Base de dados : MEDLINE
Pesquisa : D12.776.580.219 [Categoria DeCS]
Referências encontradas : 576 [refinar]
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[PMID]:28460463
[Au] Autor:Almeida LO; Neto MPC; Sousa LO; Tannous MA; Curti C; Leopoldino AM
[Ad] Endereço:Department of Clinical Analyses, Toxicology and Food Sciences, School of Pharmaceutical Sciences of Ribeirão Preto, University of São Paulo, Ribeirão Preto, SP, Brazil.
[Ti] Título:SET oncoprotein accumulation regulates transcription through DNA demethylation and histone hypoacetylation.
[So] Source:Oncotarget;8(16):26802-26818, 2017 Apr 18.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Epigenetic modifications are essential in the control of normal cellular processes and cancer development. DNA methylation and histone acetylation are major epigenetic modifications involved in gene transcription and abnormal events driving the oncogenic process. SET protein accumulates in many cancer types, including head and neck squamous cell carcinoma (HNSCC); SET is a member of the INHAT complex that inhibits gene transcription associating with histones and preventing their acetylation. We explored how SET protein accumulation impacts on the regulation of gene expression, focusing on DNA methylation and histone acetylation. DNA methylation profile of 24 tumour suppressors evidenced that SET accumulation decreased DNA methylation in association with loss of 5-methylcytidine, formation of 5-hydroxymethylcytosine and increased TET1 levels, indicating an active DNA demethylation mechanism. However, the expression of some suppressor genes was lowered in cells with high SET levels, suggesting that loss of methylation is not the main mechanism modulating gene expression. SET accumulation also downregulated the expression of 32 genes of a panel of 84 transcription factors, and SET directly interacted with chromatin at the promoter of the downregulated genes, decreasing histone acetylation. Gene expression analysis after cell treatment with 5-aza-2'-deoxycytidine (5-AZA) and Trichostatin A (TSA) revealed that histone acetylation reversed transcription repression promoted by SET. These results suggest a new function for SET in the regulation of chromatin dynamics. In addition, TSA diminished both SET protein levels and SET capability to bind to gene promoter, suggesting that administration of epigenetic modifier agents could be efficient to reverse SET phenotype in cancer.
[Mh] Termos MeSH primário: Metilação de DNA
Regulação Neoplásica da Expressão Gênica
Chaperonas de Histonas/metabolismo
Histonas/metabolismo
Proteínas Oncogênicas/metabolismo
Fatores de Transcrição/metabolismo
Transcrição Genética
[Mh] Termos MeSH secundário: Acetilação
Carcinoma Pulmonar de Células não Pequenas/genética
Carcinoma Pulmonar de Células não Pequenas/metabolismo
Linhagem Celular Tumoral
Epigênese Genética
Perfilação da Expressão Gênica
Chaperonas de Histonas/genética
Seres Humanos
Modelos Biológicos
Fatores de Transcrição/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Histone Chaperones); 0 (Histones); 0 (Oncogene Proteins); 0 (SET protein, human); 0 (Transcription Factors)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.15818


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[PMID]:29339748
[Au] Autor:Lee S; Oh S; Jeong K; Jo H; Choi Y; Seo HD; Kim M; Choe J; Kwon CS; Lee D
[Ad] Endereço:Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon, 34141, Republic of Korea.
[Ti] Título:Dot1 regulates nucleosome dynamics by its inherent histone chaperone activity in yeast.
[So] Source:Nat Commun;9(1):240, 2018 01 16.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Dot1 (disruptor of telomeric silencing-1, DOT1L in humans) is the only known enzyme responsible for histone H3 lysine 79 methylation (H3K79me) and is evolutionarily conserved in most eukaryotes. Yeast Dot1p lacks a SET domain and does not methylate free histones and thus may have different actions with respect to other histone methyltransferases. Here we show that Dot1p displays histone chaperone activity and regulates nucleosome dynamics via histone exchange in yeast. We show that a methylation-independent function of Dot1p is required for the cryptic transcription within transcribed regions seen following disruption of the Set2-Rpd3S pathway. Dot1p can assemble core histones to nucleosomes and facilitate ATP-dependent chromatin-remodeling activity through its nucleosome-binding domain, in vitro. Global analysis indicates that Dot1p appears to be particularly important for histone exchange and chromatin accessibility on the transcribed regions of long-length genes. Our findings collectively suggest that Dot1p-mediated histone chaperone activity controls nucleosome dynamics in transcribed regions.
