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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

PP2A  -  serine/threonine protein phosphatase 2A

Arabidopsis thaliana

Synonyms: F20P5.30, F20P5_30, TYPE 2A SERINE/THREONINE PROTEIN PHOSPHATASE
 
 
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High impact information on PP2A

  • Molecular markers of these two developmental processes (phosphatase PP2A and MYB65 in germination; LFY during flowering) were up-regulated in GCR1 overexpressors [1].
  • Using mass spectrometric analysis, several of these proteins, including Hsp90, 14-3-3 proteins, an SnRK2 serine/threonine protein kinase and the PP2A regulatory subunit RCN1 could be identified [2].
  • Taken together, our results suggest a myriad of PP2A subunit combinations, possibly with distinct substrate specificities, may occur within each Arabidopsis cell [3].
 

Analytical, diagnostic and therapeutic context of PP2A

  • PKIII was Ca2+-indepdented, inactivated by PP2A or PP2C, had a requirement for a hydrophobic residue in the +4 position of peptide substrates, had a molecular mass by gel filtration of approximately 140 kDa, and an antibody against the rye SNF1-related PK (RKIN1) recognized a 58 kDa subunit in fractions containing PKIII [4].

References

  1. GCR1, the putative Arabidopsis G protein-coupled receptor gene is cell cycle-regulated, and its overexpression abolishes seed dormancy and shortens time to flowering. Colucci, G., Apone, F., Alyeshmerni, N., Chalmers, D., Chrispeels, M.J. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  2. Isolation and identification of phosphatidic acid targets from plants. Testerink, C., Dekker, H.L., Lim, Z.Y., Johns, M.K., Holmes, A.B., Koster, C.G., Ktistakis, N.T., Munnik, T. Plant J. (2004) [Pubmed]
  3. Characterization of DNA sequences encoding a novel isoform of the 55 kDa B regulatory subunit of the type 2A protein serine/threonine phosphatase of Arabidopsis thaliana. Corum, J.W., Hartung, A.J., Stamey, R.T., Rundle, S.J. Plant Mol. Biol. (1996) [Pubmed]
  4. Three spinach leaf nitrate reductase-3-hydroxy-3-methylglutaryl-CoA reductase kinases that are required by reversible phosphorylation and/or Ca2+ ions. Douglas, P., Pigaglio, E., Ferrer, A., Halfords, N.G., MacKintosh, C. Biochem. J. (1997) [Pubmed]
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