Yeast Sec14‐like lipid transfer proteins Pdr16 and Pdr17 bind and transfer the ergosterol precursor lanosterol in addition to phosphatidylinositol. Issue 4 (21st December 2022)
- Record Type:
- Journal Article
- Title:
- Yeast Sec14‐like lipid transfer proteins Pdr16 and Pdr17 bind and transfer the ergosterol precursor lanosterol in addition to phosphatidylinositol. Issue 4 (21st December 2022)
- Main Title:
- Yeast Sec14‐like lipid transfer proteins Pdr16 and Pdr17 bind and transfer the ergosterol precursor lanosterol in addition to phosphatidylinositol
- Authors:
- Šťastný, Dominik
Petrisková, Lívia
Tahotná, Dana
Bauer, Jacob
Pokorná, Lucia
Holič, Roman
Valachovič, Martin
Pevala, Vladimír
Cockcroft, Shamshad
Griač, Peter - Abstract:
- 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. Abstract : Yeast Sec14 family phosphatidylinositol (PI) transfer proteins Pdr16p (Sfh3p) and Pdr17p (Sfh4p) possess high‐affinity binding and transfer towards lanosterol. In addition, a pdr16Δpdr17Δ double mutant had a significantly increased level of cellular lanosterol. Based on the lipid profiles of 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.
- Is Part Of:
- FEBS letters. Volume 597:Issue 4(2023)
- Journal:
- FEBS letters
- Issue:
- Volume 597:Issue 4(2023)
- Issue Display:
- Volume 597, Issue 4 (2023)
- Year:
- 2023
- Volume:
- 597
- Issue:
- 4
- Issue Sort Value:
- 2023-0597-0004-0000
- Page Start:
- 504
- Page End:
- 514
- Publication Date:
- 2022-12-21
- Subjects:
- azol -- cholesterol -- ergosterol -- lanosterol -- lipid binding -- phosphatidylinositol transfer -- PITP -- Saccharomyces cerevisiae
Biochemistry -- Periodicals
Biophysics -- Periodicals
Molecular biology -- Periodicals
Biochimie -- Périodiques
Biochemistry
Biophysics
Molecular biology
Periodicals
572.05 - Journal URLs:
- http://www.sciencedirect.com/science/journal/00145793 ↗
http://febs.onlinelibrary.wiley.com/hub/journal/10.1002/(ISSN)1873-3468/ ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1002/1873-3468.14558 ↗
- Languages:
- English
- ISSNs:
- 0014-5793
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3901.600000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 26066.xml