Characterization of protein kinase C-mediated phosphorylation of the short cytoplasmic domain isoform of C-CAM.
FEBS Lett
; 425(1): 166-70, 1998 Mar 20.
Article
en En
| MEDLINE
| ID: mdl-9541029
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 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.
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Banco de datos:
MEDLINE
Asunto principal:
Proteína Quinasa C
/
Moléculas de Adhesión Celular
/
Adenosina Trifosfatasas
Límite:
Animals
Idioma:
En
Año:
1998
Tipo del documento:
Article