[Mh] Termos MeSH primário: Chaperonas de Histonas/metabolismo
Histona-Lisina N-Metiltransferase/metabolismo
Proteínas Nucleares/metabolismo
Nucleossomos/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Cromatina/genética
Cromatina/metabolismo
Regulação Fúngica da Expressão Gênica
Chaperonas de Histonas/genética
Histona-Lisina N-Metiltransferase/genética
Histonas/metabolismo
Lisina/metabolismo
Mutação
Proteínas Nucleares/genética
Nucleossomos/genética
Ligação Proteica
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Chromatin); 0 (Histone Chaperones); 0 (Histones); 0 (Nuclear Proteins); 0 (Nucleosomes); 0 (Saccharomyces cerevisiae Proteins); EC 2.1.1.43 (Dot1 protein, S cerevisiae); EC 2.1.1.43 (Histone-Lysine N-Methyltransferase); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180118
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02759-8


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[PMID]:28781233
[Au] Autor:Krishnan S; Smits AH; Vermeulen M; Reinberg D
[Ad] Endereço:Howard Hughes Medical Institute, New York University Langone School of Medicine, New York, NY 10016, USA; Department of Biochemistry and Molecular Pharmacology, New York University Langone School of Medicine, New York, NY 10016, USA.
[Ti] Título:Phospho-H1 Decorates the Inter-chromatid Axis and Is Evicted along with Shugoshin by SET during Mitosis.
[So] Source:Mol Cell;67(4):579-593.e6, 2017 Aug 17.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Precise control of sister chromatid separation during mitosis is pivotal to maintaining genomic integrity. Yet, the regulatory mechanisms involved are not well understood. Remarkably, we discovered that linker histone H1 phosphorylated at S/T18 decorated the inter-chromatid axial DNA on mitotic chromosomes. Sister chromatid resolution during mitosis required the eviction of such H1S/T18ph by the chaperone SET, with this process being independent of and most likely downstream of arm-cohesin dissociation. SET also directed the disassembly of Shugoshins in a polo-like kinase 1-augmented manner, aiding centromere resolution. SET ablation compromised mitotic fidelity as evidenced by unresolved sister chromatids with marked accumulation of H1S/T18ph and centromeric Shugoshin. Thus, chaperone-assisted eviction of linker histones and Shugoshins is a fundamental step in mammalian mitotic progression. Our findings also elucidate the functional implications of the decades-old observation of mitotic linker histone phosphorylation, serving as a paradigm to explore the role of linker histones in bio-signaling processes.
[Mh] Termos MeSH primário: Proteínas de Ciclo Celular/metabolismo
Cromátides/metabolismo
Chaperonas de Histonas/metabolismo
Histonas/metabolismo
Mitose
Proteínas Oncogênicas/metabolismo
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas de Ciclo Celular/genética
Cromátides/genética
Segregação de Cromossomos
Fibroblastos/metabolismo
Células HEK293
Chaperonas de Histonas/genética
Seres Humanos
Camundongos
Proteínas Oncogênicas/genética
Fosforilação
Proteínas Serina-Treonina Quinases/genética
Proteínas Serina-Treonina Quinases/metabolismo
Proteínas Proto-Oncogênicas/genética
Proteínas Proto-Oncogênicas/metabolismo
Interferência de RNA
Epitélio Pigmentado da Retina/metabolismo
Transdução de Sinais
Fatores de Transcrição/genética
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Cycle Proteins); 0 (Histone Chaperones); 0 (Histones); 0 (Oncogene Proteins); 0 (Proto-Oncogene Proteins); 0 (SET protein, human); 0 (SET protein, mouse); 0 (SGOL1 protein, human); 0 (Transcription Factors); 0 (shugoshin protein, mouse); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.1 (polo-like kinase 1)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170808
[St] Status:MEDLINE


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[PMID]:28637236
[Au] Autor:Gómez-Herreros F; Margaritis T; Rodríguez-Galán O; Pelechano V; Begley V; Millán-Zambrano G; Morillo-Huesca M; Muñoz-Centeno MC; Pérez-Ortín JE; de la Cruz J; Holstege FCP; Chávez S
[Ad] Endereço:Instituto de Biomedicina de Sevilla (IBiS), Hospital Virgen del Rocío-CSIC-Universidad de Sevilla, and Departamento de Genética, Universidad de Sevilla, 41013 Seville, Spain.
