Dephosphorylation of the deinhibitor protein by the PCSH protein phosphatase

FEBS Letters

Goris, Jozef¹  Merlevede, Wilfried¹  Waelkens, Etienne¹ 

[1] Afdeling Biochemie, Faculteit Geneeskunde, Campus Gasthuisberg, Katholieke Universiteit te Leuven, B-3000 Leuven, Belgium

关键词: Deinhibitor protein (activation);    ATP;    Mg-dependent phosphatase;    Inhibitor-1 Modulator protein (inhibitor-2);    Polycation-stimulated phosphatase;   

DOI  :  10.1016/0014-5793(85)80384-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The deinhibitor protein, responsible for the decreased sensitivity of the ATP, Mg-dependent protein phosphatase to inhibitor-1 and the modulator protein, is inactivated by cyclic AMP-dependent protein kinase and reactivated by dephosphorylation. The specificity of this reaction was tested with the ATP, Mg-dependent phosphatase in its activated or spontaneously active form, four different forms of polycation-stimulated phosphatases (PCS_H, PCS_M, PCS_L and PCS_C) and calcineurin. Only the high -M _r, polycation-stimulated protein phosphatase (PCS_H), but not its catalytic subunit (PCS_C), shows a high degree of specificity for the deinhibitor protein. Deinhibitor phosphatase activity of PCS_H is affected neither by polycations nor by Mn ions.

【 授权许可】

Unknown