CHARACTERIZATION OF PROTEIN-KINASE C-MEDIATED PHOSPHORYLATION OF THE SHORT CYTOPLASMIC DOMAIN ISOFORM OF C-CAM

Citation
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
Citations number
28
Categorie Soggetti
Biology,"Cell Biology",Biophysics
Journal title
ISSN journal
00145793
Volume
425
Issue
1
Year of publication
1998
Pages
166 - 170
Database
ISI
SICI code
0014-5793(1998)425:1<166:COPCPO>2.0.ZU;2-J
Abstract
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.