[Ti] Título:The ribosome assembly gene network is controlled by the feedback regulation of transcription elongation.
[So] Source:Nucleic Acids Res;45(16):9302-9318, 2017 Sep 19.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Ribosome assembly requires the concerted expression of hundreds of genes, which are transcribed by all three nuclear RNA polymerases. Transcription elongation involves dynamic interactions between RNA polymerases and chromatin. We performed a synthetic lethal screening in Saccharomyces cerevisiae with a conditional allele of SPT6, which encodes one of the factors that facilitates this process. Some of these synthetic mutants corresponded to factors that facilitate pre-rRNA processing and ribosome biogenesis. We found that the in vivo depletion of one of these factors, Arb1, activated transcription elongation in the set of genes involved directly in ribosome assembly. Under these depletion conditions, Spt6 was physically targeted to the up-regulated genes, where it helped maintain their chromatin integrity and the synthesis of properly stable mRNAs. The mRNA profiles of a large set of ribosome biogenesis mutants confirmed the existence of a feedback regulatory network among ribosome assembly genes. The transcriptional response in this network depended on both the specific malfunction and the role of the regulated gene. In accordance with our screening, Spt6 positively contributed to the optimal operation of this global network. On the whole, this work uncovers a feedback control of ribosome biogenesis by fine-tuning transcription elongation in ribosome assembly factor-coding genes.
[Mh] Termos MeSH primário: Redes Reguladoras de Genes
Chaperonas de Histonas/genética
Biogênese de Organelas
Ribossomos/genética
Proteínas de Saccharomyces cerevisiae/genética
Elongação da Transcrição Genética
Fatores de Elongação da Transcrição/genética
[Mh] Termos MeSH secundário: Transportadores de Cassetes de Ligação de ATP/genética
Adenosina Trifosfatases/genética
Retroalimentação Fisiológica
Chaperonas de Histonas/metabolismo
Mutação
Processamento Pós-Transcricional do RNA
RNA Ribossômico/metabolismo
Proteínas Ribossômicas/genética
Ribossomos/metabolismo
Saccharomyces cerevisiae
Proteínas de Saccharomyces cerevisiae/metabolismo
Mutações Sintéticas Letais
Fatores de Elongação da Transcrição/metabolismo
Transcriptoma
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Histone Chaperones); 0 (RNA, Ribosomal); 0 (Ribosomal Proteins); 0 (SPT6 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (Transcriptional Elongation Factors); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.1.3 (ARB1 protein, S cerevisiae)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170623
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx529


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[PMID]:28636114
[Au] Autor:Sobral LM; Coletta RD; Alberici LC; Curti C; Leopoldino AM
[Ad] Endereço:Department of Clinical Analyses, Toxicology and Food Sciences, School of Pharmaceutical Sciences of Ribeirão Preto, University of São Paulo, SP, Brazil.
[Ti] Título:SET/I2PP2A overexpression induces phenotypic, molecular, and metabolic alterations in an oral keratinocyte cell line.
