基础医学与临床 ›› 2015, Vol. 35 ›› Issue (4): 536-540.

• 短篇综述 • 上一篇    下一篇

PRAS40活性调节与功能的研究进展

朱燕婷,赵迪,史道华   

  1. 福建省妇幼保健院
  • 收稿日期:2014-10-15 修回日期:2014-12-25 出版日期:2015-04-05 发布日期:2015-04-08
  • 通讯作者: 史道华 E-mail:shidh@yeah.net
  • 基金资助:
    福建省自然科学基金;福建省医学创新课题

Research progress in regulation of the activities and functions of PRAS40

  • Received:2014-10-15 Revised:2014-12-25 Online:2015-04-05 Published:2015-04-08

摘要: PRAS40是蛋白激酶B(PKB/ Akt)的作用底物,亦是mTORC1的特异性结合蛋白,有多个位点可发生磷酸化,其中Thr246磷酸化受Akt调控,而Ser183、Ser212及Ser221等磷酸化主要受mTORC1调控。磷酸化修饰的PRAS40可调节与Raptor及14-3-3等蛋白的结合,参与Akt、mTORC1活性的调控。PRAS40具有调控细胞增殖、参与神经损伤保护等作用,在胰岛素抵抗、神经退行性病变及肿瘤中扮演重要角色,有望成为药物作用的新靶点。

关键词: 关键词:PRAS40, 磷酸化修饰, 胰岛素抵抗, 神经退行性病变, 癌症

Abstract: PRAS40, a substrate of protein kinase B (PKB/ Akt), is a specific binding protein of mTORC1. There are several conservative phosphorylation sites in PRAS40 including Thr246 induced by Akt and Ser183, Ser212 and Ser221 regulated by mTORC1. When phosphorylated, PRAS40 interacts with Raptor or 14-3-3 protein and participates in regulating the activity of Akt and mTORC1. PRAS40 also plays an important role in insulin resistance, neurodegenerative disorders and cancer owing to its function in regulating cell growth and neuroprotective effects. As a result, PRAS40 may be a promising drug target.

Key words: KEY WORDS: PRAS40, phosphorylation, insulin resistance, neurodegenerative disorders, cancer

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