UnpEL/Usp4 is ubiquitinated by Ro52 and deubiquitinated by itself
UnpEL/Usp4 is ubiquitinated by Ro52 and deubiquitinated by itself
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DOI：
10.1016/j.bbrc.2006.01.144
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发表时间：
2006-03-31
影响因子：
3.1
通讯作者：
Kamitani, T
中科院分区：
文献类型：
--
作者：
Wada, K;Kamitani, T
自身抗原Ro 52是一种E3泛素连接酶，可以将自身泛素化（自我泛素化）。最近，我们发现UnpEL/Usp 4是一种异肽酶，可以从自身泛素化的Ro 52中解偶联泛素。在这里，我们表明UnpEL是由Ro 52在体外与UbcH 5 B合作泛素化。我们还表明，UnpEL是泛素化的Ro 52在HEK 293 T细胞。有趣的是，催化失活的UnpEL突变体在HEK 293 T细胞中被Ro 52强烈泛素化。这些结果表明，野生型UnpEL是由Ro 52泛素化和自身去泛素化（自我去泛素化），而突变体UnpEL是由Ro 52泛素化，但本身不去泛素化。总之，Ro 52和UnpEL通过泛素化和去泛素化相互反式调节。(c)2006年爱思唯尔公司All rights reserved.
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. (c) 2006 Elsevier Inc. All rights reserved.