Involvement of the Src kinase Lyn in phospholipase C-gamma 2 phosphorylation and phosphatidylinositol 3-kinase activation in Epo signalling.
Fiche publication
Date publication
janvier 2003
Auteurs
Membres identifiés du Cancéropôle Est :
Pr DEVARENNE-CHARPENTIER Emmanuelle
Tous les auteurs :
Boudot C, Dasse E, Lambert E, Kadri Z, Mayeux P, Chretien S, Haye B, Billat C, Petitfrere E
Lien Pubmed
Résumé
We examined the role of the Src kinase Lyn in phospholipase C-gamma 2 (PLC-gamma 2) and phosphatidylinositol (PI) 3-kinase activation in erythropoietin (Epo)-stimulated FDC-P1 cells transfected with a wild type (WT) Epo-receptor (Epo-R). We showed that two inhibitors of Src kinases, PP1 and PP2, abolish both PLC-gamma 2 tyrosine phosphorylation and PI 3-kinase activity in WT Epo-R FDC-P1 cells. We also demonstrated that Epo-phosphorylated Lyn is associated with tyrosine phosphorylated PLC-gamma 2 and PI 3-kinase in WT Epo-R FDC-P1-stimulated cells. Moreover Epo-activated Lyn phosphorylates in vitro PLC-gamma 2 immunoprecipitated from unstimulated cells. Our results suggest that the Src kinase Lyn is involved in PLC-gamma 2 phosphorylation and PI 3-kinase activation induced by Epo.
Référence
Biochem Biophys Res Commun. 2003 Jan 10;300(2):437-42.