Regulation of Mst1 activity by Akt = Akt에 의한 Mst1 인산화효소의 기능 조절에 대한 연구

Cited 0 time in webofscience Cited 0 time in scopus
  • Hit : 270
  • Download : 0
The Akt family of serine/threonine kinases promotes cell survival in part by phosphorylating and inhibiting death-inducing proteins. Here, I described a novel functional interaction between Akt and mammalian sterile20-like kinase 1 (Mst1), a mitogen-activated protein kinase kinase kinase kinase (MAPKKKK). Akt decreased Mst1 activity in HEK293T cells by phosphorylating a consensus Akt site at Thr 120 of Mst1. Consistently, activation of the phosphoinositide 3-kinase (PI3K)/Akt pathway by EGF inhibited the activity of Mst1 in HEK293T cells. The functional interaction between Akt and Mst1 was also confirmed by Drosophila genetic analysis using gain-of-function and loss-of-function mutants of Hippo, the Drosophila orthologue of Mst1. These results provide the first direct connection between Akt and tumor-suppressor Mst1
Advisors
Chung, Jong-Kyeongresearcher정종경researcher
Description
한국과학기술원 : 생명과학과,
Publisher
한국과학기술원
Issue Date
2006
Identifier
260021/325007  / 020053117
Language
eng
Description

학위논문(석사) - 한국과학기술원 : 생명과학과, 2006.8, [ iv, 47 p. ]

Keywords

Mst1; 발암억제인자

URI
http://hdl.handle.net/10203/28080
Link
http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=260021&flag=dissertation
Appears in Collection
BS-Theses_Master(석사논문)
Files in This Item
There are no files associated with this item.

qr_code

  • mendeley

    citeulike


rss_1.0 rss_2.0 atom_1.0