title: Multifaceted plasma membrane Ca(2+) pumps: From structure to intracellular Ca(2+) handling and cancer.
abstract: Plasma membrane Ca(2+) ATPases (PMCAs) are intimately involved in the control of intracellular Ca(2+) concentration. They reduce Ca(2+) in the cytosol not only by direct ejection, but also by controlling the formation of inositol-1,4,5-trisphosphate and decreasing Ca(2+) release from the endoplasmic reticulum Ca(2+) pool. In mammals four genes (PMCA1-4) are expressed, and alternative RNA splicing generates more than twenty variants. The variants differ in their regulatory characteristics. They localize into highly specialized membrane compartments and respond to the incoming Ca(2+) with distinct temporal resolution. The expression pattern of variants depends on cell type; a change in this pattern can result in perturbed Ca(2+) homeostasis and thus altered cell function. Indeed, PMCAs undergo remarkable changes in their expression pattern during tumorigenesis that might significantly contribute to the unbalanced Ca(2+) homeostasis of cancer cells. This article is part of a Special Issue entitled: Calcium and Cell Fate. Guest Editors: Jacques Haiech, Claus Heizmann, Joachim Krebs, Thierry Capiod and Olivier Mignen.
authors.affiliation: 2(nd) Department of Pathology, Semmelweis University, Budapest, Hungary.
authors.forename: Rita
authors.initials: R
authors.lastname: Padányi
authors.affiliation: Molecular Biophysics Research Group of the Hungarian Academy of Sciences and Department of Biophysics, Semmelweis University, Budapest, Hungary.
authors.forename: Katalin
authors.initials: K
authors.lastname: Pászty
authors.affiliation: Department of Pathophysiology and Allergy Research, Medical University of Vienna, Vienna, Austria.
authors.forename: Luca
authors.initials: L
authors.lastname: Hegedűs
authors.affiliation: 2(nd) Department of Pathology, Semmelweis University, Budapest, Hungary.
authors.forename: Karolina
authors.initials: K
authors.lastname: Varga
authors.affiliation: Institut National de la Santé et de la Recherche Médicale, UMR U978 and Université Paris-13, PRES Sorbonne Paris-Cité, Bobigny, France.
authors.forename: Béla
authors.initials: B
authors.lastname: Papp
authors.affiliation: Department of Neurosurgery, Massachusetts General Hospital, Boston, MA, USA.
authors.forename: John T
authors.initials: JT
authors.lastname: Penniston
authors.affiliation: 2(nd) Department of Pathology, Semmelweis University, Budapest, Hungary; Molecular Oncology Research Group of the Hungarian Academy of Sciences and Semmelweis University, Budapest, Hungary. Electronic address: enyedi.agnes@med.semmelweis-univ.hu.
authors.forename: Ágnes
authors.initials: Á
authors.lastname: Enyedi
mesh_terms: D000818:Animals; D002118:Calcium / Q000378:metabolism*; D020013:Calcium Signaling; D002462:Cell Membrane / Q000378:metabolism*; D006706:Homeostasis; D006801:Humans; D015544:Inositol 1,4,5-Trisphosphate / Q000378:metabolism; D007527:Isoenzymes / Q000235:genetics / Q000378:metabolism; D009369:Neoplasms / Q000378:metabolism / Q000473:pathology; D053499:Plasma Membrane Calcium-Transporting ATPases / Q000235:genetics / Q000378:metabolism*
chemical_list: D007527:Isoenzymes; D015544:Inositol 1,4,5-Trisphosphate; D053499:Plasma Membrane Calcium-Transporting ATPases; D002118:Calcium
keywords: Ca(2+) signaling; Ca(2+)-calmodulin; Differentiation; Phosphatidylinositol-4,5-bisphosphate binding; Plasma membrane Ca(2+) ATPase; Tumor progression