Base de dados : MEDLINE
Pesquisa : D08.811.913.050.134.415.500.062 [Categoria DeCS]
Referências encontradas : 293 [refinar]
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  1 / 293 MEDLINE  
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[PMID]:29045464
[Au] Autor:Rajagopalan D; Pandey AK; Xiuzhen MC; Lee KK; Hora S; Zhang Y; Chua BH; Kwok HS; Bhatia SS; Deng LW; Tenen DG; Kappei D; Jha S
[Ad] Endereço:Cancer Science Institute of Singapore, National University of Singapore, Singapore.
[Ti] Título:TIP60 represses telomerase expression by inhibiting Sp1 binding to the TERT promoter.
[So] Source:PLoS Pathog;13(10):e1006681, 2017 Oct.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:HIV1-TAT interactive protein (TIP60) is a haploinsufficient tumor suppressor. However, the potential mechanisms endowing its tumor suppressor ability remain incompletely understood. It plays a vital role in virus-induced cancers where TIP60 down-regulates the expression of human papillomavirus (HPV) oncoprotein E6 which in turn destabilizes TIP60. This intrigued us to identify the role of TIP60, in the context of a viral infection, where it is targeted by oncoproteins. Through an array of molecular biology techniques such as Chromatin immunoprecipitation, expression analysis and mass spectrometry, we establish the hitherto unknown role of TIP60 in repressing the expression of the catalytic subunit of the human telomerase complex, TERT, a key driver for immortalization. TIP60 acetylates Sp1 at K639, thus inhibiting Sp1 binding to the TERT promoter. We identified that TIP60-mediated growth suppression of HPV-induced cervical cancer is mediated in part due to TERT repression through Sp1 acetylation. In summary, our study has identified a novel substrate for TIP60 catalytic activity and a unique repressive mechanism acting at the TERT promoter in virus-induced malignancies.
[Mh] Termos MeSH primário: Regulação Enzimológica da Expressão Gênica
Regulação Neoplásica da Expressão Gênica
Histona Acetiltransferases/metabolismo
Proteínas de Neoplasias/metabolismo
Elementos de Resposta
Fator de Transcrição Sp1/metabolismo
Telomerase/biossíntese
Neoplasias do Colo do Útero/metabolismo
[Mh] Termos MeSH secundário: Feminino
Células HeLa
Histona Acetiltransferases/genética
Seres Humanos
Lisina Acetiltransferase 5
Proteínas de Neoplasias/genética
Fator de Transcrição Sp1/genética
Telomerase/genética
Neoplasias do Colo do Útero/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Neoplasm Proteins); 0 (Sp1 Transcription Factor); 0 (Sp1 protein, human); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.48 (KAT5 protein, human); EC 2.3.1.48 (Lysine Acetyltransferase 5); EC 2.7.7.49 (TERT protein, human); EC 2.7.7.49 (Telomerase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171019
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006681


  2 / 293 MEDLINE  
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[PMID]:28892470
[Au] Autor:Kwon HK; Chen HM; Mathis D; Benoist C
[Ad] Endereço:Division of Immunology, Department of Microbiology and Immunobiology, Harvard Medical School, and Evergrande Center for Immunologic Diseases, Harvard Medical School and Brigham and Women's Hospital, Boston, Massachusetts, USA.
[Ti] Título:Different molecular complexes that mediate transcriptional induction and repression by FoxP3.
[So] Source:Nat Immunol;18(11):1238-1248, 2017 Nov.
