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Ppp2cb  -  protein phosphatase 2 (formerly 2A),...

Mus musculus

Synonyms: AI115466, D8Ertd766e, PP2A-beta, PP2Ac, Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
 
 
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High impact information on Ppp2cb

  • We show here that a phosphoprotein encoded by mouse alpha4 (malpha4) gene transmitting a signal through B-cell antigen receptor (BCR) is associated with the catalytic subunit of protein phosphatase 2A (PP2Ac) [1].
  • Introduction of the malpha4 cDNA into Jurkat cells or the increased association of PP2Ac/alpha4 by the culture with low serum concentration confers cells with rapamycin resistance [1].
  • Rapamycin treatment disrupts the association of PP2Ac/alpha4 in parallel with the inhibitory effect of lymphoid cell proliferation [1].
  • Reciprocal changes in binding because of mutations indicate competitive distribution of PP2Ac between these regulatory subunits and demonstrate that the mutated catalytic subunits retained a native conformation [2].
  • Interestingly, mast cells treated with P. aeruginosa had reduced protein levels of phosphatase 2A catalytic unit (PP2Ac), which prompted us to determine whether a direct association between PKCalpha and PP2A occurs in mast cells [3].
 

Biological context of Ppp2cb

  • By using transfection experiments and immune kinase assays, we show that endogenous PP2Ac and CK2beta are the only major substrates associating with epitope-tagged CK2alpha, and that expression of activated Raf results in disruption of the CK2alpha-PP2A association [4].
 

Anatomical context of Ppp2cb

  • A trimeric protein phosphatase 2A (PP2A(T55)) composed of the catalytic (PP2Ac), structural (PR65/A), and regulatory (PR55/B) subunits was isolated from rabbit skeletal muscle by thiophosphorylase affinity chromatography, and contained two additional proteins of 54 and 55 kDa, respectively [5].
  • The catalytic subunit of protein phosphatase 2A (PP2Ac) with EF-2 as a substrate exhibits the same sensitivity towards okadaic acid and insensitivity towards heparin as the EF-2 phosphatase of epidermal cytosol [6].
 

Associations of Ppp2cb with chemical compounds

 

Other interactions of Ppp2cb

References

  1. Ig receptor binding protein 1 (alpha4) is associated with a rapamycin-sensitive signal transduction in lymphocytes through direct binding to the catalytic subunit of protein phosphatase 2A. Inui, S., Sanjo, H., Maeda, K., Yamamoto, H., Miyamoto, E., Sakaguchi, N. Blood (1998) [Pubmed]
  2. Overlapping binding sites in protein phosphatase 2A for association with regulatory A and alpha-4 (mTap42) subunits. Prickett, T.D., Brautigan, D.L. J. Biol. Chem. (2004) [Pubmed]
  3. Protein phosphatase 2A and protein kinase Calpha are physically associated and are involved in Pseudomonas aeruginosa-induced interleukin 6 production by mast cells. Boudreau, R.T., Garduno, R., Lin, T.J. J. Biol. Chem. (2002) [Pubmed]
  4. CK2alpha-protein phosphatase 2A molecular complex: possible interaction with the MAP kinase pathway. Lebrin, F., Bianchini, L., Rabilloud, T., Chambaz, E.M., Goldberg, Y. Mol. Cell. Biochem. (1999) [Pubmed]
  5. Interaction of nucleoredoxin with protein phosphatase 2A. Lechward, K., Sugajska, E., de Baere, I., Goris, J., Hemmings, B.A., Zolnierowicz, S. FEBS Lett. (2006) [Pubmed]
  6. A type 2A protein phosphatase dephosphorylates the elongation factor 2 and is stimulated by the phorbol ester TPA in mouse epidermis in vivo. Gschwendt, M., Kittstein, W., Mieskes, G., Marks, F. FEBS Lett. (1989) [Pubmed]
  7. The delta isoform of protein phosphatase type 1 is localized in nucleolus and dephosphorylates nucleolar phosphoproteins. Kotani, H., Ito, M., Hamaguchi, T., Ichikawa, K., Nakano, T., Shima, H., Nagao, M., Ohta, N., Furuichi, Y., Takahashi, T., Umekawa, H. Biochem. Biophys. Res. Commun. (1998) [Pubmed]
 
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