Cargando…
Effectors and effects of arginine methylation
Arginine methylation is a ubiquitous and relatively stable post-translational modification (PTM) that occurs in three types: monomethylarginine (MMA), asymmetric dimethylarginine (ADMA) and symmetric dimethylarginine (SDMA). Methylarginine marks are catalyzed by members of the protein arginine methy...
Autores principales: | , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Portland Press Ltd.
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10212539/ https://www.ncbi.nlm.nih.gov/pubmed/37013969 http://dx.doi.org/10.1042/BST20221147 |
_version_ | 1785047437364166656 |
---|---|
author | Wang, Yalong Bedford, Mark T. |
author_facet | Wang, Yalong Bedford, Mark T. |
author_sort | Wang, Yalong |
collection | PubMed |
description | Arginine methylation is a ubiquitous and relatively stable post-translational modification (PTM) that occurs in three types: monomethylarginine (MMA), asymmetric dimethylarginine (ADMA) and symmetric dimethylarginine (SDMA). Methylarginine marks are catalyzed by members of the protein arginine methyltransferases (PRMTs) family of enzymes. Substrates for arginine methylation are found in most cellular compartments, with RNA-binding proteins forming the majority of PRMT targets. Arginine methylation often occurs in intrinsically disordered regions of proteins, which impacts biological processes like protein–protein interactions and phase separation, to modulate gene transcription, mRNA splicing and signal transduction. With regards to protein–protein interactions, the major ‘readers’ of methylarginine marks are Tudor domain-containing proteins, although additional domain types and unique protein folds have also recently been identified as methylarginine readers. Here, we will assess the current ‘state-of-the-art' in the arginine methylation reader field. We will focus on the biological functions of the Tudor domain-containing methylarginine readers and address other domains and complexes that sense methylarginine marks. |
format | Online Article Text |
id | pubmed-10212539 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Portland Press Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-102125392023-05-26 Effectors and effects of arginine methylation Wang, Yalong Bedford, Mark T. Biochem Soc Trans Review Articles Arginine methylation is a ubiquitous and relatively stable post-translational modification (PTM) that occurs in three types: monomethylarginine (MMA), asymmetric dimethylarginine (ADMA) and symmetric dimethylarginine (SDMA). Methylarginine marks are catalyzed by members of the protein arginine methyltransferases (PRMTs) family of enzymes. Substrates for arginine methylation are found in most cellular compartments, with RNA-binding proteins forming the majority of PRMT targets. Arginine methylation often occurs in intrinsically disordered regions of proteins, which impacts biological processes like protein–protein interactions and phase separation, to modulate gene transcription, mRNA splicing and signal transduction. With regards to protein–protein interactions, the major ‘readers’ of methylarginine marks are Tudor domain-containing proteins, although additional domain types and unique protein folds have also recently been identified as methylarginine readers. Here, we will assess the current ‘state-of-the-art' in the arginine methylation reader field. We will focus on the biological functions of the Tudor domain-containing methylarginine readers and address other domains and complexes that sense methylarginine marks. Portland Press Ltd. 2023-04-26 2023-04-04 /pmc/articles/PMC10212539/ /pubmed/37013969 http://dx.doi.org/10.1042/BST20221147 Text en © 2023 The Author(s) https://creativecommons.org/licenses/by/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Review Articles Wang, Yalong Bedford, Mark T. Effectors and effects of arginine methylation |
title | Effectors and effects of arginine methylation |
title_full | Effectors and effects of arginine methylation |
title_fullStr | Effectors and effects of arginine methylation |
title_full_unstemmed | Effectors and effects of arginine methylation |
title_short | Effectors and effects of arginine methylation |
title_sort | effectors and effects of arginine methylation |
topic | Review Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10212539/ https://www.ncbi.nlm.nih.gov/pubmed/37013969 http://dx.doi.org/10.1042/BST20221147 |
work_keys_str_mv | AT wangyalong effectorsandeffectsofargininemethylation AT bedfordmarkt effectorsandeffectsofargininemethylation |