Substrate and Functional Diversity of Protein Lysine Post-translational Modifications

Author:

Hao Bingbing123ORCID,Chen Kaifeng12ORCID,Zhai Linhui145ORCID,Liu Muyin6,Liu Bin7ORCID,Tan Minjia124ORCID

Affiliation:

1. State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences , Shanghai 201203, China

2. University of Chinese Academy of Sciences , Beijing 100049, China

3. Tianjian Laboratory of Advanced Biomedical Sciences, Institute of Advanced Biomedical Sciences, Zhengzhou University , Zhengzhou 450001, China

4. Zhongshan Institute for Drug Discovery, Shanghai Institute of Materia Medica, Chinese Academy of Sciences , Zhongshan 528400, China

5. State Key Laboratory of Pharmaceutical Biotechnology, Nanjing University , Nanjing 210023, China

6. Department of Cardiology, Shanghai Institute of Cardiovascular Diseases, Zhongshan Hospital, Fudan University , Shanghai 200032, China

7. Jiangsu Key Laboratory of Marine Pharmaceutical Compound Screening, College of Pharmacy, Jiangsu Ocean University , Lianyungang 222005, China

Abstract

Abstract Lysine post-translational modifications (PTMs) are widespread and versatile protein PTMs that are involved in diverse biological processes by regulating the fundamental functions of histone and non-histone proteins. Dysregulation of lysine PTMs is implicated in many diseases, and targeting lysine PTM regulatory factors, including writers, erasers, and readers, has become an effective strategy for disease therapy. The continuing development of mass spectrometry (MS) technologies coupled with antibody-based affinity enrichment technologies greatly promotes the discovery and decoding of PTMs. The global characterization of lysine PTMs is crucial for deciphering the regulatory networks, molecular functions, and mechanisms of action of lysine PTMs. In this review, we focus on lysine PTMs, and provide a summary of the regulatory enzymes of diverse lysine PTMs and the proteomics advances in lysine PTMs by MS technologies. We also discuss the types and biological functions of lysine PTM crosstalks on histone and non-histone proteins and current druggable targets of lysine PTM regulatory factors for disease therapy.

Publisher

Oxford University Press (OUP)

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