[Is] ISSN:1529-2916
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:FoxP3 conditions the transcriptional signature and functional facets of regulatory T cells (T cells). Its mechanism of action, whether as an activator or a repressor, has remained unclear. Here, chromatin analysis showed that FoxP3 bound active enhancer elements, not repressed chromatin, around loci over- or under-expressed in T cells. We evaluated the impact of a panel of FoxP3 mutants on its transcriptional activity and interactions with DNA, transcriptional cofactors and chromatin. Computational integration, confirmed by biochemical interaction and size analyses, showed that FoxP3 existed in distinct multimolecular complexes. It was active and primarily an activator when complexed with the transcriptional factors RELA, IKZF2 and KAT5. In contrast, FoxP3 was inactive when complexed with the histone methyltransferase EZH2 and transcription factors YY1 and IKZF3. The latter complex partitioned to a peripheral region of the nucleus, as shown by super-resolution microscopy. Thus, FoxP3 acts in multimodal fashion to directly activate or repress transcription, in a context- and partner-dependent manner, to govern T cell phenotypes.
[Mh] Termos MeSH primário: Fatores de Transcrição Forkhead/genética
Regulação da Expressão Gênica
Linfócitos T Reguladores/metabolismo
Ativação Transcricional
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
DNA/genética
DNA/metabolismo
Fatores de Transcrição Forkhead/imunologia
Fatores de Transcrição Forkhead/metabolismo
Perfilação da Expressão Gênica/métodos
Histona Acetiltransferases/genética
Histona Acetiltransferases/metabolismo
Histona-Lisina N-Metiltransferase/genética
Histona-Lisina N-Metiltransferase/metabolismo
Immunoblotting
Lisina Acetiltransferase 5
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Transgênicos
Mutação
Células NIH 3T3
Ligação Proteica
Linfócitos T Reguladores/imunologia
Transativadores/genética
Transativadores/metabolismo
Fator de Transcrição RelA/genética
Fator de Transcrição RelA/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Forkhead Transcription Factors); 0 (Foxp3 protein, mouse); 0 (Rela protein, mouse); 0 (Trans-Activators); 0 (Transcription Factor RelA); 9007-49-2 (DNA); EC 2.1.1.- (histone methyltransferase); EC 2.1.1.43 (Histone-Lysine N-Methyltransferase); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.48 (Kat5 protein, mouse); EC 2.3.1.48 (Lysine Acetyltransferase 5)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170912
[St] Status:MEDLINE
[do] DOI:10.1038/ni.3835


  3 / 293 MEDLINE  
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[PMID]:28837777
[Au] Autor:Tam LM; Jiang J; Wang P; Li L; Miao W; Dong X; Wang Y
[Ad] Endereço:Environmental Toxicology Graduate Program, ‡Cell, Molecular, and Developmental Biology Graduate Program, and §Department of Chemistry, University of California at Riverside , Mail Drop 027, Riverside, California 92521-0403, United States.
[Ti] Título:Arsenite Binds to the Zinc Finger Motif of TIP60 Histone Acetyltransferase and Induces Its Degradation via the 26S Proteasome.
[So] Source:Chem Res Toxicol;30(9):1685-1693, 2017 Sep 18.
[Is] ISSN:1520-5010
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Arsenic is a ubiquitous environmental contaminant with widespread public health concern. Epidemiological studies have revealed that chronic human exposure to arsenic in drinking water is associated with the prevalence of skin, lung, and bladder cancers. Aberrant histone modifications (e.g., methylation, acetylation, and ubiquitination) were previously found to be accompanied by arsenic exposure; thus, perturbation of epigenetic pathways is thought to contribute to arsenic carcinogenesis. Arsenite is known to interact with zinc finger motifs of proteins, and zinc finger motif is present in and indispensable for the enzymatic activities of crucial histone-modifying enzymes especially the MYST family of histone acetyltransferases (e.g., TIP60). Hence, we reasoned that trivalent arsenic may target the zinc finger motif of these enzymes, disturb their enzymatic activities, and alter histone acetylation. Herein, we found that As could bind directly to the zinc-finger motif of TIP60 in vitro and in cells. In addition, exposure to As could lead to a dose-dependent decrease in TIP60 protein level via the ubiquitin-proteasome pathway. Thus, the results from the present study revealed, for the first time, that arsenite may target cysteine residues in the zinc-finger motif of the TIP60 histone acetyltransferase, thereby altering the H4K16Ac histone epigenetic mark. Our results also shed some new light on the mechanisms underlying the arsenic-induced epigenotoxicity and carcinogenesis in humans.
