title: Lipid traffic: Osh4p makes an unexpected exchange.
abstract: A new study in this issue (De Saint-Jean et al. 2011. J. Cell Biol. http://dx.doi.org/jcb.201104062) reveals that the sterol transfer protein Osh4p can also transport the signaling phospholipid phosphatidylinositol 4-phosphate (PI(4)P), which binds to the same site in Osh4p as sterol. This finding helps explain some previously published studies and also indicates that lipid/sterol exchange could contribute to establishing a sterol gradient in cells.
authors.affiliation: Institute of Ophthalmology, University College London, London EC1V 9EL, England, UK. tim.levine@ucl.ac.uk
authors.forename: Tim P
authors.initials: TP
authors.lastname: Levine
mesh_terms: D004875:Ergosterol / Q000031:analogs & derivatives* / Q000737:chemistry; D008051:Lipid Bilayers / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry*; D018129:Phosphatidylinositol Phosphates / Q000737:chemistry*; D011987:Receptors, Steroid / Q000737:chemistry*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D000098825:Oxysterol Binding Proteins
chemical_list: D004875:Ergosterol; D008051:Lipid Bilayers; D008565:Membrane Proteins; D018129:Phosphatidylinositol Phosphates; D011987:Receptors, Steroid; D029701:Saccharomyces cerevisiae Proteins; C087901:KES1 protein, S cerevisiae; D000098825:Oxysterol Binding Proteins; C037178:phosphatidylinositol 4-phosphate; C010905:dehydroergosterol