FEBS Letters | |
Characterization of protein kinase C‐mediated phosphorylation of the short cytoplasmic domain isoform of C‐CAM | |
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
【 预 览 】
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RO201912020305718ZK.pdf | 160KB | download |