[Mh] Termos MeSH primário: Arsenitos/metabolismo
Histona Acetiltransferases/metabolismo
Complexo de Endopeptidases do Proteassoma/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Arsenitos/química
Biotina/química
Ditiotreitol/química
Células HEK293
Histona Acetiltransferases/química
Histona Acetiltransferases/genética
Histonas/metabolismo
Seres Humanos
Leupeptinas/química
Lisina Acetiltransferase 5
Ligação Proteica
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
Ubiquitina/metabolismo
Dedos de Zinco
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arsenites); 0 (Histones); 0 (Leupeptins); 0 (Ubiquitin); 6SO6U10H04 (Biotin); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.48 (KAT5 protein, human); EC 2.3.1.48 (Lysine Acetyltransferase 5); EC 3.4.25.1 (Proteasome Endopeptidase Complex); EC 3.4.99.- (ATP dependent 26S protease); N5509X556J (arsenite); RF1P63GW3K (benzyloxycarbonylleucyl-leucyl-leucine aldehyde); T8ID5YZU6Y (Dithiothreitol)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170825
[St] Status:MEDLINE
[do] DOI:10.1021/acs.chemrestox.7b00146


  4 / 293 MEDLINE  
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[PMID]:28694333
[Au] Autor:Dong Y; Isono KI; Ohbo K; Endo TA; Ohara O; Maekawa M; Toyama Y; Ito C; Toshimori K; Helin K; Ogonuki N; Inoue K; Ogura A; Yamagata K; Kitabayashi I; Koseki H
[Ad] Endereço:RIKEN Center for Integrative Medical Science, Yokohama, Kanagawa, Japan yixin.dong@riken.jp haruhiko.koseki@riken.jp.
[Ti] Título:EPC1/TIP60-Mediated Histone Acetylation Facilitates Spermiogenesis in Mice.
[So] Source:Mol Cell Biol;37(19), 2017 Oct 01.
[Is] ISSN:1098-5549
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Global histone hyperacetylation is suggested to play a critical role for replacement of histones by transition proteins and protamines to compact the genome during spermiogenesis. However, the underlying mechanisms for hyperacetylation-mediated histone replacement remains poorly understood. Here, we report that EPC1 and TIP60, two critical components of the mammalian nucleosome acetyltransferase of H4 (NuA4) complexes, are coexpressed in male germ cells. Strikingly, genetic ablation of either or disrupts hyperacetylation and impairs histone replacement, in turn causing aberrant spermatid development. Taking these observations together, we reveal an essential role of the NuA4 complexes for histone hyperacetylation and subsequent compaction of the spermatid genome.
[Mh] Termos MeSH primário: Histona Acetiltransferases/metabolismo
Histonas/metabolismo
Proteínas Repressoras/metabolismo
Espermátides/crescimento & desenvolvimento
Espermatogênese
Transativadores/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Animais
Células Cultivadas
Regulação da Expressão Gênica no Desenvolvimento
Técnicas de Inativação de Genes
Histona Acetiltransferases/genética
Lisina Acetiltransferase 5
Masculino
Camundongos
Proteínas Repressoras/genética
Espermátides/metabolismo
Transativadores/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Epc1 protein, mouse); 0 (Histones); 0 (Repressor Proteins); 0 (Trans-Activators); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.48 (Kat5 protein, mouse); EC 2.3.1.48 (Lysine Acetyltransferase 5)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170712
[St] Status:MEDLINE


  5 / 293 MEDLINE  
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[PMID]:28546430
[Au] Autor:Li L; Wang Y
[Ad] Endereço:From the Department of Chemistry, University of California, Riverside, California 92521-0403.
[Ti] Título:Cross-talk between the H3K36me3 and H4K16ac histone epigenetic marks in DNA double-strand break repair.
