Advances in Research on Protein Arginine Methyltransferase 2: Functions and Diseases

被引:1
|
作者
Min, Zhen-Qi [1 ]
Jiang, Ming-Jun [1 ]
Liu, Xi-Lian [2 ]
Yuan, Su-Peng [1 ]
Chen, Ping-An [1 ]
Wang, Chu-Hao [1 ]
Chen, Ya-Jun [2 ]
Dai, Xian-Peng [1 ]
机构
[1] Univ South China, Affiliated Hosp 2, Hengyang Med Sch, Dept Vasc Surg, POB 421001, Hengyang, Peoples R China
[2] Univ South China, Affiliated Hosp 2, Hengyang Med Sch, Dept Endocrinol, POB 421001, Hengyang, Peoples R China
来源
PROTEIN AND PEPTIDE LETTERS | 2024年 / 31卷 / 01期
关键词
PRMT2; epigenetic regulation; transcriptional regulation; malignancies; atherosclerosis; inflammation; RNA-POLYMERASE-II; MOLECULAR CYTOGENETIC CHARACTERIZATION; C-TERMINAL DOMAIN; HISTONE H3; IN-VIVO; SELECTIVE INHIBITOR; EXPRESSION ANALYSIS; PRENATAL-DIAGNOSIS; RING CHROMOSOME-21; STRUCTURAL BASIS;
D O I
10.2174/0109298665281395231211060535
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Protein arginine methylation stands as a prevalent post-translational modification process, exerting vital roles in cellular signal transduction, gene expression, and cell cycle regulation. Amidst the protein arginine methyltransferase (PRMT) family, PRMT2 stands as a less explored constituent. Nonetheless, its regulatory roles in transcriptional regulation, post-transcriptional modification, methylation activity regulation, immunoregulation, and developmental regulation have garnered attention. These capabilities enable PRMT2 to exert pivotal regulatory functions in certain malignancies, metabolic disorders, inflammatory diseases, and atherosclerosis. In this review, we highlight the structure and functions of PRMT2, emphasizing its association with diseases. We also discuss PRMT2 inhibitors and explore the potential for therapeutic targeting.
引用
收藏
页码:25 / 42
页数:18
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