[So] Source:FEBS J;284(17):2774-2785, 2017 Sep.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The multifunctional SET/I2PP2A protein is known to be overexpressed in head and neck squamous cell carcinoma. However, SET has been reported to have apparently conflicting roles in promoting cancer cell survival under oxidative stress conditions and preventing invasion and metastasis, complicating efforts to understand the contribution of SET to carcinogenesis. In the present study, we overexpressed SETin a spontaneously immortalized oral keratinocyte cell line (NOK-SI SET) and demonstrated that SET upregulation alone was sufficient to transform cells. In comparison with NOK-SI cells, NOK-SI SET cells demonstrated increased levels of phosphorylated Akt, c-Myc and inactive/phosphorylated Rb, together with decreased total Rb protein levels. In addition, NOK-SI SET cells presented the following: (a) a spindle-cell shape morphology compared with the polygonal morphology of NOK-SI cells; (b) loss of mesenchymal stem cell markers CD44 and CD73, and epithelial cell markers CD71 and integrin α6/ß4; (c) the ability to form xenograft tumors in nude mice; and (d) increased mitochondrial respiration accompanied by decreased ROSlevels. Overall, our results show that SEToverexpression promotes morphological and oncogenic cell transformation of an oral keratinocyte cell.
[Mh] Termos MeSH primário: Chaperonas de Histonas/genética
Queratinócitos/fisiologia
Fatores de Transcrição/genética
[Mh] Termos MeSH secundário: Carcinogênese/genética
Carcinogênese/metabolismo
Diferenciação Celular
Linhagem Celular
Expressão Gênica
Chaperonas de Histonas/metabolismo
Seres Humanos
Queratinócitos/ultraestrutura
Dinâmica Mitocondrial
Mucosa Bucal/citologia
Fenótipo
Fatores de Transcrição/metabolismo
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Histone Chaperones); 0 (SET protein, human); 0 (Transcription Factors)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170622
[St] Status:MEDLINE
[do] DOI:10.1111/febs.14148


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[PMID]:28610839
[Au] Autor:Warren C; Shechter D
[Ad] Endereço:Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
[Ti] Título:Fly Fishing for Histones: Catch and Release by Histone Chaperone Intrinsically Disordered Regions and Acidic Stretches.
[So] Source:J Mol Biol;429(16):2401-2426, 2017 Aug 04.
[Is] ISSN:1089-8638
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Chromatin is the complex of eukaryotic DNA and proteins required for the efficient compaction of the nearly 2-meter-long human genome into a roughly 10-micron-diameter cell nucleus. The fundamental repeating unit of chromatin is the nucleosome: 147bp of DNA wrapped about an octamer of histone proteins. Nucleosomes are stable enough to organize the genome yet must be dynamically displaced and reassembled to allow access to the underlying DNA for transcription, replication, and DNA damage repair. Histone chaperones are a non-catalytic group of proteins that are central to the processes of nucleosome assembly and disassembly and thus the fluidity of the ever-changing chromatin landscape. Histone chaperones are responsible for binding the highly basic histone proteins, shielding them from non-specific interactions, facilitating their deposition onto DNA, and aiding in their eviction from DNA. Although most histone chaperones perform these common functions, recent structural studies of many different histone chaperones reveal that there are few commonalities in their folds. Importantly, sequence-based predictions show that histone chaperones are highly enriched in intrinsically disordered regions (IDRs) and acidic stretches. In this review, we focus on the molecular mechanisms underpinning histone binding, selectivity, and regulation of these highly dynamic protein regions. We highlight new evidence suggesting that IDRs are often critical for histone chaperone function and play key roles in chromatin assembly and disassembly pathways.
[Mh] Termos MeSH primário: Cromatina/metabolismo
Chaperonas de Histonas/química
Chaperonas de Histonas/metabolismo
Histonas/metabolismo
Nucleossomos/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Seres Humanos
Modelos Biológicos
Modelos Moleculares
Ligação Proteica
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Chromatin); 0 (Histone Chaperones); 0 (Histones); 0 (Nucleosomes)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170814
[Lr] Data última revisão:
170814
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170615
[St] Status:MEDLINE


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[PMID]:28552960
[Au] Autor:Liu C; Wang T; Bai Y; Wang J
[Ad] Endereço:State Key Laboratory of Electroanalytical Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, Jilin, P.R. China, 130022.
[Ti] Título:Electrostatic forces govern the binding mechanism of intrinsically disordered histone chaperones.
