Ca2+ Pumps and Ca2+ Antiporters in Plant Development

Pittman, Jon K.; Bonza, Maria Cristina; Michelis, Maria Ida De

doi:10.1007/978-3-642-14369-4_5

Cited by 19 publications

(19 citation statements)

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“…Ca 2+ -ATPase plays a crucial role in maintaining cytoplasmic Ca 2+ homeostasis, which could use the energy of ATP hydrolysis to pump Ca 2+ from the cytoplasm into intracellular compartments or into the apoplast, maintaining the Ca 2+ balance Pittman et al, 2011). In normal conditions, free Ca 2+ levels in the cytoplasm of cells are very low, but a large amount of Ca 2+ is located in vacuoles and intercellular spaces.…”

Section: Tablementioning

confidence: 99%

Regulation of 2,4-epibrassinolide on mineral nutrient uptake and ion distribution in Ca(NO3)2 stressed cucumber plants

Yuan

Zhu

Shu

et al. 2015

Journal of Plant Physiology

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Section: Tablementioning

confidence: 99%

Regulation of 2,4-epibrassinolide on mineral nutrient uptake and ion distribution in Ca(NO3)2 stressed cucumber plants

Yuan

Zhu

Shu

et al. 2015

Journal of Plant Physiology

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“…An increasing amount of evidence indicates that signal specificity is encoded by the amplitude, frequency, and time extension of cytosolic Ca 2+ waves, which in turn depend on the activity of Ca 2+ channels—which when open flood the cytosol with Ca 2+ from the apoplast and/or intracellular stores—and of active Ca 2+ transporters—which extrude Ca 2+ to the apoplast or sequester it in intracellular stores. Fine-tuning of the Ca 2+ transport systems in response to different signals is thus a crucial feature of Ca 2+ -mediated signal transduction (Sanders et al , 2002; Boursiac and Harper, 2007; McAinsh and Pittman, 2009; Das and Pandey, 2010; Dodd et al , 2010; Bonza and De Michelis, 2011; Pittman et al , 2011). …”

Section: Introductionmentioning

confidence: 99%

“…PM Ca 2+ pumps are likely to play a crucial role in re-establishing the low basal Ca 2+ concentration especially after its increase due to opening of PM Ca 2+ channels. Indeed, the available evidence, albeit fragmentary, demonstrates their involvement in fundamental processes such as development, hormonal regulation, and response to biotic and abiotic stresses; however, their physiological role and the mechanisms underlying their regulation in response to specific signals have not been ascertained yet (Boursiac and Harper, 2007; Bonza and De Michelis, 2011; Pittman et al , 2011). …”

Section: Introductionmentioning

confidence: 99%

“…PM Ca 2+ pumps are calmodulin (CaM)-regulated Ca 2+ -ATPases, belonging to the P-type ATPase superfamily: three isoforms of CaM-regulated Ca 2+ -ATPase, all belonging to the same cluster, have been identified as PM-localized pumps in Arabidopsis thaliana : among these, the best characterized at the biochemical level is ACA8, a widely expressed isoform found in all plant organs (Bonza and De Michelis, 2011; Pittman et al , 2011). …”

Section: Introductionmentioning

confidence: 99%

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Phosphorylation of serine residues in the N-terminus modulates the activity of ACA8, a plasma membrane Ca2+-ATPase of Arabidopsis thaliana