[So] Source:J Biol Chem;292(28):11951-11959, 2017 Jul 14.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Post-translational modifications of histone proteins regulate numerous cellular processes. Among these modifications, trimethylation of lysine 36 in histone H3 (H3K36me3) and acetylation of lysine 16 in histone H4 (H4K16ac) have important roles in transcriptional regulation and DNA damage response signaling. However, whether these two epigenetic histone marks are mechanistically linked remains unclear. Here we discovered a new pathway through which H3K36me3 stimulates H4K16ac upon DNA double-strand break (DSB) induction in human cells. In particular, we examined, using Western blot analysis, the levels of H3K36me3 and H4K16ac in cells after exposure to various DSB-inducing agents, including neocarzinostatin, γ rays, and etoposide, and found that H3K36me3 and H4K16ac were both elevated in cells upon these treatments. We also observed that DSB-induced H4K16 acetylation was abolished in cells upon depletion of the histone methyltransferase gene SET-domain containing 2 ( ) and the ensuing loss of H3K36me3. Furthermore, the H3K36me3-mediated increase in H4K16ac necessitated lens epithelium-derived growth factor p75 splicing variant (LEDGF), which is a reader protein of H3K36me3, and the KAT5 (TIP60) histone acetyltransferase. Mechanistically, the chromatin-bound LEDGF, through its interaction with KAT5, promoted chromatin localization of KAT5, thereby stimulating H4K16 acetylation. In this study, we unveiled cross-talk between two important histone epigenetic marks and defined the function of this cross-talk in DNA DSB repair.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Reparo do DNA
Epigênese Genética
Histona Acetiltransferases/metabolismo
Histona-Lisina N-Metiltransferase/metabolismo
Histonas/metabolismo
Processamento de Proteína Pós-Traducional
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Proteínas Adaptadoras de Transdução de Sinal/antagonistas & inibidores
Proteínas Adaptadoras de Transdução de Sinal/genética
Biomarcadores/metabolismo
Sistemas CRISPR-Cas
Linhagem Celular Tumoral
Cromatina/metabolismo
DNA/metabolismo
Quebras de DNA de Cadeia Dupla
Técnicas de Inativação de Genes
Células HEK293
Histona Acetiltransferases/genética
Histona-Lisina N-Metiltransferase/antagonistas & inibidores
Histona-Lisina N-Metiltransferase/genética
Seres Humanos
Lisina/metabolismo
Lisina Acetiltransferase 5
Metilação
Transporte Proteico
Interferência de RNA
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Fatores de Transcrição/antagonistas & inibidores
Fatores de Transcrição/genética
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Biomarkers); 0 (Chromatin); 0 (Histones); 0 (PSIP1 protein, human); 0 (Recombinant Proteins); 0 (Transcription Factors); 9007-49-2 (DNA); EC 2.1.1.43 (Histone-Lysine N-Methyltransferase); EC 2.1.1.43 (Set2 protein, human); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.48 (KAT5 protein, human); EC 2.3.1.48 (Lysine Acetyltransferase 5); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170527
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.788224


  6 / 293 MEDLINE  
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[PMID]:28511652
[Au] Autor:Nabbi A; McClurg UL; Thalappilly S; Almami A; Mobahat M; Bismar TA; Binda O; Riabowol KT
[Ad] Endereço:Department of Biochemistry & Molecular Biology, Arnie Charbonneau Cancer Institute, Cumming School of Medicine, University of Calgary, Calgary, AB, Canada.
[Ti] Título:ING3 promotes prostate cancer growth by activating the androgen receptor.
[So] Source:BMC Med;15(1):103, 2017 May 16.
