Reconstitution of a Mg‐ATP‐dependent protein phosphatase and its activation through a phosphorylation mechanism

FEBS Letters

Resink, Therese J.¹  Hemmings, Brian A.¹  Cohen, Philip¹ 

[1] Department of Biochemistry, Medical Sciences Institute, University of Dundee, Dundee, DD1 4HN, Scotland

关键词: Protein phosphatase-1;    Glycogen synthase kinase;    Inhibitor-2;    Phosphorylase;    Thiophosphorylation;   

DOI  :  10.1016/0014-5793(82)80760-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A Mg-ATP-dependent protein phosphatase has been reconstituted from the catalytic subunit of protein phosphatase-1 and inhibitor-2, and consists of a 1:1 complex between these proteins. Activation of this enzyme by glycogen synthase kinase-3 and Mg-ATP results from the phosphorylation of inhibitor-2 on a threonine residue(s) and is accompanied by the dissociation of the complex. The results prove that protein phosphatase-1 and the Mg-ATP-dependent protein phosphatase contain the same catalytic subunit, and that they are interconvertible forms of the same enzyme.

【 授权许可】

Unknown