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Gene Review

Pdp1  -  pyruvate dehyrogenase phosphatase...

Rattus norvegicus

Synonyms: PDP 1, PDPC 1, Ppm2c, Protein phosphatase 2C, Pyruvate dehydrogenase phosphatase catalytic subunit 1
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Disease relevance of Ppm2c

  • In the present study, recombinant rat protein phosphatase 2C (PrP-2C) expressed in Escherichia coli could dephosphorylate both Thr286/287 and Thr305/306 phosphorylation sites of CaM kinase II, which are responsible for the generation of Ca(2+)-independent activity and the inhibition of the total activity, respectively [1].
  • These results suggest that concomitant greater PDK4 and less PDP1 expression in skeletal muscle of OLETF rats before the onset of diabetes are responsible for the lowering of the PDC activity and may be related with the development of diabetes mellitus [2].

High impact information on Ppm2c

  • Protein phosphatase 2C binds selectively to and dephosphorylates metabotropic glutamate receptor 3 [3].
  • Protein phosphatase 2C (PP2C), an Mg(2+)-dependent enzyme that dephosphorylates serine and threonine residues, defines one of the three major families of structurally unrelated eukaryotic protein phosphatases [4].
  • Of the two PDP isoforms expressed in mammalian tissues, the Ca(2+)-sensitive isoform (PDP1) is highly expressed in rat heart, brain, and testis and is detectable but less abundant in rat muscle, lung, kidney, liver, and spleen [5].
  • We describe the cloning of a cDNA encoding a novel neuronal protein, named NERPP-2C, which is distantly related to protein phosphatase 2C and plays a role in the inhibitory response pathway to myelin inhibitors [6].
  • SCOP protein is predominantly expressed in the brain and has domains including a pleckstrin homology domain, leucine-rich repeats, a protein phosphatase 2C-like domain and a glutamine-rich region [7].

Biological context of Ppm2c


Anatomical context of Ppm2c


Associations of Ppm2c with chemical compounds


Analytical, diagnostic and therapeutic context of Ppm2c


  1. Dephosphorylation of autophosphorylated Ca2+/calmodulin-dependent protein kinase II by protein phosphatase 2C. Fukunaga, K., Kobayashi, T., Tamura, S., Miyamoto, E. J. Biol. Chem. (1993) [Pubmed]
  2. Downregulation of the skeletal muscle pyruvate dehydrogenase complex in the Otsuka Long-Evans Tokushima Fatty rat both before and after the onset of diabetes mellitus. Bajotto, G., Murakami, T., Nagasaki, M., Tamura, T., Tamura, N., Harris, R.A., Shimomura, Y., Sato, Y. Life Sci. (2004) [Pubmed]
  3. Protein phosphatase 2C binds selectively to and dephosphorylates metabotropic glutamate receptor 3. Flajolet, M., Rakhilin, S., Wang, H., Starkova, N., Nuangchamnong, N., Nairn, A.C., Greengard, P. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  4. Protein phosphatase 2C, encoded by ptc1+, is important in the heat shock response of Schizosaccharomyces pombe. Shiozaki, K., Akhavan-Niaki, H., McGowan, C.H., Russell, P. Mol. Cell. Biol. (1994) [Pubmed]
  5. Starvation and diabetes reduce the amount of pyruvate dehydrogenase phosphatase in rat heart and kidney. Huang, B., Wu, P., Popov, K.M., Harris, R.A. Diabetes (2003) [Pubmed]
  6. A novel phosphatase regulating neurite extension on CNS inhibitors. Labes, M., Roder, J., Roach, A. Mol. Cell. Neurosci. (1998) [Pubmed]
  7. SCOP, a novel gene product expressed in a circadian manner in rat suprachiasmatic nucleus. Shimizu, K., Okada, M., Takano, A., Nagai, K. FEBS Lett. (1999) [Pubmed]
  8. On the 6-phosphofructo-1-kinase phosphatase activity of protein phosphatase 2C and its dimeric nature. Mieskes, G., Söling, H.D. FEBS Lett. (1985) [Pubmed]
  9. Evidence that AMP triggers phosphorylation as well as direct allosteric activation of rat liver AMP-activated protein kinase. A sensitive mechanism to protect the cell against ATP depletion. Moore, F., Weekes, J., Hardie, D.G. Eur. J. Biochem. (1991) [Pubmed]
  10. Characterization of protein serine/threonine phosphatases in rat pancreas and development of an endogenous substrate-specific phosphatase assay. Lutz, M.P., Pinon, D.I., Miller, L.J. Pancreas (1994) [Pubmed]
  11. Purification and characterization of enkephalinase, angiotensin converting enzyme, and a third peptidyldipeptidase from rat brain. Cushman, D.W., Gordon, E.M., Wang, F.L., Cheung, H.S., Tung, R., Delaney, N.G. Life Sci. (1983) [Pubmed]
  12. Biochemical characterization of two forms of 3-hydroxy-3-methylglutaryl-CoA reductase kinase from cauliflower (Brassica oleracia). Ball, K.L., Dale, S., Weekes, J., Hardie, D.G. Eur. J. Biochem. (1994) [Pubmed]
  13. Covalent activation of heart AMP-activated protein kinase in response to physiological concentrations of long-chain fatty acids. Clark, H., Carling, D., Saggerson, D. Eur. J. Biochem. (2004) [Pubmed]
  14. The protein phosphatases involved in cellular regulation. 6. Measurement of type-1 and type-2 protein phosphatases in extracts of mammalian tissues; an assessment of their physiological roles. Ingebritsen, T.S., Stewart, A.A., Cohen, P. Eur. J. Biochem. (1983) [Pubmed]
  15. Histidyl phosphorylation and dephosphorylation of P36 in rat liver extract. Motojima, K., Goto, S. J. Biol. Chem. (1994) [Pubmed]
  16. Molecular cloning and primary structure of a protein phosphatase 2C isoform. Wenk, J., Trompeter, H.I., Pettrich, K.G., Cohen, P.T., Campbell, D.G., Mieskes, G. FEBS Lett. (1992) [Pubmed]
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