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Hereditas(Beijing) ›› 2025, Vol. 47 ›› Issue (9): 967-978.doi: 10.16288/j.yczz.25-034

• Review • Previous Articles     Next Articles

AARS1/2: dual functions in protein translation and metabolic- immune regulation

Zongwang Zhang1,2,3(), Jingwei Xiong1,4()   

  1. 1. Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Institute of Molecular Medicine, College of Future Technology, Peking University, Beijing 100871, China
    2. Center for Life Sciences, Shaoxing Institute, Zhejiang University, Shaoxing 321000, China
    3. Zhejiang Provincial Key Laboratory of Cancer Molecular Cell Biology, Life Sciences Institute, Zhejiang University, Hangzhou 310058, China
    4. School of Basic Medical Sciences and The Second Affiliated Hospital, Jiangxi Medical College, Nanchang University, Nanchang 330031, China
  • Received:2025-02-08 Revised:2025-04-02 Online:2025-04-03 Published:2025-04-03
  • Contact: Jingwei Xiong E-mail:zhang_zw@zju.edu.cn;jingwei_xiong@pku.edu.cn
  • Supported by:
    National Key R&D Program of China(2023YFA1800600);National Natural Science Foundation of China(32230032)

Abstract:

Highly precise regulation of protein synthesis is critical for the homeostasis and functionality of living organisms. Alanyl-tRNA synthase (AARS1/2) plays a crucial role in this process. AARS1/2 are a class of enzymes that synthesize alanyl-tRNA in cells, participating in protein synthesis encoded by genes, and catalyzing the propionylation of lysine residues in proteins, thereby regulating protein function. This article reviews the research progress on the involvement of AARS1/2 in disease progression induced by protein mistranslation and in the regulation of the metabolic-immune interaction network, aiming to better understand the pathophysiological mechanisms of AARS1/2 and to provide a reference for the development of potential therapeutic drugs.

Key words: AARS1/2, protein translation, protein lactylation, tumor, metabolism