Non-histone lactylation: unveiling its functional significance
Lactylation, a newly discovered protein posttranslational modification (PTM) in 2019, primarily occurs on lysine residues. Lactylation of histones was initially identified, and subsequent studies have increasingly demonstrated its widespread presence on non-histone proteins. Recently, high-throughpu...
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Frontiers Media S.A.
2025-01-01
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| Series: | Frontiers in Cell and Developmental Biology |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fcell.2025.1535611/full |
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| author | Pusong Shi Yongjie Ma Yongjie Ma Yongjie Ma Yongjie Ma Yongjie Ma Shaolu Zhang Shaolu Zhang Shaolu Zhang Shaolu Zhang Shaolu Zhang |
| author_facet | Pusong Shi Yongjie Ma Yongjie Ma Yongjie Ma Yongjie Ma Yongjie Ma Shaolu Zhang Shaolu Zhang Shaolu Zhang Shaolu Zhang Shaolu Zhang |
| author_sort | Pusong Shi |
| collection | DOAJ |
| description | Lactylation, a newly discovered protein posttranslational modification (PTM) in 2019, primarily occurs on lysine residues. Lactylation of histones was initially identified, and subsequent studies have increasingly demonstrated its widespread presence on non-histone proteins. Recently, high-throughput proteomics studies have identified a large number of lactylated proteins and sites, revealing their global regulatory role in disease development. Notably, this modification is catalyzed by lactyltransferase and reversed by delactylase, with numerous new enzymes, such as AARS1/2, reported to be involved. Specifically, these studies have revealed how lactylation exerts its influence through alterations in protein spatial conformation, molecular interactions, enzyme activity and subcellular localization. Indeed, lactylation is implicated in various physiological and pathological processes, including tumor development, cardiovascular and cerebrovascular diseases, immune cell activation and psychiatric disorders. This review provides the latest advancements in research on the regulatory roles of non-histone protein lactylation, highlighting its crucial scientific importance for future studies. |
| format | Article |
| id | doaj-art-ff226285e0d6482f9cccdfb5bd0dab22 |
| institution | Kabale University |
| issn | 2296-634X |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Cell and Developmental Biology |
| spelling | doaj-art-ff226285e0d6482f9cccdfb5bd0dab222025-01-24T07:14:01ZengFrontiers Media S.A.Frontiers in Cell and Developmental Biology2296-634X2025-01-011310.3389/fcell.2025.15356111535611Non-histone lactylation: unveiling its functional significancePusong Shi0Yongjie Ma1Yongjie Ma2Yongjie Ma3Yongjie Ma4Yongjie Ma5Shaolu Zhang6Shaolu Zhang7Shaolu Zhang8Shaolu Zhang9Shaolu Zhang10School of Integrative Medicine, Tianjin University of Traditional Chinese Medicine, Tianjin, ChinaLaboratory of Cancer Cell Biology, Tianjin Medical University Cancer Institute and Hospital, National Clinical Research Center for Cancer, Tianjin, ChinaTianjin’s Clinical Research Center for Cancer, Tianjin, ChinaKey Laboratory of Breast Cancer Prevention and Therapy, Ministry of Education, Tianjin Medical University, Tianjin, ChinaKey Laboratory of Cancer Prevention and Therapy, Tianjin, ChinaState Key Laboratory of Druggability Evaluation and Systematic Translational Medicine, Tianjin, ChinaLaboratory of Cancer Cell Biology, Tianjin Medical University Cancer Institute and Hospital, National Clinical Research Center for Cancer, Tianjin, ChinaTianjin’s Clinical Research Center for Cancer, Tianjin, ChinaKey Laboratory of Breast Cancer Prevention and Therapy, Ministry of Education, Tianjin Medical University, Tianjin, ChinaKey Laboratory of Cancer Prevention and Therapy, Tianjin, ChinaState Key Laboratory of Druggability Evaluation and Systematic Translational Medicine, Tianjin, ChinaLactylation, a newly discovered protein posttranslational modification (PTM) in 2019, primarily occurs on lysine residues. Lactylation of histones was initially identified, and subsequent studies have increasingly demonstrated its widespread presence on non-histone proteins. Recently, high-throughput proteomics studies have identified a large number of lactylated proteins and sites, revealing their global regulatory role in disease development. Notably, this modification is catalyzed by lactyltransferase and reversed by delactylase, with numerous new enzymes, such as AARS1/2, reported to be involved. Specifically, these studies have revealed how lactylation exerts its influence through alterations in protein spatial conformation, molecular interactions, enzyme activity and subcellular localization. Indeed, lactylation is implicated in various physiological and pathological processes, including tumor development, cardiovascular and cerebrovascular diseases, immune cell activation and psychiatric disorders. This review provides the latest advancements in research on the regulatory roles of non-histone protein lactylation, highlighting its crucial scientific importance for future studies.https://www.frontiersin.org/articles/10.3389/fcell.2025.1535611/fullnon-histonelactylationposttranslational modificationlysinemetabolism |
| spellingShingle | Pusong Shi Yongjie Ma Yongjie Ma Yongjie Ma Yongjie Ma Yongjie Ma Shaolu Zhang Shaolu Zhang Shaolu Zhang Shaolu Zhang Shaolu Zhang Non-histone lactylation: unveiling its functional significance Frontiers in Cell and Developmental Biology non-histone lactylation posttranslational modification lysine metabolism |
| title | Non-histone lactylation: unveiling its functional significance |
| title_full | Non-histone lactylation: unveiling its functional significance |
| title_fullStr | Non-histone lactylation: unveiling its functional significance |
| title_full_unstemmed | Non-histone lactylation: unveiling its functional significance |
| title_short | Non-histone lactylation: unveiling its functional significance |
| title_sort | non histone lactylation unveiling its functional significance |
| topic | non-histone lactylation posttranslational modification lysine metabolism |
| url | https://www.frontiersin.org/articles/10.3389/fcell.2025.1535611/full |
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