%0 Journal Article
%T p38¦Á MAP kinase phosphorylates RCAN1 and regulates its interaction with calcineurin
%A Lei Ma
%A HaiPing Tang
%A Yan Ren
%A HaiTeng Deng
%A JiaWei Wu
%A ZhiXin Wang
%J Science China Life Sciences
%@ 1869-1889
%D 2012
%I 
%R 10.1007/s11427-012-4340-9
%X 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¦Á 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¦Á MAP kinase decreases the binding affinity of RCAN1 for calcineurin. These findings reveal the molecular mechanism by which p38¦Á MAP kinase regulates the function of RCAN1/calcineurin through phosphorylation.
%K p38¦Á MAP kinase
%K RCAN1
%K calcineurin
%K phosphorylation
%U http://link.springer.com/article/10.1007/s11427-012-4340-9