Journal
JOURNAL OF CELLULAR AND MOLECULAR MEDICINE
Volume 25, Issue 15, Pages 7101-7109Publisher
WILEY
DOI: 10.1111/jcmm.16676
Keywords
histone; succinylation; desuccinylation; nucleosome
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Funding
- Science and Technology Planning Project of Guangdong Province, China [2017B020209001]
- Shenzhen Key Medical Discipline Construction Fund [SZXK011, SZXK059]
- Shenzhen Fund for Guangdong Provincial High-level Clinical Key Specialties [SZGSP001]
- Guangxi Key Laboratory of Metabolic Diseases Research [20-065-76]
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Lysine succinylation is a newly identified histone post-translational modification that influences nucleosomal structure, chromatin dynamics, gene expression, and several diseases. Studies on lysine succinylation of histones are ongoing, highlighting its potential as a target for disease treatment in the future.
Protein post-translational modifications (PTMs) of histones are ubiquitous regulatory mechanisms involved in many biological processes, including replication, transcription, DNA damage repair and ontogenesis. Recently, many short-chain acylation histone modifications have been identified by mass spectrometry (MS). Lysine succinylation (Ksuc or Ksucc) is a newly identified histone PTM that changes the chemical environment of histones and is similar to other acylation modifications; lysine succinylation appears to accumulate at transcriptional start sites and to correlate with gene expression. Although numerous studies are ongoing, there is a lack of reviews on the Ksuc of histones. Here, we review lysine succinylation sites on histones, including the chemical characteristics and the mechanism by which lysine succinylation influences nucleosomal structure, chromatin dynamics and several diseases and then discuss lysine succinylation regulation to identify theoretical and experimental proof of Ksuc on histones and in diseases to inspire further research into histone lysine succinylation as a target of disease treatment in the future.
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