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Gene Review

Atp2b2  -  ATPase, Ca++ transporting, plasma membrane 2

Rattus norvegicus

Synonyms: PMCA2, Plasma membrane calcium ATPase isoform 2, Plasma membrane calcium pump isoform 2, Plasma membrane calcium-transporting ATPase 2
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Disease relevance of Atp2b2


High impact information on Atp2b2

  • Taken together, our findings suggest that glutamate, which recently has been implicated in EAE pathogenesis, suppresses neuronal PMCA2 expression leading to Ca(2+) dyshomeostasis at initial clinical phases [2].
  • Moreover, exposure of spinal cord slice cultures to kainic acid significantly reduced PMCA2 mRNA levels [2].
  • These conditions, which cause a chronic increase of the resting free Ca(2+) concentration in the neurons, have recently been shown to promote up-regulation of the PMCA2, 3, and 1CII isoforms [3].
  • PMCA2 mRNAs are generated either by the inclusion of a 172-nucleotide exon, by the inclusion of both the 172-nucleotide exon and a 55-nucleotide exon, or by the exclusion of both exons [4].
  • PMCA2 mRNAs are expressed predominantly in brain and heart, whereas PMCA3 mRNAs are expressed predominantly in brain and skeletal muscle [5].

Biological context of Atp2b2


Anatomical context of Atp2b2

  • In contrast, astrocytes contain smaller amounts of PMCA2 [6].
  • After spinal cord injury, the expression of PMCA2 was decreased; however, the change in expression of other isoforms showed a tendency of decrease but did not reach a statistically significant level [7].
  • PMCA2 mRNA was highest in Purkinje cells of cerebellum and low in caudate-putamen, hypothalamic nuclei, habenula and choroid plexus [8].
  • It exhibits 81% and 85% amino acid identity, respectively, to isoforms 1 and 2 (PMCA1 and PMCA2) of the plasma membrane Ca-ATPase [5].
  • Within the dentate gyrus, PMCA 2 mRNA hybridized below control levels 4 h post-injection, but recovered to control levels by 24 h post-injection [9].

Associations of Atp2b2 with chemical compounds

  • Taken together, the kinetic data suggest that the deafwaddler mutation affects PMCA2 by slowing the E(1)P to E(2)P transition, resulting in approximately 70% reduction in the PMCA2-mediated Ca(2+) export [1].
  • A nucleotide substitution in deafwaddler results in a Gly to Ser transition at amino acid 283 in the small cytoplasmic loop of PMCA isoform 2 (PMCA2) [1].
  • PMCA 2 is the isoform with the highest affinity for calmodulin, and has also been associated with high levels of inositol triphosphate [10].

Other interactions of Atp2b2

  • By P10 (by postnatal day 10), most inner retinal PMCA consisted of PMCA2 and PMCA3 [11].
  • This provides the first evidence for the presence of PMCA2 and PMCA3 isoforms at the protein level in non-neuronal tissue [12].

Analytical, diagnostic and therapeutic context of Atp2b2

  • Using reverse transcription-polymerase chain reaction (RT-PCR) and Southern blot analyses, we have demonstrated PMCA1, -3, and -4, but not PMCA2, to be present in MC from these rat strains [13].
  • When PMCA2 isoforms were immunoprecipitated from purified hair bundles of rat utricle, 2w was the only site A variant detected; moreover, immunocytochemistry for 2w in rat vestibular and cochlear tissues indicated that this splice form was located solely in bundles [14].
  • Using immunofluorescence, we determined that PMCA2 is enriched in the stereocilia and present at a relatively low concentration in the kinocilium and in the remaining apical membrane [15].


  1. Characterization of the deafwaddler mutant of the rat plasma membrane calcium-ATPase 2. Penheiter, A.R., Filoteo, A.G., Croy, C.L., Penniston, J.T. Hear. Res. (2001) [Pubmed]
  2. Regulation of gene expression in experimental autoimmune encephalomyelitis indicates early neuronal dysfunction. Nicot, A., Ratnakar, P.V., Ron, Y., Chen, C.C., Elkabes, S. Brain (2003) [Pubmed]
  3. Calcineurin controls the expression of isoform 4CII of the plasma membrane Ca(2+) pump in neurons. Guerini, D., Wang, X., Li, L., Genazzani, A., Carafoli, E. J. Biol. Chem. (2000) [Pubmed]
  4. Alternative splicing of exons encoding the calmodulin-binding domains and C termini of plasma membrane Ca(2+)-ATPase isoforms 1, 2, 3, and 4. Keeton, T.P., Burk, S.E., Shull, G.E. J. Biol. Chem. (1993) [Pubmed]
  5. Molecular cloning of a third isoform of the calmodulin-sensitive plasma membrane Ca2+-transporting ATPase that is expressed predominantly in brain and skeletal muscle. Greeb, J., Shull, G.E. J. Biol. Chem. (1989) [Pubmed]
  6. Plasma membrane calcium ATPase isoforms in astrocytes. Fresu, L., Dehpour, A., Genazzani, A.A., Carafoli, E., Guerini, D. Glia (1999) [Pubmed]
  7. Plasma membrane calcium ATPase expression in the rat spinal cord. Tachibana, T., Ogura, H., Tokunaga, A., Dai, Y., Yamanaka, H., Seino, D., Noguchi, K. Brain Res. Mol. Brain Res. (2004) [Pubmed]
  8. Plasma membrane Ca(2+)-ATPase isoforms: distribution of mRNAs in rat brain by in situ hybridization. Stahl, W.L., Eakin, T.J., Owens, J.W., Breininger, J.F., Filuk, P.E., Anderson, W.R. Brain Res. Mol. Brain Res. (1992) [Pubmed]
  9. Seizure-induced alterations of plasma membrane calcium ATPase isoforms 1, 2 and 3 mRNA and protein in rat hippocampus. Garcia, M.L., Murray, K.D., Garcia, V.B., Strehler, E.E., Isackson, P.J. Brain Res. Mol. Brain Res. (1997) [Pubmed]
  10. Evidence for differential regulation of calcium by outer versus inner hair cells: plasma membrane Ca-ATPase gene expression. Furuta, H., Luo, L., Hepler, K., Ryan, A.F. Hear. Res. (1998) [Pubmed]
  11. Ontogeny of plasma membrane Ca2+ ATPase isoforms in the neural retina of the postnatal rat. Rentería, R.C., Strehler, E.E., Copenhagen, D.R., Krizaj, D. Vis. Neurosci. (2005) [Pubmed]
  12. Expression of multiple plasma membrane Ca(2+)-ATPases in rat pancreatic islet cells. Kamagate, A., Herchuelz, A., Bollen, A., Van Eylen, F. Cell Calcium (2000) [Pubmed]
  13. Plasma membrane calcium ATPase isoform expression in cultured rat mesangial cells. Rouse, D., Abramowitz, J., Zhou, X., Kamijo, T., Gonzalez, J., Wang, J., Vaziri, N.D., Suki, W.N. Am. J. Physiol. (1997) [Pubmed]
  14. Splice-site A choice targets plasma-membrane Ca2+-ATPase isoform 2 to hair bundles. Hill, J.K., Williams, D.E., LeMasurier, M., Dumont, R.A., Strehler, E.E., Gillespie, P.G. J. Neurosci. (2006) [Pubmed]
  15. Rapid turnover of stereocilia membrane proteins: evidence from the trafficking and mobility of plasma membrane Ca(2+)-ATPase 2. Grati, M., Schneider, M.E., Lipkow, K., Strehler, E.E., Wenthold, R.J., Kachar, B. J. Neurosci. (2006) [Pubmed]
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