{"doi":"10.1074/jbc.m105993200","title":"Functional Domains of Histone Deacetylase-3","abstract":"Post-translational modifications of histones, in general, and acetylation/deacetylation, in particular, can dramatically alter gene expression in eukaryotic cells. In humans, four highly homologous class I HDAC enzymes (HDAC1, HDAC2, HDAC3, and HDAC8) have been identified to date. Although HDAC3 shares some structural and functional similarities with other class I HDACs, it exists in multisubunit complexes separate and different from other known HDAC complexes, implying that individual HDACs might function in a distinct manner. In this current study, to understand further the cellular function of HDAC3 and to uncover possible unique roles this protein may have in gene regulation, we performed a detailed analysis of HDAC3 using deletion mutations. Surprisingly, we found that the non-conserved C-terminal region of HDAC3 is required for both deacetylase and transcriptional repression activity. In addition, we discovered that the central portion of the HDAC3 protein possesses a nuclear export signal, whereas the C-terminal part of HDAC3 contributes to the protein's localization in the nucleus. Finally, we found that HDAC3 forms oligomers in vitro and in vivo and that the N-terminal portion of HDAC3 is necessary for this property. These data indicate that HDAC3 comprises separate, non-overlapping domains that contribute to the unique properties and function of this protein.","journal":"Journal of Biological Chemistry","year":2002,"id":3035,"datarank":0.8245752337939805,"base_score":5.497168225293202,"endowment":5.497168225293202,"self_citation_contribution":0.8245752337939805,"citation_network_contribution":0.0,"self_endowment_contribution":0.8245752337939805,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":243,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":0.0577,"is_oa":true,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":"2002-03-01","fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":33870,"name":"Shih-Chang Tsai","orcid":null,"position":1,"is_corresponding":false},{"id":33871,"name":"Yu-Der Wen","orcid":null,"position":2,"is_corresponding":false},{"id":33872,"name":"György Fejér","orcid":"0000-0001-6761-0506","position":3,"is_corresponding":false},{"id":33873,"name":"Edward Seto","orcid":"0000-0001-7562-7316","position":4,"is_corresponding":false},{"id":33874,"name":"Wen‐Ming Yang","orcid":"0000-0002-5871-5979","position":5,"is_corresponding":false},{"id":33875,"name":"Shih‐Chang Tsai","orcid":"0000-0001-9018-607X","position":6,"is_corresponding":false},{"id":33876,"name":"Yu‐Der Wen","orcid":null,"position":7,"is_corresponding":false},{"id":33869,"name":"Wen-Ming Yang","orcid":null,"position":0,"is_corresponding":true}],"reference_count":69,"raw_metadata":{"citation_network_status":"fetched"},"created_at":"2026-03-01T18:20:47.508186Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}