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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1982 Jul;79(14):4280–4284. doi: 10.1073/pnas.79.14.4280

alpha-Actinin interacts specifically with model membranes containing glycerides and fatty acids.

R K Meyer, H Schindler, M M Burger
PMCID: PMC346654  PMID: 6956857

Abstract

A method was developed to identify specific protein-lipid interactions of complex lipid mixtures and to assess their effect upon the arrangement of such complexes in monolayers at an air-water interface. Its application to striated muscle alpha-actinin revealed that just two lipids selectively interact with alpha-actinin. One molecule of glyceride and one molecule of fatty acid were found to be associated in a constant stoichiometry with one molecule of the alpha-actinin dimer. In the presence of both glycerides and fatty acids unexpectedly rigid monolayer areas formed. This lipid specificity could be confirmed by brief protease digestion of alpha-actinin liposome mixtures followed by peptide analysis; the peptide patterns of alpha-actinin depended on the presence or absence of only these two lipids. Possible implications of these findings are discussed in the context of Z-line formation.

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Selected References

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