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 / Foregin | Foregin |
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 |