Journal
MOLECULAR BIOLOGY OF THE CELL
Volume 28, Issue 1, Pages 161-172Publisher
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E16-09-0668
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Funding
- Ontario Early Researcher Award
- Canada Research Chair Award
- Natural Sciences and Engineering Research Council
- Ryerson Health Research Fund Award
- Canadian Institutes of Health Research [125854]
- Ontario Graduate Scholarship
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Phosphoinositides (PIPs) are key regulators of membrane traffic and signaling. The interconversion of PIPs by lipid kinases and phosphatases regulates their functionality. Phosphatidylinositol (PI) and PIPs have a unique enrichment of 1-stearoyl-2-arachidonyl acyl species; however, the regulation and function of this specific acyl profile remains poorly understood. We examined the role of the PI acyltransferase LYCAT in control of PIPs and PIP-dependent membrane traffic. LYCAT silencing selectively perturbed the levels and localization of phosphatidylinositol-4,5-bisphosphate [PI(4,5)P-2] and phosphatidylinositol-3-phosphate and the membrane traffic dependent on these specific PIPs but was without effect on phosphatidylinositol- 4-phosphate or biosynthetic membrane traffic. The acyl profile of PI(4,5)P-2 was selectively altered in LYCAT-deficient cells, whereas LYCAT localized with phosphatidylinositol synthase. We propose that LYCAT remodels the acyl chains of PI, which is then channeled into PI(4,5)P-2. Our observations suggest that the PIP acyl chain profile may exert broad control of cell physiology.
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