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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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Autor principal: Rathert, Philipp
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
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
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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.
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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
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