PPase-2A

Protein Phosphatase-2A (PPase-2A) is a serine/threonine phosphatase isolated from human red blood cells. It is isolated as the heterodimer of 60kDa (A) and 36kDa (C) subunits. It has the ability to dephosphorylate the α-subunit of phosphorylase kinase. With its 36–38kDa catalytic subunit, PPase-2A has broad substrate specificity and may play a regulatory role in DNA replication, transcription, protein synthesis, mitosis and glycogen metabolism. PPase-2A is stimulated in vitro by basic proteins such as protamine, histones and polylysine. The enzyme is inhibited by several environmental toxins and tumor promoters su...

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Protein Phosphatase-2A (PPase-2A) is a serine/threonine phosphatase isolated from human red blood cells. It is isolated as the heterodimer of 60kDa (A) and 36kDa (C) subunits. It has the ability to dephosphorylate the α-subunit of phosphorylase kinase. With its 36–38kDa catalytic subunit, PPase-2A has broad substrate specificity and may play a regulatory role in DNA replication, transcription, protein synthesis, mitosis and glycogen metabolism. PPase-2A is stimulated in vitro by basic proteins such as protamine, histones and polylysine. The enzyme is inhibited by several environmental toxins and tumor promoters such as okadaic acid and microcystin-LR. The chemically synthesized phosphopeptide, RRA(pT)VA (available in the Ser/Thr Phosphatase Assay System, Cat.# V2460), is an excellent substrate for PPase-2A.

References

1. Tung, H.Y. et al. (1985) Eur. J. Biochem. 148, 253–63.
2. Shenolikar, S. (1994) Annu. Rev. Cell Biol. 10, 55–86.
3. Bialojan, C. and Takai, A. (1988) Biochem. J. 256, 283–90.
4. Yoshizawa, S. et al. (1990) J. Cancer Res. Clin. Oncol. 116, 609–14.

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