Dissociation of the ligand and dephosphorylation of the platelet‐derived growth factor receptor

FEBS Letters

Alberghina, L.¹  Zippel, R.¹  Brambillo, R.¹  Sturani, E.¹  Morello, L.¹ 

[1] Dipartimento di Fisiologia e Biochimica Generali, Universita`di Milano, Via Celoria 26, 20133 Milano, Italy

关键词: Platelet-derived growth factor;    Platelet-derived growth factor receptor;    Phosphotyrosine;    Suramin;    Protein kinase;    Phosphatase;   

DOI  :  10.1016/0014-5793(88)80463-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The ligand-induced phosphorylation of the platelet-derived growth factor (PDGF) receptor was followed at 37°C by a rapid dephosphorylation which was roughly parallel to the down regulation of the ¹²⁵I-PDGF binding sites. At 4°C, when the ligand-receptor complexes remain associated with the cell surface, the phosphorylated form of the receptor was more stable. However if the ligand was dissociated from the receptor by means of a mild acid wash or a treatment with suramin, the dephosphorylation of the receptor also occurred at a low temperature. These data suggest that, due to the dissociation of the ligand, the kinase activity of the receptor is switched off so that the phosphotyrosine-containing receptors remain exposed to the action of phosphatases that rapidly dephosphorylate them.

【 授权许可】

Unknown