[So] Source:PLoS One;12(5):e0178405, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A unified picture to understand the protein recognition and function must include the native binding complex structure ensembles and the underlying binding mechanisms involved in specific biological processes. However, quantifications of both binding complex structures and dynamical mechanisms are still challenging for IDP. In this study, we have investigated the underlying molecular mechanism of the chaperone Chz1 and histone H2A.Z-H2B association by equilibrium and kinetic stopped-flow fluorescence spectroscopy. The dependence of free energy and kinetic rate constant on electrolyte mean activity coefficient and urea concentration are uncovered. Our results indicate a previous unseen binding kinetic intermediate. An initial conformation selection step of Chz1 is also revealed before the formation of this intermediate state. Based on these observations, a mixed mechanism of three steps including both conformation selection and induced fit is proposed. By combination of the ion- and denaturant-induced experiments, we demonstrate that electrostatic forces play a dominant role in the recognition of bipolar charged intrinsically disordered protein Chz1 to its preferred partner H2A.Z-H2B. Both the intra-chain and inter-chain electrostatic interactions have direct impacts on the native collapsed structure and binding mechanism.
[Mh] Termos MeSH primário: Chaperonas de Histonas/metabolismo
Proteínas Intrinsicamente Desordenadas/metabolismo
Eletricidade Estática
[Mh] Termos MeSH secundário: Calorimetria
Dicroísmo Circular
Cinética
Espectrometria de Fluorescência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Histone Chaperones); 0 (Intrinsically Disordered Proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170918
[Lr] Data última revisão:
170918
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170530
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0178405


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[PMID]:28548025
[Au] Autor:Hung MH; Chen KF
[Ad] Endereço:a Division of Medical Oncology, Department of Oncology , Taipei Veterans General Hospital , Taipei , Taiwan.
[Ti] Título:Reprogramming the oncogenic response: SET protein as a potential therapeutic target in cancer.
[So] Source:Expert Opin Ther Targets;21(7):685-694, 2017 Jul.
[Is] ISSN:1744-7631
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: SET is a multitask oncoprotein that promotes the initiation and progression of cancer. Overexpression of SET has been characterized as being tumor-specific and is associated with adverse clinical outcomes in many different human malignant diseases. Notably, SET has been shown to promote the development of therapeutic resistance in cancer cells. Area covered: In this review, we summarized the currently available evidence relating to the oncogenic roles, biological functions and clinical relevance of SET protein in cancer. The anti-cancer effects of three different SET antagonists undergoing preclinical investigation are also discussed. Expert opinion: Emerging evidence supports the critical role of SET in regulating various different cancer hallmarks. Targeting the SET-associated protein interfaces may be a potential anti-cancer strategy for future development. However, more studies are required to clarify the best strategy to combine SET antagonists with other anti-cancer treatments and to explore possible biomarkers that predict responsiveness.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
Chaperonas de Histonas/metabolismo
Neoplasias/tratamento farmacológico
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Animais
Biomarcadores Tumorais/metabolismo
Progressão da Doença
Desenho de Drogas
Resistência a Medicamentos Antineoplásicos
Chaperonas de Histonas/antagonistas & inibidores
Seres Humanos
Terapia de Alvo Molecular
Neoplasias/patologia
Fatores de Transcrição/antagonistas & inibidores
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Biomarkers, Tumor); 0 (Histone Chaperones); 0 (SET protein, human); 0 (Transcription Factors)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170629
[Lr] Data última revisão:
170629
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170527
[St] Status:MEDLINE
[do] DOI:10.1080/14728222.2017.1336226


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[PMID]:28515277
[Au] Autor:Li Y; Jiao J
[Ad] Endereço:State Key Laboratory of Stem Cell and Reproductive Biology, Institute of Zoology, Chinese Academy of Sciences, Beijing 100101, China.
[Ti] Título:Histone chaperone HIRA regulates neural progenitor cell proliferation and neurogenesis via ß-catenin.
