), 365-372 (gesamt 8)
- Creator
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Luna‐Vargas, Mark P. A.
Faesen, Alex C.
van Dijk, Willem J.
Rape, Michael
Fish, Alexander
Sixma, Titia K.
- DOI
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10.1038/embor.2011.33
- URN
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urn:nbn:de:101:1-2023032106442499688397
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 11:04 AM CEST
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Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Luna‐Vargas, Mark P. A.
- Faesen, Alex C.
- van Dijk, Willem J.
- Rape, Michael
- Fish, Alexander
- Sixma, Titia K.
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