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Lysine Crotonylation: An Emerging Player in DNA Damage Response
The DNA damage response (DDR) system plays an important role in maintaining genome stability and preventing related diseases. The DDR network comprises many proteins and posttranslational modifications (PTMs) to proteins, which work in a coordinated manner to counteract various genotoxic stresses. L...
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Published in: | Biomolecules (Basel, Switzerland) Switzerland), 2022-10, Vol.12 (10), p.1428 |
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description | The DNA damage response (DDR) system plays an important role in maintaining genome stability and preventing related diseases. The DDR network comprises many proteins and posttranslational modifications (PTMs) to proteins, which work in a coordinated manner to counteract various genotoxic stresses. Lysine crotonylation (Kcr) is a newly identified PTM occurring in both core histone and non-histone proteins in various organisms. This novel PTM is classified as a reversible acylation modification, which is regulated by a variety of acylases and deacylases and the intracellular crotonyl-CoA substrate concentration. Recent studies suggest that Kcr links cellular metabolism with gene regulation and is involved in numerous cellular processes. In this review, we summarize the regulatory mechanisms of Kcr and its functions in DDR, including its involvement in double-strand break (DSB)-induced transcriptional repression, DSB repair, and the DNA replication stress response. |
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The DDR network comprises many proteins and posttranslational modifications (PTMs) to proteins, which work in a coordinated manner to counteract various genotoxic stresses. Lysine crotonylation (Kcr) is a newly identified PTM occurring in both core histone and non-histone proteins in various organisms. This novel PTM is classified as a reversible acylation modification, which is regulated by a variety of acylases and deacylases and the intracellular crotonyl-CoA substrate concentration. Recent studies suggest that Kcr links cellular metabolism with gene regulation and is involved in numerous cellular processes. In this review, we summarize the regulatory mechanisms of Kcr and its functions in DDR, including its involvement in double-strand break (DSB)-induced transcriptional repression, DSB repair, and the DNA replication stress response.</description><identifier>ISSN: 2218-273X</identifier><identifier>EISSN: 2218-273X</identifier><identifier>DOI: 10.3390/biom12101428</identifier><language>eng</language><publisher>Basel: MDPI AG</publisher><subject>Acylation ; Cell cycle ; Crystal structure ; Deoxyribonucleic acid ; DNA ; DNA biosynthesis ; DNA damage ; DNA damage response (DDR) ; DNA double-strand break (DSB) ; DNA repair ; DNA replication stress response ; Double-strand break repair ; Enzymes ; Epigenetics ; Fatty acids ; Gene regulation ; Gene silencing ; Genetic aspects ; Genomes ; Genotoxicity ; Health aspects ; Histones ; Lysine ; lysine crotonylation ; Mammals ; Medical research ; Medicine, Experimental ; Metabolism ; Metabolites ; Oxidation ; Phosphorylation ; Post-translational modification ; Proteins ; Review</subject><ispartof>Biomolecules (Basel, Switzerland), 2022-10, Vol.12 (10), p.1428</ispartof><rights>COPYRIGHT 2022 MDPI AG</rights><rights>2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2022 by the authors. 2022</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c522t-9654b2af94957556add1c5fff6479284bd6bf18517cf33573c0f9246f907a3443</citedby><cites>FETCH-LOGICAL-c522t-9654b2af94957556add1c5fff6479284bd6bf18517cf33573c0f9246f907a3443</cites><orcidid>0000-0003-3751-3283</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/2728437293/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2728437293?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,37013,44590,53791,53793,75126</link.rule.ids></links><search><creatorcontrib>Zhao, Yuqin</creatorcontrib><creatorcontrib>Hao, Shuailin</creatorcontrib><creatorcontrib>Wu, Wenchi</creatorcontrib><creatorcontrib>Li, Youhang</creatorcontrib><creatorcontrib>Hou, Kaiping</creatorcontrib><creatorcontrib>Liu, Yu</creatorcontrib><creatorcontrib>Cui, Wei</creatorcontrib><creatorcontrib>Xu, Xingzhi</creatorcontrib><creatorcontrib>Wang, Hailong</creatorcontrib><title>Lysine Crotonylation: An Emerging Player in DNA Damage Response</title><title>Biomolecules (Basel, Switzerland)</title><description>The DNA damage response (DDR) system plays an important role in maintaining genome stability and preventing related diseases. The DDR network comprises many proteins and posttranslational modifications (PTMs) to proteins, which work in a coordinated manner to counteract various genotoxic stresses. Lysine crotonylation (Kcr) is a newly identified PTM occurring in both core histone and non-histone proteins in various organisms. This novel PTM is classified as a reversible acylation modification, which is regulated by a variety of acylases and deacylases and the intracellular crotonyl-CoA substrate concentration. Recent studies suggest that Kcr links cellular metabolism with gene regulation and is involved in numerous cellular processes. 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The DDR network comprises many proteins and posttranslational modifications (PTMs) to proteins, which work in a coordinated manner to counteract various genotoxic stresses. Lysine crotonylation (Kcr) is a newly identified PTM occurring in both core histone and non-histone proteins in various organisms. This novel PTM is classified as a reversible acylation modification, which is regulated by a variety of acylases and deacylases and the intracellular crotonyl-CoA substrate concentration. Recent studies suggest that Kcr links cellular metabolism with gene regulation and is involved in numerous cellular processes. In this review, we summarize the regulatory mechanisms of Kcr and its functions in DDR, including its involvement in double-strand break (DSB)-induced transcriptional repression, DSB repair, and the DNA replication stress response.</abstract><cop>Basel</cop><pub>MDPI AG</pub><doi>10.3390/biom12101428</doi><orcidid>https://orcid.org/0000-0003-3751-3283</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Acylation Cell cycle Crystal structure Deoxyribonucleic acid DNA DNA biosynthesis DNA damage DNA damage response (DDR) DNA double-strand break (DSB) DNA repair DNA replication stress response Double-strand break repair Enzymes Epigenetics Fatty acids Gene regulation Gene silencing Genetic aspects Genomes Genotoxicity Health aspects Histones Lysine lysine crotonylation Mammals Medical research Medicine, Experimental Metabolism Metabolites Oxidation Phosphorylation Post-translational modification Proteins Review |
title | Lysine Crotonylation: An Emerging Player in DNA Damage Response |
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