A heat-sensitive Osh protein controls PI4P polarity
| Autor: | Angela Cadou, Gary H. C. Chung, Deike J. Omnus, Ffion B. Thomas, Andrew Vaughan, Nathaniel Soh, Christopher J. Stefan, Jakob M. Bader |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Cell division Phosphatidylinositol 4-phosphate Physiology Exocyst Saccharomyces cerevisiae Plant Science Biology General Biochemistry Genetics and Molecular Biology 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Phosphatidylinositol Phosphates Structural Biology Extracellular Secretion Phosphatidylinositol lcsh:QH301-705.5 Ecology Evolution Behavior and Systematics 030304 developmental biology 0303 health sciences Cell Membrane Cell Biology Lipid Metabolism Transport protein Protein Transport chemistry lcsh:Biology (General) Biophysics Carrier Proteins General Agricultural and Biological Sciences Oxysterol-binding protein 030217 neurology & neurosurgery Research Article Developmental Biology Biotechnology |
| Zdroj: | BMC Biology, Vol 18, Iss 1, Pp 1-21 (2020) BMC BIOLOGY BMC Biology |
| ISSN: | 1741-7007 |
| DOI: | 10.1186/s12915-020-0758-x |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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