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. 2023 Feb;597(4):504-514.
doi: 10.1002/1873-3468.14558. Epub 2022 Dec 21.

Yeast Sec14-like lipid transfer proteins Pdr16 and Pdr17 bind and transfer the ergosterol precursor lanosterol in addition to phosphatidylinositol

Dominik Šťastný  1 , Lívia Petrisková  1 , Dana Tahotná  1 , Jacob Bauer  2 , Lucia Pokorná  1 , Roman Holič  1 , Martin Valachovič  1 , Vladimír Pevala  2 , Shamshad Cockcroft  3 , Peter Griač  1
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Free article

Yeast Sec14-like lipid transfer proteins Pdr16 and Pdr17 bind and transfer the ergosterol precursor lanosterol in addition to phosphatidylinositol

Dominik Šťastný et al. FEBS Lett. 2023 Feb.
Free article

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.

Keywords: Saccharomyces cerevisiae; PITP; azol; cholesterol; ergosterol; lanosterol; lipid binding; phosphatidylinositol transfer.

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References

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