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Sec14p, the major phosphatidylinositol/ phosphatidylcholine transfer protein of Saccharomyces cerevisiae, is the prototypical member of the eukaryotic Sec14 protein superfamily. A hydrogen bond network links two structural motifs into a novel gating module that controls the major conformational dynamics of Sec14p, as depicted. These conformational dynamics regulate access of ligands to the hydrophobic binding pocket of Sec14-like proteins. The importance of the gating module in the general function of Sec14-like proteins is indicated by the presence of disease-causing mutations within the gating module substructures of human Sec14 proteins such as α-tocopherol transfer protein, cellular retinaldehyde binding protein, and neurofibromin-1. See the article by Ryan et al. on p. 1928 of this issue of MBC. (Image: Margaret M. Ryan, Department of Cell and Developmental Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC)

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