[Is] ISSN:1741-7015
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The androgen receptor (AR) is a major driver of prostate cancer, and increased AR levels and co-activators of the receptor promote the development of prostate cancer. INhibitor of Growth (ING) proteins target lysine acetyltransferase or lysine deacetylase complexes to the histone H3K4Me3 mark of active transcription, to affect chromatin structure and gene expression. ING3 is a stoichiometric member of the TIP60 lysine acetyltransferase complex implicated in prostate cancer development. METHODS: Biopsies of 265 patients with prostate cancer were stained for ING3, pan-cytokeratin, and DNA. LNCaP and C4-2 androgen-responsive cells were used for in vitro assays including immunoprecipitation, western blotting, Luciferase reporter assay and quantitative polymerase chain reaction. Cell viability and migration assays were performed in prostate cancer cell lines using scrambled siRNA or siRNA targeting ING3. RESULTS: We find that ING3 levels and AR activity positively correlate in prostate cancer. ING3 potentiates androgen effects, increasing expression of androgen-regulated genes and androgen response element-driven reporters to promote growth and anchorage-independent growth. Conversely, ING3 knockdown inhibits prostate cancer cell growth and invasion. ING3 activates the AR by serving as a scaffold to increase interaction between TIP60 and the AR in the cytoplasm, enhancing receptor acetylation and translocation to the nucleus. Activation is independent of ING3's ability to target the TIP60 complex to H3K4Me3, identifying a previously unknown chromatin-independent cytoplasmic activity for ING3. In agreement with in vitro observations, analysis of The Cancer Genome Atlas (TCGA) data (n = 498) and a prostate cancer tissue microarray (n = 256) show that ING3 levels are higher in aggressive prostate cancers, with high levels of ING3 predicting shorter patient survival in a low AR subgroup. Including ING3 levels with currently used indicators such as the Gleason score provides more accurate prognosis in primary prostate cancer. CONCLUSIONS: In contrast to the majority of previous reports suggesting tumor suppressive functions in other cancers, our observations identify a clear oncogenic role for ING3, which acts as a co-activator of AR in prostate cancer. Data from TCGA and our previous and current tissue microarrays suggest that ING3 levels correlate with AR levels and that in patients with low levels of the receptor, ING3 level could serve as a useful prognostic biomarker.
[Mh] Termos MeSH primário: Proteínas de Homeodomínio/metabolismo
Neoplasias da Próstata/metabolismo
Receptores Androgênicos/metabolismo
Proteínas Supressoras de Tumor/metabolismo
[Mh] Termos MeSH secundário: Androgênios
Linhagem Celular Tumoral
Células HEK293
Histona Acetiltransferases
Seres Humanos
Lisina Acetiltransferase 5
Masculino
Neoplasias da Próstata/patologia
RNA Interferente Pequeno
Análise de Sobrevida
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (AR protein, human); 0 (Androgens); 0 (Homeodomain Proteins); 0 (ING3 protein, human); 0 (RNA, Small Interfering); 0 (Receptors, Androgen); 0 (Tumor Suppressor Proteins); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.48 (KAT5 protein, human); EC 2.3.1.48 (Lysine Acetyltransferase 5)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170518
[St] Status:MEDLINE
[do] DOI:10.1186/s12916-017-0854-0


  7 / 293 MEDLINE  
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[PMID]:28504697
[Au] Autor:Geng J; Yu S; Zhao H; Sun X; Li X; Wang P; Xiong X; Hong L; Xie C; Gao J; Shi Y; Peng J; Johnson RL; Xiao N; Lu L; Han J; Zhou D; Chen L
[Ad] Endereço:State Key Laboratory of Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, Xiamen, Fujian, China.
[Ti] Título:The transcriptional coactivator TAZ regulates reciprocal differentiation of T 17 cells and T cells.
[So] Source:Nat Immunol;18(7):800-812, 2017 Jul.
