{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Jarome TJ"],"funding":["NIMH NIH HHS","National Institute of Mental Health","NINDS NIH HHS","NIGMS NIH HHS"],"pagination":["1176-1187"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8178164"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["89(12)"],"pubmed_abstract":["<h4>Background</h4>Posttranslational histone modifications play a critical role in the regulation of gene transcription underlying synaptic plasticity and memory formation. One such epigenetic change is histone ubiquitination, a process that is mediated by the ubiquitin-proteasome system in a manner similar to that by which proteins are normally targeted for degradation. However, histone ubiquitination mechanisms are poorly understood in the brain and in learning. In this article, we describe a new role for the ubiquitin-proteasome system in histone crosstalk, showing that learning-induced monoubiquitination of histone H2B (H2Bubi) is required for increases in the transcriptionally active H3 lysine 4 trimethylation (H3K4me3) mark at learning-related genes in the hippocampus.<h4>Methods</h4"],"journal":["Biological psychiatry"],"pubmed_title":["Ubiquitination of Histone H2B by Proteasome Subunit RPT6 Controls Histone Methylation Chromatin Dynamics During Memory Formation."],"pmcid":["PMC8178164"],"funding_grant_id":["R56 MH097909","K99 MH082106","T32 GM008361","T32 NS061788","R01 MH097909","R00 MH082106","R25 NS089463","T32 NS095775","F30 NS100340"],"pubmed_authors":["Webb WM","Hatch KM","Navabpour S","Butler AA","Lubin FD","Perez GA","Farrell K","Wang J","Jarome TJ","Martin K","Hauser RM","McFadden T","Musaus M"],"additional_accession":[]},"is_claimable":false,"name":"Ubiquitination of Histone H2B by Proteasome Subunit RPT6 Controls Histone Methylation Chromatin Dynamics During Memory Formation.","description":"<h4>Background</h4>Posttranslational histone modifications play a critical role in the regulation of gene transcription underlying synaptic plasticity and memory formation. One such epigenetic change is histone ubiquitination, a process that is mediated by the ubiquitin-proteasome system in a manner similar to that by which proteins are normally targeted for degradation. However, histone ubiquitination mechanisms are poorly understood in the brain and in learning. In this article, we describe a new role for the ubiquitin-proteasome system in histone crosstalk, showing that learning-induced monoubiquitination of histone H2B (H2Bubi) is required for increases in the transcriptionally active H3 lysine 4 trimethylation (H3K4me3) mark at learning-related genes in the hippocampus.<h4>Methods</h4","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Jun","modification":"2026-05-09T03:20:40.661Z","creation":"2025-04-04T22:15:22.95Z"},"accession":"S-EPMC8178164","cross_references":{"pubmed":["33934885"],"doi":["10.1016/j.biopsych.2020.12.029"]}}