The BioGRID | PUBLICATION VIEW

	Biochem. Biophys. Res. Commun. Jun (1998); 247(3):569-75
Kell and Kx, two disulfide-linked proteins of the human erythrocyte membrane are phosphorylated in vivo.
Carbonnet F, Hattab C, Cartron JP, Bertrand O
INSERM U76, Institut National de la Transfusion Sanguine, Paris, France.
Abstract: Kell and Kx are two quantitatively minor proteins from the human erythrocyte membrane which carry blood groups antigens and are thought to be a metalloprotease and a membrane transporter, respectively. In the red cell membrane, these proteins form a complex stabilized by disulfide bond(s). Phosphorylation status of these proteins was studied, in the presence or absence of effectors of several kinases, either on intact cells incubated with [32P]-orthophosphate or on ghosts incubated with [gamma-32P]ATP. Purification of Kell-Kx complex, by immunochromatography on an immobilized human monoclonal antibody of Kell blood group specificity allowed to establish that (i) neither protein is phosphorylated on tyrosine; (ii) the Kell protein is a putative substrate for Casein Kinase II (CKII) and Casein Kinase I (CKI) but not for protein kinase C (PKC), whereas Kx protein is phosphorylated by CKII and PKC but not by CKI; (iii) Protein Kinase A neither phosphorylates the Kell nor the Kx proteins.
[PUBMED: 9647734]