[Is] ISSN:1529-2916
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:An imbalance in the lineages of immunosuppressive regulatory T cells (T cells) and the inflammatory T 17 subset of helper T cells leads to the development of autoimmune and/or inflammatory disease. Here we found that TAZ, a coactivator of TEAD transcription factors of Hippo signaling, was expressed under T 17 cell-inducing conditions and was required for T 17 differentiation and T 17 cell-mediated inflammatory diseases. TAZ was a critical co-activator of the T 17-defining transcription factor RORγt. In addition, TAZ attenuated T cell development by decreasing acetylation of the T cell master regulator Foxp3 mediated by the histone acetyltransferase Tip60, which targeted Foxp3 for proteasomal degradation. In contrast, under T cell-skewing conditions, TEAD1 expression and sequestration of TAZ from the transcription factors RORγt and Foxp3 promoted T cell differentiation. Furthermore, deficiency in TAZ or overexpression of TEAD1 induced T cell differentiation, whereas expression of a transgene encoding TAZ or activation of TAZ directed T 17 cell differentiation. Our results demonstrate a pivotal role for TAZ in regulating the differentiation of T cells and T 17 cells.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/imunologia
Diferenciação Celular/imunologia
Colite/imunologia
Citocinas/imunologia
Encefalomielite Autoimune Experimental/imunologia
Peptídeos e Proteínas de Sinalização Intracelular/imunologia
Linfócitos T Reguladores/imunologia
Células Th17/imunologia
[Mh] Termos MeSH secundário: Acetilação
Proteínas Adaptadoras de Transdução de Sinal/genética
Animais
Artrite Reumatoide/imunologia
Estudos de Casos e Controles
Imunoprecipitação da Cromatina
Proteínas de Ligação a DNA/imunologia
Proteínas de Ligação a DNA/metabolismo
Citometria de Fluxo
Fatores de Transcrição Forkhead/imunologia
Fatores de Transcrição Forkhead/metabolismo
Células HEK293
Células HeLa
Histona Acetiltransferases/metabolismo
Seres Humanos
Immunoblotting
Lisina Acetiltransferase 5
Camundongos
Camundongos Knockout
Camundongos Transgênicos
Microscopia Confocal
Microscopia de Fluorescência
Membro 3 do Grupo F da Subfamília 1 de Receptores Nucleares/imunologia
Membro 3 do Grupo F da Subfamília 1 de Receptores Nucleares/metabolismo
Complexo de Endopeptidases do Proteassoma/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Fator de Transcrição STAT3/imunologia
Fator de Transcrição STAT3/metabolismo
Síndrome de Sjogren/imunologia
Proteínas Smad/imunologia
Proteínas Smad/metabolismo
Transativadores/metabolismo
Fatores de Transcrição/imunologia
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Cytokines); 0 (DNA-Binding Proteins); 0 (Forkhead Transcription Factors); 0 (Foxp3 protein, mouse); 0 (Intracellular Signaling Peptides and Proteins); 0 (Nuclear Receptor Subfamily 1, Group F, Member 3); 0 (STAT3 Transcription Factor); 0 (Smad Proteins); 0 (Tead1 protein, mouse); 0 (Trans-Activators); 0 (Transcription Factors); 0 (WWTR1 protein, human); 0 (Wwtr1 protein, mouse); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.48 (Kat5 protein, mouse); EC 2.3.1.48 (Lysine Acetyltransferase 5); EC 3.4.25.1 (Proteasome Endopeptidase Complex)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170516
[St] Status:MEDLINE
[do] DOI:10.1038/ni.3748


  8 / 293 MEDLINE  
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[PMID]:28238654
[Au] Autor:Clarke TL; Sanchez-Bailon MP; Chiang K; Reynolds JJ; Herrero-Ruiz J; Bandeiras TM; Matias PM; Maslen SL; Skehel JM; Stewart GS; Davies CC
[Ad] Endereço:Institute of Cancer and Genomic Sciences, College of Medical and Dental Sciences, University of Birmingham, Birmingham B15 2TT, UK.
[Ti] Título:PRMT5-Dependent Methylation of the TIP60 Coactivator RUVBL1 Is a Key Regulator of Homologous Recombination.
