TTC3 泛素化终止 Akt 的激活。
TTC3 ubiquitination terminates Akt-ivation.
机构信息
Department of Pathology, Beth Israel Deaconess Medical Center, Harvard Medical School, 330 Brookline Avenue, Boston, MA 02215, USA.
出版信息
Dev Cell. 2009 Dec;17(6):752-4. doi: 10.1016/j.devcel.2009.12.003.
PMID:20059946
Abstract
In this issue of Developmental Cell, Suizu et al. (2009) describe a new mechanism for posttranslational regulation of the Akt serine/threonine protein kinase involving ubiquitination. They show that the E3 ubiquitin ligase TTC3 modifies phosphorylated and activated Akt and thereby promotes its degradation by the proteasome in the nucleus.
摘要
在本期《发育细胞》中，Suizu 等人（2009 年）描述了 Akt 丝氨酸/苏氨酸蛋白激酶的一种新的翻译后调控机制，涉及泛素化。他们表明，E3 泛素连接酶 TTC3 修饰磷酸化和激活的 Akt，从而促进其在核内被蛋白酶体降解。
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