和田 圭司
   Department   Other, Other
   Position  
Article types Original article
Language English
Peer review Peer reviewed
Title UnpEL/Usp4 is ubiquitinated by Ro52 and deubiquitinated by itself.
Journal Formal name:Biochemical and biophysical research communications
Abbreviation:Biochem Biophys Res Commun
ISSN code:0006291X/0006291X
Domestic / ForeginForegin
Volume, Issue, Page 342(1),pp.253-8
Author and coauthor Wada Keiji, Kamitani Tetsu
Publication date 2006/03
Summary 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.
DOI 10.1016/j.bbrc.2006.01.144
PMID 16472766