Ca2+ ATPases are P-type ATPases which use the energy of ATP hydrolysis to pump Ca2+ from the cytoplasm into intracellular compartments or into the apoplast. Plant cells possess two types of Ca2+ pumping ATPases, named respectively ECAs (for ER-type Ca2+ ATPase) and ACAs (for auto-inhibited Ca2+ ATPase). Each type comprehends different isoforms, localised on different membranes. Here we summarise the available knowledge of the biochemical characteristics and of the physiological role of plant Ca2+ ATPases, greatly improved after gene identification which allows both biochemical analysis of single isoforms through heterologous expression in yeast and expression profiling and phenotypic analysis of single isoform knock-out mutants.

The plant Ca2+-ATPases repertoire : biochemical features and physiological functions / M.C. Bonza, M.I. De Michelis. - In: PLANT BIOLOGY. - ISSN 1435-8603. - 13:3(2011 May), pp. 421-430. [10.1111/j.1438-8677.2010.00405.x]

The plant Ca2+-ATPases repertoire : biochemical features and physiological functions

M.C. Bonza
Primo
;
M.I. De Michelis
Ultimo
2011

Abstract

Ca2+ ATPases are P-type ATPases which use the energy of ATP hydrolysis to pump Ca2+ from the cytoplasm into intracellular compartments or into the apoplast. Plant cells possess two types of Ca2+ pumping ATPases, named respectively ECAs (for ER-type Ca2+ ATPase) and ACAs (for auto-inhibited Ca2+ ATPase). Each type comprehends different isoforms, localised on different membranes. Here we summarise the available knowledge of the biochemical characteristics and of the physiological role of plant Ca2+ ATPases, greatly improved after gene identification which allows both biochemical analysis of single isoforms through heterologous expression in yeast and expression profiling and phenotypic analysis of single isoform knock-out mutants.
Ca2+ ATPase ; Calmodulin ; Phospholipids ; Phosphorylation ; P-type ATPases
Settore BIO/04 - Fisiologia Vegetale
mag-2011
2010
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/158244
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