[So] Source:Mol Cell;65(5):900-916.e7, 2017 Mar 02.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Protein post-translation modification plays an important role in regulating DNA repair; however, the role of arginine methylation in this process is poorly understood. Here we identify the arginine methyltransferase PRMT5 as a key regulator of homologous recombination (HR)-mediated double-strand break (DSB) repair, which is mediated through its ability to methylate RUVBL1, a cofactor of the TIP60 complex. We show that PRMT5 targets RUVBL1 for methylation at position R205, which facilitates TIP60-dependent mobilization of 53BP1 from DNA breaks, promoting HR. Mechanistically, we demonstrate that PRMT5-directed methylation of RUVBL1 is critically required for the acetyltransferase activity of TIP60, promoting histone H4K16 acetylation, which facilities 53BP1 displacement from DSBs. Interestingly, RUVBL1 methylation did not affect the ability of TIP60 to facilitate ATM activation. Taken together, our findings reveal the importance of PRMT5-mediated arginine methylation during DSB repair pathway choice through its ability to regulate acetylation-dependent control of 53BP1 localization.
[Mh] Termos MeSH primário: Proteínas de Transporte/metabolismo
Quebras de DNA de Cadeia Dupla
DNA Helicases/metabolismo
Histona Acetiltransferases/metabolismo
Processamento de Proteína Pós-Traducional
Proteína-Arginina N-Metiltransferases/metabolismo
Reparo de DNA por Recombinação
[Mh] Termos MeSH secundário: ATPases Associadas a Diversas Atividades Celulares
Acetilação
Animais
Arginina
Proteínas Mutadas de Ataxia Telangiectasia/metabolismo
Proteínas de Transporte/genética
DNA Helicases/genética
Instabilidade Genômica
Células HEK293
Células HeLa
Histona Acetiltransferases/genética
Histonas/metabolismo
Seres Humanos
Lisina Acetiltransferase 5
Metilação
Camundongos
Camundongos Transgênicos
Proteína-Arginina N-Metiltransferases/genética
Interferência de RNA
Fatores de Tempo
Transfecção
Proteína 1 de Ligação à Proteína Supressora de Tumor p53/genética
Proteína 1 de Ligação à Proteína Supressora de Tumor p53/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Histones); 0 (TP53BP1 protein, human); 0 (Tumor Suppressor p53-Binding Protein 1); 94ZLA3W45F (Arginine); EC 2.1.1.319 (PRMT5 protein, human); EC 2.1.1.319 (Prmt5 protein, mouse); EC 2.1.1.319 (Protein-Arginine N-Methyltransferases); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.48 (KAT5 protein, human); EC 2.3.1.48 (Lysine Acetyltransferase 5); EC 2.7.11.1 (ATM protein, human); EC 2.7.11.1 (Ataxia Telangiectasia Mutated Proteins); EC 3.6.4.- (ATPases Associated with Diverse Cellular Activities); EC 3.6.4.- (DNA Helicases); EC 3.6.4.12 (RUVBL1 protein, human)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170228
[St] Status:MEDLINE


  9 / 293 MEDLINE  
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[PMID]:28231279
[Au] Autor:Rollins M; Huard S; Morettin A; Takuski J; Pham TT; Fullerton MD; Côté J; Baetz K
[Ad] Endereço:Ottawa Institute of Systems Biology, uOttawa, Ottawa, Ontario, Canada.
[Ti] Título:Lysine acetyltransferase NuA4 and acetyl-CoA regulate glucose-deprived stress granule formation in Saccharomyces cerevisiae.
[So] Source:PLoS Genet;13(2):e1006626, 2017 Feb.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Eukaryotic cells form stress granules under a variety of stresses, however the signaling pathways regulating their formation remain largely unknown. We have determined that the Saccharomyces cerevisiae lysine acetyltransferase complex NuA4 is required for stress granule formation upon glucose deprivation but not heat stress. Further, the Tip60 complex, the human homolog of the NuA4 complex, is required for stress granule formation in cancer cell lines. Surprisingly, the impact of NuA4 on glucose-deprived stress granule formation is partially mediated through regulation of acetyl-CoA levels, which are elevated in NuA4 mutants. While elevated acetyl-CoA levels suppress the formation of glucose-deprived stress granules, decreased acetyl-CoA levels enhance stress granule formation upon glucose deprivation. Further our work suggests that NuA4 regulates acetyl-CoA levels through the Acetyl-CoA carboxylase Acc1. Altogether this work establishes both NuA4 and the metabolite acetyl-CoA as critical signaling pathways regulating the formation of glucose-deprived stress granules.
