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Membrane Lipid Requirements of the Lysine Transporter Lyp1 from Saccharomyces cerevisiae

van 't Klooster, J. S., Cheng, T-Y., Sikkema, H. R., Jeucken, A., Moody, D. B. & Poolman, B., 26-Jun-2020, In : Journal of Molecular Biology. 432, 14, p. 4023-4031 9 p.

Research output: Contribution to journalArticleAcademicpeer-review

Membrane lipids act as solvents and functional cofactors for integral membrane proteins. The yeast plasma membrane is unusual in that it may have a high lipid order, which coincides with low passive permeability for small molecules and a slow lateral diffusion of proteins. Yet, membrane proteins whose functions require altered conformation must have flexibility within membranes. We have determined the molecular composition of yeast plasma membrane lipids located within a defined diameter of model proteins, including the APC-superfamily lysine transporter Lyp1. We now use the composition of lipids that naturally surround Lyp1 to guide testing of lipids that support the normal functioning of the transporter, when reconstituted in vesicles of defined lipid composition. We find that phosphatidylserine and ergosterol are essential for Lyp1 function, and the transport activity displays a sigmoidal relationship with the concentration of these lipids. Non-bilayer lipids stimulate transport activity, but different types are interchangeable. Remarkably, Lyp1 requires a relatively high fraction of lipids with one or more unsaturated acyl chains. The transport data and predictions of the periprotein lipidome of Lyp1, support a new model in which a narrow band of lipids immediately surrounding the transmembrane stalk of a model protein allows conformational changes in the protein.

Original languageEnglish
Pages (from-to)4023-4031
Number of pages9
JournalJournal of Molecular Biology
Volume432
Issue number14
Early online date13-May-2020
Publication statusPublished - 26-Jun-2020

    Keywords

  • APC superfamily, Saccharomyces cerevisiae, amino acids, membrane transport, yeast plasma membrane

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