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The acyltransferase LYCAT controls specific phosphoinositides and related membrane traffic

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 an...

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Autores principales: Bone, Leslie N., Dayam, Roya M., Lee, Minhyoung, Kono, Nozomu, Fairn, Gregory D., Arai, Hiroyuki, Botelho, Roberto J., Antonescu, Costin N.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5221620/
https://www.ncbi.nlm.nih.gov/pubmed/28035047
http://dx.doi.org/10.1091/mbc.E16-09-0668
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author Bone, Leslie N.
Dayam, Roya M.
Lee, Minhyoung
Kono, Nozomu
Fairn, Gregory D.
Arai, Hiroyuki
Botelho, Roberto J.
Antonescu, Costin N.
author_facet Bone, Leslie N.
Dayam, Roya M.
Lee, Minhyoung
Kono, Nozomu
Fairn, Gregory D.
Arai, Hiroyuki
Botelho, Roberto J.
Antonescu, Costin N.
author_sort Bone, Leslie N.
collection PubMed
description 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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spelling pubmed-52216202017-03-16 The acyltransferase LYCAT controls specific phosphoinositides and related membrane traffic Bone, Leslie N. Dayam, Roya M. Lee, Minhyoung Kono, Nozomu Fairn, Gregory D. Arai, Hiroyuki Botelho, Roberto J. Antonescu, Costin N. Mol Biol Cell Articles 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. The American Society for Cell Biology 2017-01-01 /pmc/articles/PMC5221620/ /pubmed/28035047 http://dx.doi.org/10.1091/mbc.E16-09-0668 Text en © 2017 Bone et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology.
spellingShingle Articles
Bone, Leslie N.
Dayam, Roya M.
Lee, Minhyoung
Kono, Nozomu
Fairn, Gregory D.
Arai, Hiroyuki
Botelho, Roberto J.
Antonescu, Costin N.
The acyltransferase LYCAT controls specific phosphoinositides and related membrane traffic
title The acyltransferase LYCAT controls specific phosphoinositides and related membrane traffic
title_full The acyltransferase LYCAT controls specific phosphoinositides and related membrane traffic
title_fullStr The acyltransferase LYCAT controls specific phosphoinositides and related membrane traffic
title_full_unstemmed The acyltransferase LYCAT controls specific phosphoinositides and related membrane traffic
title_short The acyltransferase LYCAT controls specific phosphoinositides and related membrane traffic
title_sort acyltransferase lycat controls specific phosphoinositides and related membrane traffic
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5221620/
https://www.ncbi.nlm.nih.gov/pubmed/28035047
http://dx.doi.org/10.1091/mbc.E16-09-0668
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