[So] Source:J Cell Biol;216(7):1975-1992, 2017 Jul 03.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Histone cell cycle regulator (HIRA) is a histone chaperone and has been identified as an epigenetic regulator. Subsequent studies have provided evidence that HIRA plays key roles in embryonic development, but its function during early neurogenesis remains unknown. Here, we demonstrate that HIRA is enriched in neural progenitor cells, and HIRA knockdown reduces neural progenitor cell proliferation, increases terminal mitosis and cell cycle exit, and ultimately results in premature neuronal differentiation. Additionally, we demonstrate that HIRA enhances ß-catenin expression by recruiting H3K4 trimethyltransferase Setd1A, which increases H3K4me3 levels and heightens the promoter activity of ß-catenin. Significantly, overexpression of HIRA, HIRA N-terminal domain, or ß-catenin can override neurogenesis abnormities caused by HIRA defects. Collectively, these data implicate that HIRA, cooperating with Setd1A, modulates ß-catenin expression and then regulates neurogenesis. This finding represents a novel epigenetic mechanism underlying the histone code and has profound and lasting implications for diseases and neurobiology.
[Mh] Termos MeSH primário: Proteínas de Ciclo Celular/metabolismo
Proliferação Celular
Córtex Cerebral/metabolismo
Chaperonas de Histonas/metabolismo
Histonas/metabolismo
Células-Tronco Neurais/metabolismo
Neurogênese
Fatores de Transcrição/metabolismo
beta Catenina/metabolismo
[Mh] Termos MeSH secundário: Animais
Apoptose
Ciclo Celular
Proteínas de Ciclo Celular/genética
Linhagem Celular Tumoral
Córtex Cerebral/embriologia
Metilação de DNA
Epigênese Genética
Idade Gestacional
Chaperonas de Histonas/genética
Histona-Lisina N-Metiltransferase/genética
Histona-Lisina N-Metiltransferase/metabolismo
Metilação
Camundongos Endogâmicos ICR
Mitose
Células-Tronco Neurais/patologia
Fenótipo
Cultura Primária de Células
Processamento de Proteína Pós-Traducional
Interferência de RNA
Transdução de Sinais
Fatores de Transcrição/genética
Transfecção
beta Catenina/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CTNNB1 protein, mouse); 0 (Cell Cycle Proteins); 0 (Hira protein, mouse); 0 (Histone Chaperones); 0 (Histones); 0 (Transcription Factors); 0 (beta Catenin); EC 2.1.1.43 (Histone-Lysine N-Methyltransferase); EC 2.1.1.43 (Nsccn1 protein, mouse)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170913
[Lr] Data última revisão:
170913
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170519
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201610014


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[PMID]:28386724
[Au] Autor:McDaniel SL; Strahl BD
[Ad] Endereço:Department of Biomolecular Chemistry, University of Wisconsin, Madison, WI, 53706, USA.
[Ti] Título:Shaping the cellular landscape with Set2/SETD2 methylation.
[So] Source:Cell Mol Life Sci;74(18):3317-3334, 2017 Sep.
[Is] ISSN:1420-9071
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Chromatin structure is a major barrier to gene transcription that must be disrupted and re-set during each round of transcription. Central to this process is the Set2/SETD2 methyltransferase that mediates co-transcriptional methylation to histone H3 at lysine 36 (H3K36me). Studies reveal that H3K36me not only prevents inappropriate transcriptional initiation from arising within gene bodies, but that it has other conserved functions that include the repair of damaged DNA and regulation of pre-mRNA splicing. Consistent with the importance of Set2/SETD2 in chromatin biology, mutations of SETD2, or mutations at or near H3K36 in H3.3, have recently been found to underlie cancer development. This review will summarize the latest insights into the functions of Set2/SETD2 in genome regulation and cancer development.
[Mh] Termos MeSH primário: Cromatina/metabolismo
Histona-Lisina N-Metiltransferase/metabolismo
[Mh] Termos MeSH secundário: Animais
Cromatina/química
Reparo do DNA
Chaperonas de Histonas/metabolismo
Histona-Lisina N-Metiltransferase/química
Histonas/metabolismo
Seres Humanos
Metilação
Domínios Proteicos
Transcrição Genética
Leveduras/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Chromatin); 0 (Histone Chaperones); 0 (Histones); EC 2.1.1.43 (Histone-Lysine N-Methyltransferase); EC 2.1.1.43 (Set2 protein, human)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170830
[Lr] Data última revisão:
170830
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170408
[St] Status:MEDLINE
[do] DOI:10.1007/s00018-017-2517-x



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