Modulation of plasma membrane Ca2-ATPase by neutral Phospholipids: effect of the micelle-vesicle transition and the bilayer thickness

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 Ca2-ATPase activity, whose maximum depends on phosphatidylcholine characteristics. Conclusion: The optimum hydrophobic thickness for PMCA structure and Ca2-ATPase activity is about 24 Å. Significance: Differential modulation by neutral phospholipids could be a general mechanism for regulating membrane protein function.

Palabras clave: Calcium Atpase , Enzyme Turnover , Lipid Bilayer , Molecular Dynamics

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Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Unported (CC BY-NC-SA 2.5)

Identificadores

URI: http://hdl.handle.net/11336/21341

DOI: http://dx.doi.org/10.1074/jbc.M114.585828

URL: http://www.jbc.org/content/290/10/6179

URL: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4358257/

Colecciones

Articulos(CCT - PATAGONIA NORTE)
Articulos de CTRO.CIENTIFICO TECNOL.CONICET - PATAGONIA NORTE

Articulos(IQUIBICEN)
Articulos de INSTITUTO DE QUIMICA BIOLOGICA DE LA FACULTAD DE CS. EXACTAS Y NATURALES

Articulos(IQUIFIB)
Articulos de INST.DE QUIMICA Y FISICO-QUIMICA BIOLOGICAS "PROF. ALEJANDRO C. PALADINI"

Citación

Pignataro, María Florencia; Dodes Traian, Martín Miguel; Gonzalez Flecha, Francisco Luis; Sica, Mauricio Pablo; Mangialavori, Irene Cecilia; et al.; Modulation of plasma membrane Ca2-ATPase by neutral Phospholipids: effect of the micelle-vesicle transition and the bilayer thickness; American Society For Biochemistry And Molecular Biology; Journal Of Biological Chemistry; 290; 10; 1-2015; 6179-6190

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