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

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 FA/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 (approximately 90%) and phosphothreonine (approximately 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.