Article (Scientific journals)
Plasma membrane calcium ATPase proteins as novel regulators of signal transduction pathways.
Holton, Mary Louisa; Wang, Weiguang; Emerson, Michael et al.
2010In World Journal of Biological Chemistry, 1 (6), p. 201-8
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Keywords :
Calcineurin; Nitric oxide; Nuclear factor of activated T cells; Plasma membrane calcium ATPase; Regulation; Signal transduction
Abstract :
[en] Emerging evidence suggests that plasma membrane calcium ATPases (PMCAs) play a key role as regulators of calcium-triggered signal transduction pathways via interaction with partner proteins. PMCAs regulate these pathways by targeting specific proteins to cellular sub-domains where the levels of intracellular free calcium are kept low by the calcium ejection properties of PMCAs. According to this model, PMCAs have been shown to interact functionally with the calcium-sensitive proteins neuronal nitric oxide synthase, calmodulin-dependent serine protein kinase, calcineurin and endothelial nitric oxidase synthase. Transgenic animals with altered expression of PMCAs are being used to evaluate the physiological significance of these interactions. To date, PMCA interactions with calcium-dependent partner proteins have been demonstrated to play a crucial role in the pathophysiology of the cardiovascular system via regulation of the nitric oxide and calcineurin/nuclear factor of activated T cells pathways. This new evidence suggests that PMCAs play a more sophisticated role than the mere ejection of calcium from the cells, by acting as modulators of signaling transduction pathways.
Disciplines :
Cardiovascular & respiratory systems
Author, co-author :
Holton, Mary Louisa
Wang, Weiguang
Emerson, Michael
Neyses, Ludwig ;  University of Luxembourg > Research Office
Armesilla, Angel L.
Language :
English
Title :
Plasma membrane calcium ATPase proteins as novel regulators of signal transduction pathways.
Publication date :
2010
Journal title :
World Journal of Biological Chemistry
ISSN :
1949-8454
Publisher :
Beijing Baishideng BioMed Scientific Co, Beijing, China
Volume :
1
Issue :
6
Pages :
201-8
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBilu :
since 11 August 2014

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