UnpEL/Usp4 is ubiquitinated by Ro52 and deubiquitinated by itself

Biochem Biophys Res Commun. 2006 Mar 31;342(1):253-8. doi: 10.1016/j.bbrc.2006.01.144.

Keiji Wada ¹, Tetsu Kamitani

Affiliations

Affiliation

1 Department of Cardiology, The University of Texas M. D. Anderson Cancer Center, Houston, TX 77030, USA.

PMID: 16472766 DOI: 10.1016/j.bbrc.2006.01.144

Abstract

The autoantigen Ro52 is an E3 ubiquitin ligase that can ubiquitinate itself (self-ubiquitination). Recently, we showed that UnpEL/Usp4 is an isopeptidase that can deconjugate ubiquitin from self-ubiquitinated Ro52. Here, we showed that UnpEL is ubiquitinated by Ro52 in cooperation with UbcH5B in vitro. We also showed that UnpEL is ubiquitinated by Ro52 in HEK293T cells. Interestingly, a catalytically inactive UnpEL mutant was strongly ubiquitinated by Ro52 in HEK293T cells. These results suggest that wild-type UnpEL is ubiquitinated by Ro52 and deubiquitinated by itself (self-deubiquitination), while mutant UnpEL is ubiquitinated by Ro52 but not deubiquitinated by itself. In conclusion, Ro52 and UnpEL transregulate each other by ubiquitination and deubiquitination.

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