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  A heat-sensitive Osh protein controls PI4P polarity

Omnus, D. J., Cadou, A., Thomas, F. B., Bader, J. M., Soh, N., Chung, G. H. C., et al. (2020). A heat-sensitive Osh protein controls PI4P polarity. BMC BIOLOGY, 18(1): 28. doi:10.1186/s12915-020-0758-x.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0006-3A8C-C Version Permalink: http://hdl.handle.net/21.11116/0000-0006-3A8D-B
Genre: Journal Article

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 Creators:
Omnus, Deike J.1, Author
Cadou, Angela1, Author
Thomas, Ffion B.1, Author
Bader, Jakob M.2, Author              
Soh, Nathaniel1, Author
Chung, Gary H. C.1, Author
Vaughan, Andrew N.1, Author
Stefan, Christopher J.1, Author
Affiliations:
1external, ou_persistent22              
2Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              

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Free keywords: OXYSTEROL-BINDING-PROTEIN; PLASMA-MEMBRANE; ER-PM; PHOSPHATIDYLINOSITOL 4-PHOSPHATE; STRUCTURAL INSIGHTS; PHASE-SEPARATION; DYNAMIC CHANGES; CELL-GROWTH; YEAST; VERSATILE
 Abstract: Background Phosphoinositide lipids provide spatial landmarks during polarized cell growth and migration. Yet how phosphoinositide gradients are oriented in response to extracellular cues and environmental conditions is not well understood. Here, we elucidate an unexpected mode of phosphatidylinositol 4-phosphate (PI4P) regulation in the control of polarized secretion. Results We show that PI4P is highly enriched at the plasma membrane of growing daughter cells in budding yeast where polarized secretion occurs. However, upon heat stress conditions that redirect secretory traffic, PI4P rapidly increases at the plasma membrane in mother cells resulting in a more uniform PI4P distribution. Precise control of PI4P distribution is mediated through the Osh (oxysterol-binding protein homology) proteins that bind and present PI4P to a phosphoinositide phosphatase. Interestingly, Osh3 undergoes a phase transition upon heat stress conditions, resulting in intracellular aggregates and reduced cortical localization. Both the Osh3 GOLD and ORD domains are sufficient to form heat stress-induced aggregates, indicating that Osh3 is highly tuned to heat stress conditions. Upon loss of Osh3 function, the polarized distribution of both PI4P and the exocyst component Exo70 are impaired. Thus, an intrinsically heat stress-sensitive PI4P regulatory protein controls the spatial distribution of phosphoinositide lipid metabolism to direct secretory trafficking as needed. Conclusions Our results suggest that control of PI4P metabolism by Osh proteins is a key determinant in the control of polarized growth and secretion.

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Language(s): eng - English
 Dates: 2020
 Publication Status: Published online
 Pages: 21
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: ISI: 000521069000001
DOI: 10.1186/s12915-020-0758-x
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Title: BMC BIOLOGY
Source Genre: Journal
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Publ. Info: CAMPUS, 4 CRINAN ST, LONDON N1 9XW, ENGLAND : BMC
Pages: - Volume / Issue: 18 (1) Sequence Number: 28 Start / End Page: - Identifier: -