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Interaction with Keap1 does not lead to ubiquitination and degradation of prothymosin alphaстатья
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
- Авторы: Melnikov S.V., Evstafieva A.G., Vartapetian A.B.
- Журнал: Molecular Biology
- Том: 41
- Номер: 5
- Год издания: 2007
- Издательство: Maik Nauka/Interperiodica Publishing
- Местоположение издательства: Russian Federation
- Первая страница: 790
- Последняя страница: 796
- DOI: 10.1134/S0026893307050123
- Аннотация: Prothymosin alpha (ProT alpha) is highly conserved among vertebrates and has many biological functions, including an enforcement of cell antioxidant defense. This function is due to ProT alpha interaction with Keap1, a repressor of the Nrf2 transcription factor, activating the expression of several antioxidant protein genes. Keap1 exports Nrf2 from the cell nucleus into the cytoplasm and, acting as an adaptor protein for ubiquitin ligase, facilitates ubiquitination of Nrf2 and its subsequent degradation by the 26S proteasome. ProT alpha and Nrf2 compete for Keap1 binding. ProT alpha is capable of displacing Nrf2 from its complex with Keap1, thereby increasing the expression of the Nrf2 target genes. It was found that ProT alpha remained stable upon its interaction with Keap1. In contrast to Nrf2, ProT alpha escaped Keap1-dependent ubiquitination, proteasomal degradation, and export from the nucleus. Moreover, ProT alpha ubiquitination was not detected even when Keap1 and ubiquitin were overproduced. Hence, activation of Nrf2-dependent transcription by ProT alpha was assumed to result from the increase in free Nrf2 rather than from an increase in total Nrf2.
- Добавил в систему: Вартапетян Андрей Борисович