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Structure, Activity and Function of the NSD3 Protein Lysine Methyltransferase
NSD3 is one of six H3K36-specific lysine methyltransferases in metazoans, and the methylation of H3K36 is associated with active transcription. NSD3 is a member of the nuclear receptor-binding SET domain (NSD) family of histone methyltransferases together with NSD1 and NSD2, which generate mono- and...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8398374/ https://www.ncbi.nlm.nih.gov/pubmed/34440470 http://dx.doi.org/10.3390/life11080726 |
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author | Rathert, Philipp |
author_facet | Rathert, Philipp |
author_sort | Rathert, Philipp |
collection | PubMed |
description | NSD3 is one of six H3K36-specific lysine methyltransferases in metazoans, and the methylation of H3K36 is associated with active transcription. NSD3 is a member of the nuclear receptor-binding SET domain (NSD) family of histone methyltransferases together with NSD1 and NSD2, which generate mono- and dimethylated lysine on histone H3. NSD3 is mutated and hyperactive in some human cancers, but the biochemical mechanisms underlying such dysregulation are barely understood. In this review, the current knowledge of NSD3 is systematically reviewed. Finally, the molecular and functional characteristics of NSD3 in different tumor types according to the current research are summarized. |
format | Online Article Text |
id | pubmed-8398374 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-83983742021-08-29 Structure, Activity and Function of the NSD3 Protein Lysine Methyltransferase Rathert, Philipp Life (Basel) Review NSD3 is one of six H3K36-specific lysine methyltransferases in metazoans, and the methylation of H3K36 is associated with active transcription. NSD3 is a member of the nuclear receptor-binding SET domain (NSD) family of histone methyltransferases together with NSD1 and NSD2, which generate mono- and dimethylated lysine on histone H3. NSD3 is mutated and hyperactive in some human cancers, but the biochemical mechanisms underlying such dysregulation are barely understood. In this review, the current knowledge of NSD3 is systematically reviewed. Finally, the molecular and functional characteristics of NSD3 in different tumor types according to the current research are summarized. MDPI 2021-07-21 /pmc/articles/PMC8398374/ /pubmed/34440470 http://dx.doi.org/10.3390/life11080726 Text en © 2021 by the author. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Rathert, Philipp Structure, Activity and Function of the NSD3 Protein Lysine Methyltransferase |
title | Structure, Activity and Function of the NSD3 Protein Lysine Methyltransferase |
title_full | Structure, Activity and Function of the NSD3 Protein Lysine Methyltransferase |
title_fullStr | Structure, Activity and Function of the NSD3 Protein Lysine Methyltransferase |
title_full_unstemmed | Structure, Activity and Function of the NSD3 Protein Lysine Methyltransferase |
title_short | Structure, Activity and Function of the NSD3 Protein Lysine Methyltransferase |
title_sort | structure, activity and function of the nsd3 protein lysine methyltransferase |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8398374/ https://www.ncbi.nlm.nih.gov/pubmed/34440470 http://dx.doi.org/10.3390/life11080726 |
work_keys_str_mv | AT rathertphilipp structureactivityandfunctionofthensd3proteinlysinemethyltransferase |