Phosphoprotein phosphatase inhibitor‐2 is phosphorylated at both serine and threonine residues in mouse diaphragm

FEBS Letters

Lee, Fook-Thean¹  DePaoli-Roach, Anna A.¹ 

[1] Department of Biochemistry, Indiana University School of Medicine, 635 Barnhill Drive, Indianapolis, IN 46223, USA

关键词: ATP-Mg-dependent phosphatase;    Antibody;    Type 1 phosphatase;    Protein phosphorylation;    Mouse diaphragm;    Inhibitor-2;   

DOI  :  10.1016/0014-5793(85)80824-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Phosphoprotein phosphatase inhibitor-2 (i-2) was rapidly isolated from mouse diaphragm extracts by the use of specific antibodies. The i-2 so obtained was associated with ATP-Mg and F _a /GSK-3 dependent phosphatase activity, supporting the idea that i-2 is in fact a component of this form of phosphatase. Inhibitor-2 isolated from diaphragms incubated with [³²P]phosphate contained both phosphoserine (~ 90%) and phosphothreonine (~ 10%). Therefore, i-2 is multiply phosphorylated in mouse diaphragm and the potential exists for control of the ATP-Mg-dependent phosphatase via multiple phosphorylation sites in vivo.

【 授权许可】

Unknown