Conformational Changes Produced by ATP Binding to the Plasma Membrane Calcium Pump

Mangialavori, Irene C.; Ferreira-Gomes, Mariela; Saffioti, Nicolás A.; González-Lebrero, Rodolfo M.; Rossi, Rolando; Rossi, Juan Pablo F.C.

doi:10.1074/jbc.m113.494633

Cited by 14 publications

(10 citation statements)

References 73 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Recently, we employed a phospholipid analog, [ 125 I]TID-PC/16, to assess different transmembrane conformations of PMCA from the study of lipid-protein interaction (12). Using the same experimental approach and kinetic measurements, we proposed a model for the PMCA cycle that included structural information about the transmembrane domain and its interaction with neutral phospholipids (13). Our results showed that the amount of PMCA annular lipids (i.e.…”

mentioning

confidence: 96%

Modulation of Plasma Membrane Ca2+-ATPase by Neutral Phospholipids

Pignataro

Dodes-Traian

González-Flecha

et al. 2015

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Background: Membrane proteins require phospholipids to be biologically active. Results: An increase of phosphatidylcholine/detergent molar ratio leads to a biphasic behavior of the PMCA Ca 2ϩ -ATPase activity, whose maximum depends on phosphatidylcholine characteristics. Conclusion: The optimum hydrophobic thickness for PMCA structure and Ca 2ϩ -ATPase activity is about 24 Å. Significance: Differential modulation by neutral phospholipids could be a general mechanism for regulating membrane protein function.

show abstract

mentioning

confidence: 96%

Modulation of Plasma Membrane Ca2+-ATPase by Neutral Phospholipids

Pignataro

Dodes-Traian

González-Flecha

et al. 2015

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

show abstract

“…Our results show that Al 3+ stabilizes a phosphorylated intermediate of PMCA whereas it binds to a dephosphorylated intermediate in SERCA. Both PMCA (39) and SERCA (40) bind ATP with high affinity in the absence of Ca 2+ . However, Ca 2+ binding is required for the enzyme activation, even if Mg 2+ is present.…”

Section: Discussionmentioning

confidence: 99%

Aluminum inhibits the plasma membrane and sarcoplasmic reticulum Ca2+-ATPases by different mechanisms

Sautu

Saffioti

Ferreira-Gomes

et al. 2018

Biochimica et Biophysica Acta (BBA) - Biomembranes

Self Cite

View full text Add to dashboard Cite

Aluminum (Al) is involved in the pathophysiology of neurodegenerative disorders. The mechanisms that have been proposed to explain the action of Al toxicity are linked to changes in the cellular calcium homeostasis, placing the transporting calcium pumps as potential targets. The aim of this work was to study the molecular inhibitory mechanism of Al on Ca-ATPases such as the plasma membrane and the sarcoplasmic reticulum calcium pumps (PMCA and SERCA, respectively). These P-ATPases transport Ca actively from the cytoplasm towards the extracellular medium and to the sarcoplasmic reticulum, respectively. For this purpose, we performed enzymatic measurements of the effect of Al on purified preparations of PMCA and SERCA. Our results show that Al is an irreversible inhibitor of PMCA and a slowly-reversible inhibitor of SERCA. The binding of Al is affected by Ca in SERCA, though not in PMCA. Al prevents the phosphorylation of SERCA and, conversely, the dephosphorylation of PMCA. The dephosphorylation time courses of the complex formed by PMCA and Al (EPAl) in the presence of ADP or ATP show that EPAl is composed mainly by the conformer EP. This work shows for the first time a distinct mechanism of Al inhibition that involves different intermediates of the reaction cycle of these two Ca-ATPases.

show abstract

“…the Na + /K + ‐ATPase), the ion transport cycle catalysed by PMCA can be described as a sequential change of protein conformations driven by the energy of ATP hydrolysis (Mangialavori et al . ). The two main conformations (E1 and E2) alternately face the ion‐binding sites with different ion affinities to the extracellular or the cytosolic side.…”

Section: Atp2b3 (Plasma Membrane Ca2+‐atpase)mentioning

confidence: 97%

Of channels and pumps: different ways to boost the aldosterone?

Bandulik

2016

Acta Physiologica

View full text Add to dashboard Cite

The mineralocorticoid aldosterone is a major factor controlling the salt and water balance and thereby also the arterial blood pressure. Accordingly, primary aldosteronism (PA) characterized by an inappropriately high aldosterone secretion is the most common form of secondary hypertension. The physiological stimulation of aldosterone synthesis in adrenocortical glomerulosa cells by angiotensin II and an increased plasma K concentration depends on a membrane depolarization and an increase in the cytosolic Ca activity. Recurrent gain-of-function mutations of ion channels and transporters have been identified in a majority of cases of aldosterone-producing adenomas and in familial forms of PA. In this review, the physiological role of these genes in the regulation of aldosterone synthesis and the altered function of the mutant proteins as well are described. The specific changes of the membrane potential and the cellular ion homoeostasis in adrenal cells expressing the different mutants are compared, and their impact on autonomous aldosterone production and proliferation is discussed.

show abstract

Conformational Changes Produced by ATP Binding to the Plasma Membrane Calcium Pump

Cited by 14 publications

References 73 publications

Modulation of Plasma Membrane Ca2+-ATPase by Neutral Phospholipids

Modulation of Plasma Membrane Ca2+-ATPase by Neutral Phospholipids

Aluminum inhibits the plasma membrane and sarcoplasmic reticulum Ca2+-ATPases by different mechanisms

Of channels and pumps: different ways to boost the aldosterone?

Contact Info

Product

Resources

About