P-type calcium ATPases in higher plants - biochemical, molecular and functional properties

Evans, D.E. and Williams, L.E. (1998) P-type calcium ATPases in higher plants - biochemical, molecular and functional properties. Biochimica et Biophysica Acta - Biomembranes, 1376 (1), 1-25. (doi:10.1016/S0304-4157(97)00009-9).

Abstract

Plant and animal cells regulate cytosolic free calcium at sub-micromolar concentrations (see 1, 2 for reviews). This is achieved by a combination of active Ca2+ pumps (P-type ATPases) and antiports energised by the primary ion-motive pumps of the cell, together with regulated Ca2+-influx channels. In plants, the primary motive force for the transport of most solutes is provided by trans-membrane proton pumps located at the plasma membrane and vacuolar membrane (tonoplast); this contrasts with the sodium/potassium systems of mammalian cells (for a review, see [1]). Recently, a variety of studies have shown that plant cells contain several types of Ca2+-pumping ATPase, including those possessing a calmodulin-binding autoinhibitory domain and those lacking such a domain 2, 3, 4, 5. Molecular and biochemical evidence indicates similarities, but also key differences (particularly in subcellular locations) between plants and animals, e.g. 2, 3, 4, 5, 6.
It is the aim of this review to draw together current molecular and related data indicating the structure, function and location of the various plant Ca2+ pumps and to compare these with their homologues from other organisms

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