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Serine phosphorylation of the ligand-activated b-platelet-derived growth factor receptor by casein kinase i-g2 inhibits the receptor’s autophosphorylating activity*.
| Content Provider | CiteSeerX |
|---|---|
| Author | Bioukar, El Bachir Marricco, Nadia Cardillo Zuo, Dongmei Larose, Louise |
| Abstract | Platelet-derived growth factor (PDGF) receptors (PDGFRs) are membrane protein-tyrosine kinases that, upon activation, become tyrosine-phosphorylated and associate with numerous SH2 domain-containing mole-cules involved in mediating signal transduction. In Rat-2 fibroblasts, we have characterized the phospho-rylation of the b-PDGFR following its activation by PDGF. In contrast to tyrosine phosphorylation, which was transient and returned to near basal levels by 30 min, PDGF-stimulated Ser/Thr phosphorylation of the b-PDGFR was increased by 5 min and remained elevated after 30 min. In vivo, after 5 min of PDGF stimulation, serine phosphorylation of the b-PDGFR was greatly re-duced by CKI-7, a specific inhibitor of casein kinase I (CKI). In vitro, recombinant CKI-g2 phosphorylated the |
| File Format | |
| Access Restriction | Open |
| Subject Keyword | Serine Phosphorylation Ligand-activated B-platelet-derived Growth Factor Receptor Casein Kinase I-g2 Autophosphorylating Activity Pdgf Stimulation Numerous Sh2 Domain-containing Mole-cules Recombinant Cki-g2 Membrane Protein-tyrosine Kinase Casein Kinase Signal Transduction Basal Level Platelet-derived Growth Factor Rat-2 Fibroblast Specific Inhibitor Pdgf-stimulated Ser Thr Phosphorylation |
| Content Type | Text |