p-IPP-1 Antibody (Ser 67): sc-14268

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Protein phosphatase inhibitor-1 (also designated inhibitor of protein phospha-tase 1, IPP-1 and I-1) plays a role in regulating the phosphorylation of other proteins, and is itself phosphorylated by a cyclic AMP-dependent protein kinase at Threonine 35. In addition, the proline-directed kinases Cdk1, Cdk5, and mitogen-activated protein kinase (MAPK) mediate in vitro phosphorylation of IPP-1 at the phylogenetically conserved position Serine 67. In striatal tissues, glutamate-dependent regulation of N-methyl-d-aspartic acid-type channels influences IPP-1 phosphorylation at Ser 67. The localization and expression of IPP-1 suggests that it may play discrete roles in certain regions and developing stages of the brain, independent of the regulation of protein phosphatase type 1 (PP-1). PP-1 binds to both phosphorylated and dephosphorylated IPP-1. Conversion of PP-1 to a Mn++-dependent state appears to play a role in its regulation by IPP-1. IPP-1 attenuates the activity of glycogen phosphorylase and is thought to be important in the hormonal control of glycogen metabolism. The human IPP-1 gene maps to chromosome 12q13.13 and encodes a mediator of cross-talk between several protein kinases and protein phosphatases.