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Versatility of ARD1/NAA10-mediated protein lysine acetylation
Post-translational modifications (PTMs) are chemical alterations that occur in proteins that play critical roles in various cellular functions. Lysine acetylation is an important PTM in eukaryotes, and it is catalyzed by lysine acetyltransferases (KATs). KATs transfer acetyl-coenzyme A to the intern...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6063952/ https://www.ncbi.nlm.nih.gov/pubmed/30054464 http://dx.doi.org/10.1038/s12276-018-0100-7 |
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author | Vo, Tam Thuy Lu Jeong, Chul-Ho Lee, Sooyeun Kim, Kyu-Won Ha, Eunyoung Seo, Ji Hae |
author_facet | Vo, Tam Thuy Lu Jeong, Chul-Ho Lee, Sooyeun Kim, Kyu-Won Ha, Eunyoung Seo, Ji Hae |
author_sort | Vo, Tam Thuy Lu |
collection | PubMed |
description | Post-translational modifications (PTMs) are chemical alterations that occur in proteins that play critical roles in various cellular functions. Lysine acetylation is an important PTM in eukaryotes, and it is catalyzed by lysine acetyltransferases (KATs). KATs transfer acetyl-coenzyme A to the internal lysine residue of substrate proteins. Arrest defective 1 (ARD1) is a member of the KAT family. Since the identification of its KAT activity 15 years ago, many studies have revealed that diverse cellular proteins are acetylated by ARD1. ARD1-mediated lysine acetylation is a key switch that regulates the enzymatic activities and biological functions of proteins and influences cell biology from development to pathology. In this review, we summarize protein lysine acetylation mediated by ARD1 and describe the biological meanings of this modification. |
format | Online Article Text |
id | pubmed-6063952 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-60639522018-08-08 Versatility of ARD1/NAA10-mediated protein lysine acetylation Vo, Tam Thuy Lu Jeong, Chul-Ho Lee, Sooyeun Kim, Kyu-Won Ha, Eunyoung Seo, Ji Hae Exp Mol Med Review Article Post-translational modifications (PTMs) are chemical alterations that occur in proteins that play critical roles in various cellular functions. Lysine acetylation is an important PTM in eukaryotes, and it is catalyzed by lysine acetyltransferases (KATs). KATs transfer acetyl-coenzyme A to the internal lysine residue of substrate proteins. Arrest defective 1 (ARD1) is a member of the KAT family. Since the identification of its KAT activity 15 years ago, many studies have revealed that diverse cellular proteins are acetylated by ARD1. ARD1-mediated lysine acetylation is a key switch that regulates the enzymatic activities and biological functions of proteins and influences cell biology from development to pathology. In this review, we summarize protein lysine acetylation mediated by ARD1 and describe the biological meanings of this modification. Nature Publishing Group UK 2018-07-27 /pmc/articles/PMC6063952/ /pubmed/30054464 http://dx.doi.org/10.1038/s12276-018-0100-7 Text en © The Author(s) 2018 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/. |
spellingShingle | Review Article Vo, Tam Thuy Lu Jeong, Chul-Ho Lee, Sooyeun Kim, Kyu-Won Ha, Eunyoung Seo, Ji Hae Versatility of ARD1/NAA10-mediated protein lysine acetylation |
title | Versatility of ARD1/NAA10-mediated protein lysine acetylation |
title_full | Versatility of ARD1/NAA10-mediated protein lysine acetylation |
title_fullStr | Versatility of ARD1/NAA10-mediated protein lysine acetylation |
title_full_unstemmed | Versatility of ARD1/NAA10-mediated protein lysine acetylation |
title_short | Versatility of ARD1/NAA10-mediated protein lysine acetylation |
title_sort | versatility of ard1/naa10-mediated protein lysine acetylation |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6063952/ https://www.ncbi.nlm.nih.gov/pubmed/30054464 http://dx.doi.org/10.1038/s12276-018-0100-7 |
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