Acyl-chain saturation regulates the order of phosphatidylinositol 4,5-bisphosphate nanodomains
Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P(2)) plays a critical role in the regulation of various plasma membrane processes and signaling pathways in eukaryotes. A significant amount of cellular resources are spent on maintaining the dominant 1-stearoyl-2-arachidonyl PI(4,5)P(2) acyl-chain comp...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9814227/ https://www.ncbi.nlm.nih.gov/pubmed/36697613 http://dx.doi.org/10.1038/s42004-021-00603-1 |
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author | Borges-Araújo, Luís Domingues, Marco M. Fedorov, Alexander Santos, Nuno C. Melo, Manuel N. Fernandes, Fábio |
author_facet | Borges-Araújo, Luís Domingues, Marco M. Fedorov, Alexander Santos, Nuno C. Melo, Manuel N. Fernandes, Fábio |
author_sort | Borges-Araújo, Luís |
collection | PubMed |
description | Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P(2)) plays a critical role in the regulation of various plasma membrane processes and signaling pathways in eukaryotes. A significant amount of cellular resources are spent on maintaining the dominant 1-stearoyl-2-arachidonyl PI(4,5)P(2) acyl-chain composition, while less abundant and more saturated species become more prevalent in response to specific stimuli, stress or aging. Here, we report the impact of acyl-chain structure on the biophysical properties of cation-induced PI(4,5)P(2) nanodomains. PI(4,5)P(2) species with increasing levels of acyl-chain saturation cluster in progressively more ordered nanodomains, culminating in the formation of gel-like nanodomains for fully saturated species. The formation of these gel-like domains was largely abrogated in the presence of 1-stearoyl-2-arachidonyl PI(4,5)P(2.) This is, to the best of our knowledge, the first report of the impact of PI(4,5)P(2) acyl-chain composition on cation-dependent nanodomain ordering, and provides important clues to the motives behind the enrichment of PI(4,5)P(2) with polyunsaturated acyl-chains. We also show how Ca(2+)-induced PI(4,5)P(2) nanodomains are able to generate local negative curvature, a phenomenon likely to play a role in membrane remodeling events. |
format | Online Article Text |
id | pubmed-9814227 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-98142272023-01-10 Acyl-chain saturation regulates the order of phosphatidylinositol 4,5-bisphosphate nanodomains Borges-Araújo, Luís Domingues, Marco M. Fedorov, Alexander Santos, Nuno C. Melo, Manuel N. Fernandes, Fábio Commun Chem Article Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P(2)) plays a critical role in the regulation of various plasma membrane processes and signaling pathways in eukaryotes. A significant amount of cellular resources are spent on maintaining the dominant 1-stearoyl-2-arachidonyl PI(4,5)P(2) acyl-chain composition, while less abundant and more saturated species become more prevalent in response to specific stimuli, stress or aging. Here, we report the impact of acyl-chain structure on the biophysical properties of cation-induced PI(4,5)P(2) nanodomains. PI(4,5)P(2) species with increasing levels of acyl-chain saturation cluster in progressively more ordered nanodomains, culminating in the formation of gel-like nanodomains for fully saturated species. The formation of these gel-like domains was largely abrogated in the presence of 1-stearoyl-2-arachidonyl PI(4,5)P(2.) This is, to the best of our knowledge, the first report of the impact of PI(4,5)P(2) acyl-chain composition on cation-dependent nanodomain ordering, and provides important clues to the motives behind the enrichment of PI(4,5)P(2) with polyunsaturated acyl-chains. We also show how Ca(2+)-induced PI(4,5)P(2) nanodomains are able to generate local negative curvature, a phenomenon likely to play a role in membrane remodeling events. Nature Publishing Group UK 2021-11-29 /pmc/articles/PMC9814227/ /pubmed/36697613 http://dx.doi.org/10.1038/s42004-021-00603-1 Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Borges-Araújo, Luís Domingues, Marco M. Fedorov, Alexander Santos, Nuno C. Melo, Manuel N. Fernandes, Fábio Acyl-chain saturation regulates the order of phosphatidylinositol 4,5-bisphosphate nanodomains |
title | Acyl-chain saturation regulates the order of phosphatidylinositol 4,5-bisphosphate nanodomains |
title_full | Acyl-chain saturation regulates the order of phosphatidylinositol 4,5-bisphosphate nanodomains |
title_fullStr | Acyl-chain saturation regulates the order of phosphatidylinositol 4,5-bisphosphate nanodomains |
title_full_unstemmed | Acyl-chain saturation regulates the order of phosphatidylinositol 4,5-bisphosphate nanodomains |
title_short | Acyl-chain saturation regulates the order of phosphatidylinositol 4,5-bisphosphate nanodomains |
title_sort | acyl-chain saturation regulates the order of phosphatidylinositol 4,5-bisphosphate nanodomains |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9814227/ https://www.ncbi.nlm.nih.gov/pubmed/36697613 http://dx.doi.org/10.1038/s42004-021-00603-1 |
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