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The Plasma Membrane Ca2+ ATPases: Isoform Specificity and Functional Versatility

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Regulation of Ca2+-ATPases,V-ATPases and F-ATPases

Part of the book series: Advances in Biochemistry in Health and Disease ((ABHD,volume 14))

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Abstract

Plasma membrane Ca2+ ATPases are single polypeptides of about 1100–1250 amino-acid residues with a molecular mass of 125–140 kDa. They contain ten membrane spanning segments and their N- and C-terminals are both on the cytosolic side. The bulk of their mass is also in the cytoplasm and contains three major intracellular domains: the A (actuator), N (nucleotide-binding), and P (catalytic phosphorylation) domains. Four basic isoforms are encoded by four distinct genes, and their transcripts originated a huge number of alternative splicing variants that in most cases are also translated in the corresponding protein variants. Emerging evidence underlines that PMCA pumps, in addition to maintain resting cytosolic Ca2+ levels against a steep concentration gradient (i.e., nM versus mM), play a local control in specific sub-plasma membrane domains by tethering Ca2+-/calmodulin-dependent enzymes and reducing their activity, i.e., by decreasing Ca2+ concentration in the microenvironment where they are confined. This aspect of pump activity confers to PMCA pump a key role as signal transducer and justifies the existence of so many PMCA variants that could be specialized in tuning the activity of different partners with different Ca2+ sensitivity.

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Acknowledgments

We are deeply grateful to Ernesto Carafoli who has greatly contributed during the years to clarify the mechanisms of action and regulation of the plasma membrane Ca2+ pump and has trained us in this field of investigation with enthusiasm and passion. T.C is supported by the Scientific Independence of Young Researchers (SIR) grant (Bando SIR 2014 n. RBSI14C65Z) from the Italian Ministry of University and Research (MIUR).

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Authors and Affiliations

  1. Department of Biomedical Sciences, University of Padova, Via Ugo Bassi 58b, 35131, Padova, Italy

    Tito Calì

  2. Department of Biology, University of Padova, Via Ugo Bassi 58b, 35131, Padova, Italy

    Denis Ottolini & Marisa Brini

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  1. Tito Calì
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  2. Denis Ottolini
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  3. Marisa Brini
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Correspondence to Marisa Brini .

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Editors and Affiliations

  1. Biochemistry and Biophysics, University of Kalyani, Kalyani, West Bengal, India

    Sajal Chakraborti

  2. University of Manitoba, Institute of Cardiovascular Science St. Boniface Hospital Research, Winnipeg, Manitoba, Canada

    Naranjan S Dhalla

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Calì, T., Ottolini, D., Brini, M. (2016). The Plasma Membrane Ca2+ ATPases: Isoform Specificity and Functional Versatility. In: Chakraborti, S., Dhalla, N. (eds) Regulation of Ca2+-ATPases,V-ATPases and F-ATPases. Advances in Biochemistry in Health and Disease, vol 14. Springer, Cham. https://doi.org/10.1007/978-3-319-24780-9_2

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