The Phosphorylation of Lipid Transfer Protein CaMBP10

被引:6
作者
Li, Cuifeng [1 ]
Xie, Wanqin [1 ]
Wang, Liqiang [1 ]
Zhao, Yulong [1 ]
机构
[1] Nankai Univ, Dept Biochem & Mol Biol, Tianjin 300071, Peoples R China
基金
中国国家自然科学基金;
关键词
Calcium-dependent protein kinase; calmodulin-binding protein-10; calmodulin; lipid transfer protein; phosphorylation; CALMODULIN-BINDING PROTEIN; IDENTIFICATION;
D O I
10.2174/092986611794328681
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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(Ca2+)-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 CaM-binding domain resides. These results provide novel insights into the molecular mechanisms that regulate CaMBP10 functions.
引用
收藏
页码:17 / 22
页数:6
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