p38α MAP kinase phosphorylates RCAN1 and regulates its interaction with calcineurin

查看全文 作　　者：MA [1]Lei;TANG [2]HaiPing;REN [3]Yan;DENG [2]HaiTeng;WU [2]JiaWei;WANG [1,2]ZhiXin

机构地区：[1]National Laboratory of Biomacromolecules, Institute of Biophysics and Graduate University, Chinese Academy of Sciences, Beijing 100101, China;[2]School of Life Sciences, Tsinghua University, Beijing 100084, China;[3]Department of Biochemistry and Molecular Biology, Beijing Normal University, Beijing 100875, China

出　　处：《Science China(Life Sciences)》索引2012年第55卷第7期,共8页

基　　金：supported in part by Ministry of Science and Technology of China (Grant 2011CB910803) 摘　　要：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 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 MAP kinase decreases the binding affinity of RCAN1 for calcineurin.These findings reveal the molecular mechanism by which p38 MAP kinase regulates the function of RCAN1/calcineurin through phosphorylation. 关键词：钙调神经磷酸酶 MAP激酶磷酸化蛋白磷酸酶非竞争性抑制结合亲和力生理过程分子机制

相关文献

参考文献（38）
引证文献（2）
耦合文献（0）

参考文献(38)

引证文献(2)

互联网出版许可证新出网证(渝)字10号全国400电话 - 免长途话费

p38α MAP kinase phosphorylates RCAN1 and regulates its interaction with calcineurin

参考文献(38)

引证文献(2)

用户提示