Lipid-protein Interactions with the Na,K-ATPase

Overview

Journal Chem Phys Lipids

Specialty Biochemistry

Date 2006 Apr 4

PMID 16580658

Citations 13

Authors

Mikael Esmann

Derek Marsh

Affiliations

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Abstract

Studies of lipid interactions with membranous Na,K-ATPase by using electron spin resonance spectroscopy in conjunction with spin-labelled lipids are reviewed. The lipid stoichiometry, selectivity and exchange dynamics at the lipid-protein interface can be determined, in addition to information on the configuration and rotational dynamics of the protein-associated lipid chains. These parameters, particularly the stoichiometry and selectivity, are related directly to the intramembranous structure of the Na,K-ATPase, and can be used to check the integrity of extensively trypsinised preparations.

Citing Articles

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General and specific interactions of the phospholipid bilayer with P-type ATPases.

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Membrane Lipid Microenvironment Modulates Thermodynamic Properties of the Na-K-ATPase in Branchial and Intestinal Epithelia in Euryhaline Fish .

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Effects of Iron Overload on the Activity of Na,K-ATPase and Lipid Profile of the Human Erythrocyte Membrane.

Sousa L, Garcia I, Costa T, Silva L, Reno C, Oliveira E PLoS One. 2015; 10(7):e0132852.

PMID: 26197432 PMC: 4510300. DOI: 10.1371/journal.pone.0132852.

Lipid Librations at the Interface with the Na,K-ATPase.

Guzzi R, Bartucci R, Esmann M, Marsh D Biophys J. 2015; 108(12):2825-32.

PMID: 26083922 PMC: 4472081. DOI: 10.1016/j.bpj.2015.05.004.