{"title":"Hetero-oligomeric interaction as a new regulatory mechanism for protein arginine methyltransferases.","authors":"Angela A Bae, Y George Zheng","doi":"10.1042/BST20240242","DOIUrl":null,"url":null,"abstract":"<p><p>Protein arginine methylation is a versatile post-translational protein modification that has notable cellular roles such as transcriptional activation or repression, cell signaling, cell cycle regulation, and DNA damage response. However, in spite of their extensive significance in the biological system, there is still a significant gap in understanding of the entire function of the protein arginine methyltransferases (PRMTs). It has been well-established that PRMTs form homo-oligomeric complexes to be catalytically active, but in recent years, several studies have showcased evidence that different members of PRMTs can have cross-talk with one another to form hetero-oligomeric complexes. Additionally, these heteromeric complexes have distinct roles separate from their homomeric counterparts. Here, we review and highlight the discovery of the heterodimerization of PRMTs and discuss the biological implications of these hetero-oligomeric interactions.</p>","PeriodicalId":8841,"journal":{"name":"Biochemical Society transactions","volume":" ","pages":"2193-2201"},"PeriodicalIF":3.8000,"publicationDate":"2024-10-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochemical Society transactions","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1042/BST20240242","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
Protein arginine methylation is a versatile post-translational protein modification that has notable cellular roles such as transcriptional activation or repression, cell signaling, cell cycle regulation, and DNA damage response. However, in spite of their extensive significance in the biological system, there is still a significant gap in understanding of the entire function of the protein arginine methyltransferases (PRMTs). It has been well-established that PRMTs form homo-oligomeric complexes to be catalytically active, but in recent years, several studies have showcased evidence that different members of PRMTs can have cross-talk with one another to form hetero-oligomeric complexes. Additionally, these heteromeric complexes have distinct roles separate from their homomeric counterparts. Here, we review and highlight the discovery of the heterodimerization of PRMTs and discuss the biological implications of these hetero-oligomeric interactions.
蛋白质精氨酸甲基化是一种多功能的蛋白质翻译后修饰,在细胞中具有显著的作用,如转录激活或抑制、细胞信号传导、细胞周期调控和 DNA 损伤反应。然而,尽管蛋白质精氨酸甲基转移酶(PRMTs)在生物系统中具有广泛的意义,但人们对其整个功能的了解仍有很大差距。人们已经确定,精氨酸甲基转移酶形成同源异构体复合物才能发挥催化活性,但近年来的一些研究表明,精氨酸甲基转移酶的不同成员之间可以相互交织,形成异源异构体复合物。此外,这些异构复合物具有不同于同构复合物的作用。在此,我们回顾并重点介绍 PRMTs 异源二聚体化的发现,并讨论这些异源同源异构体相互作用的生物学意义。
期刊介绍:
Biochemical Society Transactions is the reviews journal of the Biochemical Society. Publishing concise reviews written by experts in the field, providing a timely snapshot of the latest developments across all areas of the molecular and cellular biosciences.
Elevating our authors’ ideas and expertise, each review includes a perspectives section where authors offer comment on the latest advances, a glimpse of future challenges and highlighting the importance of associated research areas in far broader contexts.