Phosphoprotein phosphatase inhibitor‐2 is phosphorylated at both serine and threonine residues in mouse diaphragm
- 22 April 1985
- journal article
- Published by Wiley in FEBS Letters
- Vol. 183 (2), 430-432
- https://doi.org/10.1016/0014-5793(85)80824-3
Abstract
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 (~ 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 vivoKeywords
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