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Protein acylation: mechanisms, biological functions and therapeutic targets

Metabolic reprogramming is involved in the pathogenesis of not only cancers but also neurodegenerative diseases, cardiovascular diseases, and infectious diseases. With the progress of metabonomics and proteomics, metabolites have been found to affect protein acylations through providing acyl groups...

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Autores principales: Shang, Shuang, Liu, Jing, Hua, Fang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9797573/
https://www.ncbi.nlm.nih.gov/pubmed/36577755
http://dx.doi.org/10.1038/s41392-022-01245-y
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author Shang, Shuang
Liu, Jing
Hua, Fang
author_facet Shang, Shuang
Liu, Jing
Hua, Fang
author_sort Shang, Shuang
collection PubMed
description Metabolic reprogramming is involved in the pathogenesis of not only cancers but also neurodegenerative diseases, cardiovascular diseases, and infectious diseases. With the progress of metabonomics and proteomics, metabolites have been found to affect protein acylations through providing acyl groups or changing the activities of acyltransferases or deacylases. Reciprocally, protein acylation is involved in key cellular processes relevant to physiology and diseases, such as protein stability, protein subcellular localization, enzyme activity, transcriptional activity, protein–protein interactions and protein–DNA interactions. Herein, we summarize the functional diversity and mechanisms of eight kinds of nonhistone protein acylations in the physiological processes and progression of several diseases. We also highlight the recent progress in the development of inhibitors for acyltransferase, deacylase, and acylation reader proteins for their potential applications in drug discovery.
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spelling pubmed-97975732022-12-30 Protein acylation: mechanisms, biological functions and therapeutic targets Shang, Shuang Liu, Jing Hua, Fang Signal Transduct Target Ther Review Article Metabolic reprogramming is involved in the pathogenesis of not only cancers but also neurodegenerative diseases, cardiovascular diseases, and infectious diseases. With the progress of metabonomics and proteomics, metabolites have been found to affect protein acylations through providing acyl groups or changing the activities of acyltransferases or deacylases. Reciprocally, protein acylation is involved in key cellular processes relevant to physiology and diseases, such as protein stability, protein subcellular localization, enzyme activity, transcriptional activity, protein–protein interactions and protein–DNA interactions. Herein, we summarize the functional diversity and mechanisms of eight kinds of nonhistone protein acylations in the physiological processes and progression of several diseases. We also highlight the recent progress in the development of inhibitors for acyltransferase, deacylase, and acylation reader proteins for their potential applications in drug discovery. Nature Publishing Group UK 2022-12-29 /pmc/articles/PMC9797573/ /pubmed/36577755 http://dx.doi.org/10.1038/s41392-022-01245-y Text en © The Author(s) 2022 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 Review Article
Shang, Shuang
Liu, Jing
Hua, Fang
Protein acylation: mechanisms, biological functions and therapeutic targets
title Protein acylation: mechanisms, biological functions and therapeutic targets
title_full Protein acylation: mechanisms, biological functions and therapeutic targets
title_fullStr Protein acylation: mechanisms, biological functions and therapeutic targets
title_full_unstemmed Protein acylation: mechanisms, biological functions and therapeutic targets
title_short Protein acylation: mechanisms, biological functions and therapeutic targets
title_sort protein acylation: mechanisms, biological functions and therapeutic targets
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9797573/
https://www.ncbi.nlm.nih.gov/pubmed/36577755
http://dx.doi.org/10.1038/s41392-022-01245-y
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