The Structure and Functions of PRMT5 in Human Diseases
Since the discovery of protein arginine methyltransferase 5 (PRMT5) and the resolution of its structure, an increasing number of papers have investigated and delineated the structural and functional role of PRMT5 in diseased conditions. PRMT5 is a type II arginine methyltransferase that catalyzes sy...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-10-01
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| Series: | Life |
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| Online Access: | https://www.mdpi.com/2075-1729/11/10/1074 |
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| author | Aishat Motolani Matthew Martin Mengyao Sun Tao Lu |
| author_facet | Aishat Motolani Matthew Martin Mengyao Sun Tao Lu |
| author_sort | Aishat Motolani |
| collection | DOAJ |
| description | Since the discovery of protein arginine methyltransferase 5 (PRMT5) and the resolution of its structure, an increasing number of papers have investigated and delineated the structural and functional role of PRMT5 in diseased conditions. PRMT5 is a type II arginine methyltransferase that catalyzes symmetric dimethylation marks on histones and non-histone proteins. From gene regulation to human development, PRMT5 is involved in many vital biological functions in humans. The role of PRMT5 in various cancers is particularly well-documented, and investigations into the development of better PRMT5 inhibitors to promote tumor regression are ongoing. Notably, emerging studies have demonstrated the pathological contribution of PRMT5 in the progression of inflammatory diseases, such as diabetes, cardiovascular diseases, and neurodegenerative disorders. However, more research in this direction is needed. Herein, we critically review the position of PRMT5 in current literature, including its structure, mechanism of action, regulation, physiological and pathological relevance, and therapeutic strategies. |
| first_indexed | 2024-03-10T06:27:13Z |
| format | Article |
| id | doaj.art-b791295fb72e4884a47f4b02b3d11e33 |
| institution | Directory Open Access Journal |
| issn | 2075-1729 |
| language | English |
| last_indexed | 2024-03-10T06:27:13Z |
| publishDate | 2021-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Life |
| spelling | doaj.art-b791295fb72e4884a47f4b02b3d11e332023-11-22T18:53:09ZengMDPI AGLife2075-17292021-10-011110107410.3390/life11101074The Structure and Functions of PRMT5 in Human DiseasesAishat Motolani0Matthew Martin1Mengyao Sun2Tao Lu3Department of Pharmacology & Toxicology, Indiana University School of Medicine, Indianapolis, IN 46202, USADepartment of Pharmacology & Toxicology, Indiana University School of Medicine, Indianapolis, IN 46202, USADepartment of Pharmacology & Toxicology, Indiana University School of Medicine, Indianapolis, IN 46202, USADepartment of Pharmacology & Toxicology, Indiana University School of Medicine, Indianapolis, IN 46202, USASince the discovery of protein arginine methyltransferase 5 (PRMT5) and the resolution of its structure, an increasing number of papers have investigated and delineated the structural and functional role of PRMT5 in diseased conditions. PRMT5 is a type II arginine methyltransferase that catalyzes symmetric dimethylation marks on histones and non-histone proteins. From gene regulation to human development, PRMT5 is involved in many vital biological functions in humans. The role of PRMT5 in various cancers is particularly well-documented, and investigations into the development of better PRMT5 inhibitors to promote tumor regression are ongoing. Notably, emerging studies have demonstrated the pathological contribution of PRMT5 in the progression of inflammatory diseases, such as diabetes, cardiovascular diseases, and neurodegenerative disorders. However, more research in this direction is needed. Herein, we critically review the position of PRMT5 in current literature, including its structure, mechanism of action, regulation, physiological and pathological relevance, and therapeutic strategies.https://www.mdpi.com/2075-1729/11/10/1074PRMT5cancercardiovascular diseaseneurodegenerative diseasesdiabetesinflammation |
| spellingShingle | Aishat Motolani Matthew Martin Mengyao Sun Tao Lu The Structure and Functions of PRMT5 in Human Diseases Life PRMT5 cancer cardiovascular disease neurodegenerative diseases diabetes inflammation |
| title | The Structure and Functions of PRMT5 in Human Diseases |
| title_full | The Structure and Functions of PRMT5 in Human Diseases |
| title_fullStr | The Structure and Functions of PRMT5 in Human Diseases |
| title_full_unstemmed | The Structure and Functions of PRMT5 in Human Diseases |
| title_short | The Structure and Functions of PRMT5 in Human Diseases |
| title_sort | structure and functions of prmt5 in human diseases |
| topic | PRMT5 cancer cardiovascular disease neurodegenerative diseases diabetes inflammation |
| url | https://www.mdpi.com/2075-1729/11/10/1074 |
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