[Mh] Termos MeSH primário: Acetilcoenzima A/genética
Acetiltransferases/genética
Glucose/metabolismo
Histona Acetiltransferases/genética
Proteínas de Saccharomyces cerevisiae/genética
[Mh] Termos MeSH secundário: Histona Acetiltransferases/biossíntese
Histona Acetiltransferases/metabolismo
Seres Humanos
Lisina Acetiltransferase 5
Proteínas Mutantes/biossíntese
Proteínas Mutantes/genética
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/biossíntese
Proteínas de Saccharomyces cerevisiae/metabolismo
Transdução de Sinais
Estresse Fisiológico/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Mutant Proteins); 0 (Saccharomyces cerevisiae Proteins); 72-89-9 (Acetyl Coenzyme A); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.- (aminoglycoside N1-acetyltransferase); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.48 (KAT5 protein, human); EC 2.3.1.48 (Lysine Acetyltransferase 5); EC 2.3.1.48 (NuA4 protein, S cerevisiae); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170224
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006626


  10 / 293 MEDLINE  
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[PMID]:27743347
[Au] Autor:Zeng S; Wang Y; Zhang T; Bai L; Wang Y; Duan C
[Ad] Endereço:Department of Cell Biology and Medical Genetics, Molecular Medicine and Cancer Research Center, Chongqing Medical University, Chongqing, 400016, China.
[Ti] Título:E3 ligase UHRF2 stabilizes the acetyltransferase TIP60 and regulates H3K9ac and H3K14ac via RING finger domain.
[So] Source:Protein Cell;8(3):202-218, 2017 Mar.
[Is] ISSN:1674-8018
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:UHRF2 is a ubiquitin-protein ligase E3 that regulates cell cycle, genomic stability and epigenetics. We conducted a co-immunoprecipitation assay and found that TIP60 and HDAC1 interact with UHRF2. We previously demonstrated that UHRF2 regulated H3K9ac and H3K14ac differentially in normal and cancer cells. However, the accurate signal transduction mechanisms were not clear. In this study, we found that TIP60 acted downstream of UHRF2 to regulate H3K9ac and H3K14ac expression. TIP60 is stabilized in normal cells by UHRF2 ubiquitination. However, TIP60 is destabilized in cancer cells. Depletion or inhibition of TIP60 disrupts the regulatory relationship between UHRF2, H3K9ac and H3K14ac. In summary, the findings suggest that UHRF2 mediated the post-translational modification of histones and the initiation and progression of cancer.
[Mh] Termos MeSH primário: Histona Acetiltransferases/metabolismo
Histonas/metabolismo
Proteínas de Neoplasias/metabolismo
Neoplasias/metabolismo
Ubiquitina-Proteína Ligases/metabolismo
Ubiquitinação
[Mh] Termos MeSH secundário: Linhagem Celular
Histona Acetiltransferases/genética
Histonas/genética
Seres Humanos
Lisina Acetiltransferase 5
Proteínas de Neoplasias/genética
Neoplasias/genética
Domínios RING Finger
Ubiquitina-Proteína Ligases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Histones); 0 (Neoplasm Proteins); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.48 (KAT5 protein, human); EC 2.3.1.48 (Lysine Acetyltransferase 5); EC 2.3.2.27 (UHRF2 protein, human); EC 2.3.2.27 (Ubiquitin-Protein Ligases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161016
[St] Status:MEDLINE
[do] DOI:10.1007/s13238-016-0324-z



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