Characterization of protein kinase C‐mediated phosphorylation of the short cytoplasmic domain isoform of C‐CAM

FEBS Letters

Öbrink, Björn²  Edlund, Magnus²  Toomik, Reet¹  Wikström, Kristina²  Ek, Pia¹ 

[1] Department of Medical and Physiological Chemistry, University of Uppsala, S-751 23 Uppsala, Sweden;Department of Cell and Molecular Biology, Medical Nobel Institute, Karolinska Institute, S-171 77 Stockholm, Sweden

关键词: Calmodulin;    Cell-cell adhesion molecule;    Phosphorylation;    PKC;    C-CAM;    cell-cell adhesion molecule;    PMA;    phorbol myristyl acetate;    PKC;    protein kinase C;   

DOI  :  10.1016/S0014-5793(98)00222-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

C-CAM is a ubiquitously expressed cell adhesion molecule belonging to the carcinoembryonic antigen family. Two co-expressed isoforms, C-CAM-L and C-CAM-S, are known, having different cytoplasmic domains both of which can be phosphorylated in vivo. Here we have characterized the PKC-mediated phosphorylation of the short cytoplasmic domain isoform, C-CAM-S. Phorbol myristyl acetate induced phosphorylation of C-CAM-S in transfected CHO cells. Using synthetic peptides and Edman degradation we identified Ser⁴⁴⁹ as the PKC-phosphorylated amino acid residue. Binding experiments with modified peptides indicated that this phosphorylation decreases the ability of the cytoplasmic domain of C-CAM-S to bind calmodulin.

【 授权许可】

Unknown