Giacometti

Marrano

Bonza

et al. 2011

Journal of Experimental Botany

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ACA8 is a plasma membrane-localized isoform of calmodulin (CaM)-regulated Ca2+-ATPase of Arabidopsis thaliana. Several phosphopeptides corresponding to portions of the regulatory N-terminus of ACA8 have been identified in phospho-proteomic studies. To mimic phosphorylation of the ACA8 N-terminus, each of the serines found to be phosphorylated in those studies (Ser19, Ser22, Ser27, Ser29, Ser57, and Ser99) has been mutated to aspartate. Mutants have been expressed in Saccharomyces cerevisiae and characterized: mutants S19D and S57D—and to a lesser extent also mutants S22D and S27D—are deregulated, as shown by their low activation by CaM and by tryptic cleavage of the N-terminus. The His-tagged N-termini of wild-type and mutant ACA8 (6His-1M-I116) were expressed in Escherichia coli, affinity-purified, and used to analyse the kinetics of CaM binding by surface plasmon resonance. All the analysed mutations affect the kinetics of interaction with CaM to some extent: in most cases, the altered kinetics result in marginal changes in affinity, with the exception of mutants S57D (KD ∼10-fold higher than wild-type ACA8) and S99D (KD about half that of wild-type ACA8). The ACA8 N-terminus is phosphorylated in vitro by two isoforms of A. thaliana calcium-dependent protein kinase (CPK1 and CPK16); phosphorylation of mutant 6His-1M-I116 peptides shows that CPK16 is able to phosphorylate the ACA8 N-terminus at Ser19 and at Ser22. The possible physiological implications of the subtle modulation of ACA8 activity by phosphorylation of its N-terminus are discussed.

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“…Transient increases in cytosolic Ca 2+ are triggered by the opening of Ca 2+ permeable channels that mediate passive ion influx from the apoplast and/or intracellular compartments, while Ca 2+ active transporters (Ca 2+ -H + antiporters and Ca 2+ -ATPases) determine the recovery of the resting cytosolic free Ca 2+ concentration after the stimulus. Ca 2+ -ATPases are thought to be crucial in defining the shape of the calcium transient and therefore in eliciting plant specific response to various stimuli (Sanders et al 2002; McAinsh and Pittman 2009; Dodd et al 2010; Kudla et al 2010; Pittman et al 2011; Spalding and Harper 2011; Bose et al 2011). …”

Section: Introductionmentioning

confidence: 99%

ACA12 is a deregulated isoform of plasma membrane Ca2+-ATPase of Arabidopsis thaliana

et al. 2013

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Plant auto-inhibited Ca2+-ATPases (ACA) are crucial in defining the shape of calcium transients and therefore in eliciting plant responses to various stimuli. Arabidopsis thaliana genome encodes ten ACA isoforms that can be divided into four clusters based on gene structure and sequence homology. While isoforms from clusters 1, 2 and 4 have been characterized, virtually nothing is known about members of cluster 3 (ACA12 and ACA13). Here we show that a GFP-tagged ACA12 localizes at the plasma membrane and that expression of ACA12 rescues the phenotype of partial male sterility of a null mutant of the plasma membrane isoform ACA9, thus providing genetic evidence that ACA12 is a functional plasma membrane-resident Ca2+-ATPase. By ACA12 expression in yeast and purification by CaM-affinity chromatography, we show that, unlike other ACAs, the activity of ACA12 is not stimulated by CaM. Moreover, full length ACA12 is able to rescue a yeast mutant deficient in calcium pumps. Analysis of single point ACA12 mutants suggests that ACA12 loss of auto-inhibition can be ascribed to the lack of two acidic residues - highly conserved in other ACA isoforms - localized at the cytoplasmic edge of the second and third transmembrane segments. Together, these results support a model in which the calcium pump activity of ACA12 is primarily regulated by increasing or decreasing mRNA expression and/or protein translation and degradation.

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Ca2+ Pumps and Ca2+ Antiporters in Plant Development

Cited by 19 publications

References 146 publications

Regulation of 2,4-epibrassinolide on mineral nutrient uptake and ion distribution in Ca(NO3)2 stressed cucumber plants

Regulation of 2,4-epibrassinolide on mineral nutrient uptake and ion distribution in Ca(NO3)2 stressed cucumber plants

Phosphorylation of serine residues in the N-terminus modulates the activity of ACA8, a plasma membrane Ca2+-ATPase of Arabidopsis thaliana

ACA12 is a deregulated isoform of plasma membrane Ca2+-ATPase of Arabidopsis thaliana

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