期刊
BIOCHEMICAL JOURNAL
卷 449, 期 -, 页码 741-749出版社
PORTLAND PRESS LTD
DOI: 10.1042/BJ20121201
关键词
AMP-activated protein kinase (AMPK); N-myristoylation; protein phosphatase 2C (PP2C); metal-dependent protein phosphatase 1A (PPM1A); metal-dependent protein phosphatase 1B (PPM1B)
资金
- Ministry of Education, Culture, Sports, Science and Technology of Japan
- Grants-in-Aid for Scientific Research [22590261, 23249085, 25460353, 22590280, 24659907, 24590339] Funding Source: KAKEN
PPM [metal-dependent protein phosphatase, formerly called PP2C (protein phosphatase 2C)] family members play essential roles in regulating a variety of signalling pathways. While searching for protein phosphatase(s) that act on AMPK (AMP-activated protein kinase), we found that PPM1A and PPM1B are N-myristoylated and that this modification is essential for their ability to dephosphorylate the alpha subunit of AMPK (AMPK alpha) in cells. N-Myristoylation was also required for two other functions of PPM1A and PPM1B in cells. Although a non-myristoylated mutation (G2A) of PPM1A and PPM1B prevented membrane association, this relocalization did not likely cause the decreased activity towards AMPK alpha. In in vitro experiments, the G2A mutants exhibited reduced activities towards AMPK alpha, but much higher specific activity against an artificial substrate, PNPP (p-nitrophenyl phosphate), compared with the wild-type counterparts. Taken together, the results of the present study suggest that N-myristoylation of PPM1A and PPM1B plays a key role in recognition of their physiological substrates in cells.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据