Encyclopedia of Signaling Molecules

Living Edition
| Editors: Sangdun Choi

Plasma Membrane Calcium-Transporting ATPase

Living reference work entry
DOI: https://doi.org/10.1007/978-1-4614-6438-9_133-1

Synonyms

Historical Background

The existence of a plasma membrane calcium-transporting ATPase (PMCA) that actively pumps Ca2+ ions out of the cell was first demonstrated in erythrocyte (red blood cell) membranes by Schatzmann (1966). Because of its generally low abundance and difficult biochemical properties, it took over a decade until the PMCA was first isolated in purified form. Crucial for the successful purification was the discovery that the PMCA binds with high affinity, and in a Ca2+-dependent manner, to the Ca2+ sensor protein calmodulin (Niggli et al. 1979). Subsequent work showed that at least one type of plasma membrane Ca2+ ATPase is found in all eukaryotic cells including those from fungi, animals, and plants (Axelsen and Palmgren 1998; Thever and Saier 2009). It is now well established that active Ca2+ expulsion by the PMCAs is an essential component of eukaryotic cellular Ca2+handling. Although, PMCAs were...

Keywords

Hair Cell Splice Variant Cerebellar Ataxia Export System Spinal Cord Pathology 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
This is a preview of subscription content, log in to check access.

References

  1. Axelsen KB, Palmgren MG. Evolution of substrate specificities in the P-type ATPase superfamily. J Mol Evol. 1998;46:84–101.CrossRefPubMedGoogle Scholar
  2. Brini M, Carafoli E. Calcium pumps in health and disease. Physiol Rev. 2009;89:1341–78.CrossRefPubMedGoogle Scholar
  3. Brini M, Carafoli E, Cali T. The plasma membrane calcium pumps: focus on the role in (neuro) pathology. Biochem Biophys Res Commun. 2016; pii: S0006-291X(16)31239-6. doi: 10.1016/j.bbrc.2016.07.117. Available online 29 July 2016.Google Scholar
  4. Hill JK, Williams DE, LeMasurier M, Dumont RA, Strehler EE, Gillespie PG. Splice-site A choice targets plasma-membrane Ca2+-ATPase isoform 2 to hair bundles. J Neurosci. 2006;26:6172–80.CrossRefPubMedPubMedCentralGoogle Scholar
  5. Holton ML, Wang W, Emerson M, Neyses L, Armesilla AL. Plasma membrane calcium ATPase proteins as novel regulators of signal transduction pathways. World J rBiol Chem. 2010;1:201–8.CrossRefGoogle Scholar
  6. Huang H, Nagaraja RY, Garside ML, Akemann W, Knöpfel T, Empson RM. Contribution of plasma membrane Ca2+ ATPase to cerebellar synapse function. World J Biol Chem. 2010;1:95–102.CrossRefPubMedPubMedCentralGoogle Scholar
  7. Lehotsky J, Kaplán P, Murín R, Raeymaekers L. The role of plasma membrane Ca2+ pumps (PMCAs) in pathologies of mammalian cells. Front Biosci. 2002;7:d53–84.PubMedGoogle Scholar
  8. Li M, Ho PW-L, Pang SY-Y, Tse ZH-M, Kung MH-W, Sham P-C, Ho S-L. PMCA4 (ATP2B4) mutation in familial spastic paraplegia. PLoS One. 2014;9:e104790.CrossRefPubMedPubMedCentralGoogle Scholar
  9. Moeller JV, Olesen C, Winther A-ML, Nissen P. The sarcoplasmic Ca2+-ATPase: design of a perfect chemi-omotioc pump. Q Rev Biophys. 2010;43:501–66.CrossRefGoogle Scholar
  10. Niggli V, Penniston JT, Carafoli E. Purification of the (Ca2+ + Mg2+)-ATPase from human erythrocyte membranes using a calmodulin affinity column. J Biol Chem. 1979;254:9955–8.PubMedGoogle Scholar
  11. Oceandy D, Mohamed TMA, Cartwright EJ, Neyses L. Local signals with global impacts and clnical implications: lessons from the plasma membrane calcium pump (PMCA4). Biochim Biophys Acta. 2011;1813:974–8.CrossRefPubMedGoogle Scholar
  12. Pászty K, Caride AJ, Bajzer Z, Offord CP, Padányi R, Hegedüs L, Varga K, Strehler EE, Enyedi A. Plasma membrane Ca2+-ATPases can shape the pattern of Ca2+ transients induced by store-operated Ca2+ entry. Sci Signal. 2015;8:ra19.CrossRefPubMedGoogle Scholar
  13. Pedersen PL, Carafoli E. Ion motive ATPases. I. Ubiquity, properties, and significance for cell function. Trends Biochem Sci. 1987;12:146–50.CrossRefGoogle Scholar
  14. Prasad V, Okunade G, Liu L, Paul RJ, Shull GE. Distinct phenotypes among plasma membrane Ca2+-ATPase knockout mice. Ann N Y Acad Sci. 2007;1099:276–86.CrossRefPubMedGoogle Scholar
  15. Reinhardt TA, Lippolis JD, Shull GE, Horst RL. Null mutation in the gene encoding plasma membrane Ca2+-ATPase isoform 2 impairs calcium transport into milk. J Biol Chem. 2004;279:42369–73.CrossRefPubMedGoogle Scholar
  16. Schatzmann HJ. ATP-dependent Ca++ extrusion from human red cells. Experientia. 1966;22:364–8.CrossRefPubMedGoogle Scholar
  17. Strehler EE, Zacharias DA. Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps. Physiol Rev. 2001;81:21–50.PubMedGoogle Scholar
  18. Strehler EE, Caride AJ, Filoteo AG, Xiong Y, Penniston JT, Enyedi A. Plasma membrane Ca2+ ATPases as dynamic regulators of cellular calcium handling. Ann NY Acad Sci. 2007;1099:226–36.CrossRefPubMedGoogle Scholar
  19. Strehler EE. The ATP2B plasma membrane Ca2+ ATPase family: regulation in response to changing demands of cellular calcium transport. In: Chakraborti S, Dhalla NS, editors. Regulation of Ca2+-ATPases, V-ATPases and F-ATPases, Advances in Biochemistry in Health and Disease14 Cham: Springer; 2016. p. 63–80.CrossRefGoogle Scholar
  20. Thever MD, Saier MH. Bioinformatic characterization of P-type ATPases encoded within the fully sequenced genomes of 26 eukaryotes. J Membr Biol. 2009;229:115–30.CrossRefPubMedPubMedCentralGoogle Scholar
  21. Toyoshima C. How Ca2+-ATPase pumps ions across the sarcoplasmic reticulum membrane. Biochim Biophys Acta. 2009;1793:941–6.CrossRefPubMedGoogle Scholar

Copyright information

© Springer Science+Business Media LLC 2016

Authors and Affiliations

  1. 1.Department of Biochemistry and Molecular BiologyMayo Clinic College of Medicine and ScienceRochesterUSA
  2. 2.Department of BiomedicineUniversity of BaselBaselSwitzerland