Structure and Function of Protein Arginine Methyltransferase PRMT7
PRMT7 is a member of the protein arginine methyltransferase (PRMT) family, which methylates a diverse set of substrates. Arginine methylation as a posttranslational modification regulates protein–protein and protein–nucleic acid interactions, and as such, has been implicated in various biological fu...
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| Format: | Article |
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MDPI AG
2021-07-01
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| Series: | Life |
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| Online Access: | https://www.mdpi.com/2075-1729/11/8/768 |
| _version_ | 1797523179755798528 |
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| author | Levon Halabelian Dalia Barsyte-Lovejoy |
| author_facet | Levon Halabelian Dalia Barsyte-Lovejoy |
| author_sort | Levon Halabelian |
| collection | DOAJ |
| description | PRMT7 is a member of the protein arginine methyltransferase (PRMT) family, which methylates a diverse set of substrates. Arginine methylation as a posttranslational modification regulates protein–protein and protein–nucleic acid interactions, and as such, has been implicated in various biological functions. PRMT7 is a unique, evolutionarily conserved PRMT family member that catalyzes the mono-methylation of arginine. The structural features, functional aspects, and compounds that inhibit PRMT7 are discussed here. Several studies have identified physiological substrates of PRMT7 and investigated the substrate methylation outcomes which link PRMT7 activity to the stress response and RNA biology. PRMT7-driven substrate methylation further leads to the biological outcomes of gene expression regulation, cell stemness, stress response, and cancer-associated phenotypes such as cell migration. Furthermore, organismal level phenotypes of PRMT7 deficiency have uncovered roles in muscle cell physiology, B cell biology, immunity, and brain function. This rapidly growing information on PRMT7 function indicates the critical nature of context-dependent functions of PRMT7 and necessitates further investigation of the PRMT7 interaction partners and factors that control PRMT7 expression and levels. Thus, PRMT7 is an important cellular regulator of arginine methylation in health and disease. |
| first_indexed | 2024-03-10T08:39:43Z |
| format | Article |
| id | doaj.art-17126664539547c8a32b2d3257dc30b7 |
| institution | Directory Open Access Journal |
| issn | 2075-1729 |
| language | English |
| last_indexed | 2024-03-10T08:39:43Z |
| publishDate | 2021-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Life |
| spelling | doaj.art-17126664539547c8a32b2d3257dc30b72023-11-22T08:22:37ZengMDPI AGLife2075-17292021-07-0111876810.3390/life11080768Structure and Function of Protein Arginine Methyltransferase PRMT7Levon Halabelian0Dalia Barsyte-Lovejoy1Structural Genomics Consortium, Temerty Faculty of Medicine, University of Toronto, Toronto, ON M5S 1A8, CanadaStructural Genomics Consortium, Temerty Faculty of Medicine, University of Toronto, Toronto, ON M5S 1A8, CanadaPRMT7 is a member of the protein arginine methyltransferase (PRMT) family, which methylates a diverse set of substrates. Arginine methylation as a posttranslational modification regulates protein–protein and protein–nucleic acid interactions, and as such, has been implicated in various biological functions. PRMT7 is a unique, evolutionarily conserved PRMT family member that catalyzes the mono-methylation of arginine. The structural features, functional aspects, and compounds that inhibit PRMT7 are discussed here. Several studies have identified physiological substrates of PRMT7 and investigated the substrate methylation outcomes which link PRMT7 activity to the stress response and RNA biology. PRMT7-driven substrate methylation further leads to the biological outcomes of gene expression regulation, cell stemness, stress response, and cancer-associated phenotypes such as cell migration. Furthermore, organismal level phenotypes of PRMT7 deficiency have uncovered roles in muscle cell physiology, B cell biology, immunity, and brain function. This rapidly growing information on PRMT7 function indicates the critical nature of context-dependent functions of PRMT7 and necessitates further investigation of the PRMT7 interaction partners and factors that control PRMT7 expression and levels. Thus, PRMT7 is an important cellular regulator of arginine methylation in health and disease.https://www.mdpi.com/2075-1729/11/8/768protein arginine methylationPRMT7epigeneticscancerimmunitypluripotency |
| spellingShingle | Levon Halabelian Dalia Barsyte-Lovejoy Structure and Function of Protein Arginine Methyltransferase PRMT7 Life protein arginine methylation PRMT7 epigenetics cancer immunity pluripotency |
| title | Structure and Function of Protein Arginine Methyltransferase PRMT7 |
| title_full | Structure and Function of Protein Arginine Methyltransferase PRMT7 |
| title_fullStr | Structure and Function of Protein Arginine Methyltransferase PRMT7 |
| title_full_unstemmed | Structure and Function of Protein Arginine Methyltransferase PRMT7 |
| title_short | Structure and Function of Protein Arginine Methyltransferase PRMT7 |
| title_sort | structure and function of protein arginine methyltransferase prmt7 |
| topic | protein arginine methylation PRMT7 epigenetics cancer immunity pluripotency |
| url | https://www.mdpi.com/2075-1729/11/8/768 |
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