The phosphorylation of lipid transfer protein CaMBP10

Calmodulin-binding protein-10 (cambp10) was isolated previously from chinese cabbage and identified as a member of the lipid transfer protein family. in this study,we found that cambp10 was phosphorylated in a calcium( ca 2+)-dependent manner,and the phosphorylation was inhibited by calmodulin (cam) antagonists. in-gel kinase assay revealed that the phosphorylation of cambp10 was catalyzed by a 45 kda protein kinase,which underwent autophosphorylation in the presence of ca2+. immunoblotting assay further identified this kinase as a calcium-dependent protein kinase (cdpk). in addition,the phosphorylation site was mapped to the c-terminal region of cambp10,where the cambinding domain resides. these results provide novel insights into the molecular mechanisms that regulate cambp10 functions. © 2011 bentham science publishers ltd.