M. Edlund et al., CHARACTERIZATION OF PROTEIN-KINASE C-MEDIATED PHOSPHORYLATION OF THE SHORT CYTOPLASMIC DOMAIN ISOFORM OF C-CAM, FEBS letters, 425(1), 1998, pp. 166-170
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 rye have characterized the
PKC-mediated phosphorylation of the short cytoplasmic domain isoform,
C-CAM-S. Phorbol myristyl acetate induced phosphorylation of C-CAM-S i
n transfected CHO cells, Using synthetic peptides and Edman degradatio
n we identified Ser(449) as the PKC-phosphorylated amino acid residue,
Binding experiments with modified peptides indicated that this phosph
orylation decreases the ability of the cytoplasmic domain of C-CAM-S t
o bind calmodulin. (C) 1998 Federation of European Biochemical Societi
es.