Šťastný, D; Petrisková, L; Tahotná, D; Bauer, J; Pokorná, L; Holič, R; Valachovič, M; ... Griač, P; + view all Šťastný, D; Petrisková, L; Tahotná, D; Bauer, J; Pokorná, L; Holič, R; Valachovič, M; Pevala, V; Cockcroft, S; Griač, P; - view fewer (2022) Yeast Sec14-like lipid transfer proteins Pdr16 and Pdr17 bind and transfer the ergosterol precursor lanosterol in addition to phosphatidylinositol. FEBS Letters 10.1002/1873-3468.14558. (In press).

Text Stastny et al (2022) Pdr16 and Pdr17 transfer lanosterol (FEBS Lett).pdf - Accepted Version Access restricted to UCL open access staff until 9 December 2023. Download (1MB)

Abstract

Yeast Sec14-like phosphatidylinositol transfer proteins (PITPs) contain a hydrophobic cavity capable of accepting a single molecule of phosphatidylinositol (PI) or another molecule in a mutually exclusive manner. We report here that two yeast Sec14 family PITPs, Pdr16p (Sfh3p) and Pdr17p (Sfh4p), possess high-affinity binding and transfer towards lanosterol. To our knowledge, this is the first identification of lanosterol transfer proteins. In addition, a pdr16Δpdr17Δ double mutant had a significantly increased level of cellular lanosterol compared with the corresponding wild-type. Based on the lipid profiles of wild-type and pdr16Δpdr17Δ cells grown in aerobic and anaerobic conditions, we suggest that PI-lanosterol transfer proteins are important predominantly for the optimal functioning of the post-lanosterol part of sterol biosynthesis.

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