<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Topchu I</submitter><funding>NIDCR NIH HHS</funding><funding>U.S. Department of Defense</funding><funding>National Cancer Institute</funding><funding>NCI NIH HHS</funding><funding>U.S. Army Medical Research Acquisition Activity</funding><funding>National Institutes of Health</funding><funding>Prostate Cancer Foundation</funding><funding>Feinberg School of Medicine</funding><funding>NIH HHS</funding><pagination>285</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9520630</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>79(6)</volume><pubmed_abstract>NSD1, NSD2, and NSD3 constitute the nuclear receptor-binding SET Domain (NSD) family of histone 3 lysine 36 (H3K36) methyltransferases. These structurally similar enzymes mono- and di-methylate H3K36, which contribute to the maintenance of chromatin integrity and regulate the expression of genes that control cell division, apoptosis, DNA repair, and epithelial-mesenchymal transition (EMT). Aberrant expression or mutation of members of the NSD family is associated with developmental defects and the occurrence of some types of cancer. In this review, we discuss the effect of alterations in NSDs on cancer patient's prognosis and response to treatment. We summarize the current understanding of the biological functions of NSD proteins, focusing on their activities and the role in the formation </pubmed_abstract><journal>Cellular and molecular life sciences : CMLS</journal><pubmed_title>The role of NSD1, NSD2, and NSD3 histone methyltransferases in solid tumors.</pubmed_title><pmcid>PMC9520630</pmcid><funding_grant_id>W81XWH2110487</funding_grant_id><funding_grant_id>R01 CA227918</funding_grant_id><funding_grant_id>Translational Bridge Award</funding_grant_id><funding_grant_id>P30 CA006927</funding_grant_id><funding_grant_id>R01CA227918</funding_grant_id><funding_grant_id>R01 CA218802</funding_grant_id><funding_grant_id>2017CHAL2008</funding_grant_id><funding_grant_id>W81XWH-17-1-0405</funding_grant_id><funding_grant_id>P30 CA060553</funding_grant_id><funding_grant_id>1P50 DE030707-01</funding_grant_id><funding_grant_id>P50 DE030707</funding_grant_id><funding_grant_id>W81XWH-17-1-0578</funding_grant_id><funding_grant_id>R01 DE027809</funding_grant_id><pubmed_authors>Golemis E</pubmed_authors><pubmed_authors>Pangeni RP</pubmed_authors><pubmed_authors>Bychkov I</pubmed_authors><pubmed_authors>Miller SA</pubmed_authors><pubmed_authors>Boumber Y</pubmed_authors><pubmed_authors>Yu J</pubmed_authors><pubmed_authors>Topchu I</pubmed_authors><pubmed_authors>Izumchenko E</pubmed_authors><pubmed_authors>Karanicolas J</pubmed_authors></additional><is_claimable>false</is_claimable><name>The role of NSD1, NSD2, and NSD3 histone methyltransferases in solid tumors.</name><description>NSD1, NSD2, and NSD3 constitute the nuclear receptor-binding SET Domain (NSD) family of histone 3 lysine 36 (H3K36) methyltransferases. These structurally similar enzymes mono- and di-methylate H3K36, which contribute to the maintenance of chromatin integrity and regulate the expression of genes that control cell division, apoptosis, DNA repair, and epithelial-mesenchymal transition (EMT). Aberrant expression or mutation of members of the NSD family is associated with developmental defects and the occurrence of some types of cancer. In this review, we discuss the effect of alterations in NSDs on cancer patient's prognosis and response to treatment. We summarize the current understanding of the biological functions of NSD proteins, focusing on their activities and the role in the formation </description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 May</publication><modification>2025-04-04T10:21:27.035Z</modification><creation>2025-02-19T02:38:08.47Z</creation></dates><accession>S-EPMC9520630</accession><cross_references><pubmed>35532818</pubmed><doi>10.1007/s00018-022-04321-2</doi></cross_references></HashMap>