Catalase Is Regulated by Ubiquitination and Proteosomal Degradation. Role of the c-Abl and Arg Tyrosine Kinases
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- 作者：Cheng Cao ; Yumei Leng ; Xuan Liu ; Yanping Yi ; Ping Li ; and Donald Kufe
- 刊名：Biochemistry
- 出版年：2003
- 出版时间：September 9, 2003
- 年：2003
- 卷：42
- 期：35
- 页码：10348 - 10353
- 全文大小：205K
- 年卷期：v.42,no.35(September 9, 2003)
- ISSN：1520-4995
文摘
Catalase is a major effector in the defense of aerobic cells against oxidative stress. Recentstudies have shown that catalase activity is stimulated by the c-Abl and Arg tyrosine kinases. Little,however, is otherwise known about the mechanisms responsible for catalase regulation. The present workdemonstrates that mouse cells deficient in both c-Abl and Arg exhibit increased catalase stability. Theresults also show that catalase is subject to ubiquitination and degradation by the 26S proteosome.Significantly, ubiquitination of catalase is dependent on c-Abl- and Arg-mediated phosphorylation ofcatalase on both Y231 and Y386. In concert with these results, human 293 cells expressing catalase mutatedat Y231 and Y386 exhibit attenuated levels of reactive oxygen species when exposed to hydrogen peroxide.These findings indicate that, in addition to stimulating catalase activity, c-Abl and Arg promote catalasedegradation in the oxidative stress response.