Diacylglycerol regulates the plasma membrane calcium pump from human erythrocytes by direct interaction

Pérez-Gordones, María Carolina; Lugo, Miguel R.; Winkler, Moraima; Cervino, Vincenza; Benaím, Gustavo

doi:10.1016/j.abb.2009.07.010

Cited by 22 publications

(12 citation statements)

References 58 publications

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“…Recently, diacylglycerol has also been shown to be a stimulator of the PMCA. Interestingly, the activation induced by diacylglycerol is additional to that produced by calmodulin and PKC, suggesting that diacylglycerol interacts with the PMCA through a specific mechanism (14).…”

mentioning

confidence: 99%

Deletions and Mutations in the Acidic Lipid-binding Region of the Plasma Membrane Ca2+ Pump

Brini

Leva

Ortega

et al. 2010

Journal of Biological Chemistry

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mentioning

confidence: 99%

Deletions and Mutations in the Acidic Lipid-binding Region of the Plasma Membrane Ca2+ Pump

Brini

Leva

Ortega

et al. 2010

Journal of Biological Chemistry

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“…57). As was previously reported for PMCA (32) and other proteins (57), TNP-ATP is not a substrate for the pump and inhibits its ATPase activity. Table 2.…”

Section: Interaction Of Tnp-atp With Different Pmca Intermediates-mentioning

confidence: 61%

“…As described previously by Pérez-Gordones et al (32), in the presence of calcium, no hydrolysis was observed of TNP-ATP. As was reported for other ATPases (33)(34)(35)(36)(37) (39).…”

Section: Camentioning

confidence: 78%

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

Mangialavori¹,

Ferreira-Gomes²,

Saffioti

et al. 2013

Journal of Biological Chemistry

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“…Using these models, researchers have been able to identify abnormalities in PMCA activity in a number of disease states (28, 291). In addition, purified preparations of human erythrocyte PMCA have been widely used to identify molecular and pharmacological modulators of the pumps' activity such as F-and G-actin, acidic phospholipids, diacylglycerol, the bidentate chromium (III) ATP complex, the phytoalexin resveratrol, and inhibitory peptide caloxin1c2 (251,263,277,278,289,383).…”

Section: Pmca In Erythrocytesmentioning

confidence: 99%

The Plasma Membrane Calcium ATPasesand Their Role as Major New Players in Human Disease

Stafford

Wilson

Oceandy

et al. 2017

Physiological Reviews

107

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The Ca2+ extrusion function of the four mammalian isoforms of the plasma membrane calcium ATPases (PMCAs) is well established. There is also ever-increasing detail known of their roles in global and local Ca2+ homeostasis and intracellular Ca2+ signaling in a wide variety of cell types and tissues. It is becoming clear that the spatiotemporal patterns of expression of the PMCAs and the fact that their abundances and relative expression levels vary from cell type to cell type both reflect and impact on their specific functions in these cells. Over recent years it has become increasingly apparent that these genes have potentially significant roles in human health and disease, with PMCAs1-4 being associated with cardiovascular diseases, deafness, autism, ataxia, adenoma, and malarial resistance. This review will bring together evidence of the variety of tissue-specific functions of PMCAs and will highlight the roles these genes play in regulating normal physiological functions and the considerable impact the genes have on human disease.

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Diacylglycerol regulates the plasma membrane calcium pump from human erythrocytes by direct interaction

Cited by 22 publications

References 58 publications

Deletions and Mutations in the Acidic Lipid-binding Region of the Plasma Membrane Ca2+ Pump

Deletions and Mutations in the Acidic Lipid-binding Region of the Plasma Membrane Ca2+ Pump

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

The Plasma Membrane Calcium ATPasesand Their Role as Major New Players in Human Disease

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