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Open Biology: overview for special issue on dynamics of protein fatty acylation
Fatty acylation is a widespread form of protein modification that occurs on specific intracellular and secreted proteins. Beyond increasing hydrophobicity and the affinity of the modified protein for lipid bilayers, covalent attachment of a fatty acid exerts effects on protein localization, inter- a...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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The Royal Society
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8440031/ https://www.ncbi.nlm.nih.gov/pubmed/34520700 http://dx.doi.org/10.1098/rsob.210228 |
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author | Resh, Marilyn D. |
author_facet | Resh, Marilyn D. |
author_sort | Resh, Marilyn D. |
collection | PubMed |
description | Fatty acylation is a widespread form of protein modification that occurs on specific intracellular and secreted proteins. Beyond increasing hydrophobicity and the affinity of the modified protein for lipid bilayers, covalent attachment of a fatty acid exerts effects on protein localization, inter- and intramolecular interactions and signal transduction. As such, research into protein fatty acylation has been embraced by an extensive community of biologists. This special issue highlights advances at the forefront of the field, by focusing on two families of enzymes that catalyse post-translational protein fatty acylation, zDHHC palmitoyl acyltransferases and membrane-bound O-acyl transferases, and signalling pathways regulated by their fatty acylated protein substrates. The collected contributions catalogue the tremendous progress that has been made in enzyme and substrate identification. In addition, articles in this special issue provide insights into the pivotal functions of fatty acylated proteins in immune cell, insulin and EGF receptor-mediated signalling pathways. As selective inhibitors of protein fatty acyltransferases are generated, the future holds great promise for therapeutic targeting of fatty acyltransferases that play key roles in human disease. |
format | Online Article Text |
id | pubmed-8440031 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | The Royal Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-84400312021-09-17 Open Biology: overview for special issue on dynamics of protein fatty acylation Resh, Marilyn D. Open Biol Editorial Fatty acylation is a widespread form of protein modification that occurs on specific intracellular and secreted proteins. Beyond increasing hydrophobicity and the affinity of the modified protein for lipid bilayers, covalent attachment of a fatty acid exerts effects on protein localization, inter- and intramolecular interactions and signal transduction. As such, research into protein fatty acylation has been embraced by an extensive community of biologists. This special issue highlights advances at the forefront of the field, by focusing on two families of enzymes that catalyse post-translational protein fatty acylation, zDHHC palmitoyl acyltransferases and membrane-bound O-acyl transferases, and signalling pathways regulated by their fatty acylated protein substrates. The collected contributions catalogue the tremendous progress that has been made in enzyme and substrate identification. In addition, articles in this special issue provide insights into the pivotal functions of fatty acylated proteins in immune cell, insulin and EGF receptor-mediated signalling pathways. As selective inhibitors of protein fatty acyltransferases are generated, the future holds great promise for therapeutic targeting of fatty acyltransferases that play key roles in human disease. The Royal Society 2021-09-15 /pmc/articles/PMC8440031/ /pubmed/34520700 http://dx.doi.org/10.1098/rsob.210228 Text en © 2021 The Authors. https://creativecommons.org/licenses/by/4.0/Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, provided the original author and source are credited. |
spellingShingle | Editorial Resh, Marilyn D. Open Biology: overview for special issue on dynamics of protein fatty acylation |
title | Open Biology: overview for special issue on dynamics of protein fatty acylation |
title_full | Open Biology: overview for special issue on dynamics of protein fatty acylation |
title_fullStr | Open Biology: overview for special issue on dynamics of protein fatty acylation |
title_full_unstemmed | Open Biology: overview for special issue on dynamics of protein fatty acylation |
title_short | Open Biology: overview for special issue on dynamics of protein fatty acylation |
title_sort | open biology: overview for special issue on dynamics of protein fatty acylation |
topic | Editorial |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8440031/ https://www.ncbi.nlm.nih.gov/pubmed/34520700 http://dx.doi.org/10.1098/rsob.210228 |
work_keys_str_mv | AT reshmarilynd openbiologyoverviewforspecialissueondynamicsofproteinfattyacylation |