期刊
SCIENCE CHINA-LIFE SCIENCES
卷 55, 期 7, 页码 559-566出版社
SCIENCE PRESS
DOI: 10.1007/s11427-012-4340-9
关键词
p38 alpha MAP kinase; RCAN1; calcineurin; phosphorylation
类别
资金
- Ministry of Science and Technology of China [2011CB910803]
RCAN1, also known as DSCR1, is an endogenous regulator of calcineurin, a serine/threonine protein phosphatase that plays a critical role in many physiological processes. In this report, we demonstrate that p38 alpha MAP kinase can phosphorylate RCAN1 at multiple sites in vitro and show that phospho-RCAN1 is a good protein substrate for calcineurin. In addition, we found that unphosphorylated RCAN1 noncompetitively inhibits calcineurin protein phosphatase activity and that the phosphorylation of RCAN1 by p38 alpha MAP kinase decreases the binding affinity of RCAN1 for calcineurin. These findings reveal the molecular mechanism by which p38 alpha MAP kinase regulates the function of RCAN1/calcineurin through phosphorylation.
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