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Pesquisa : D12.776.930.780.625 [Categoria DeCS]
Referências encontradas : 530 [refinar]
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[PMID]:28832116
[Au] Autor:Dhall A; Weller CE; Chu A; Shelton PMM; Chatterjee C
[Ad] Endereço:Department of Chemistry, University of Washington , Seattle, Washington 98195, United States.
[Ti] Título:Chemically Sumoylated Histone H4 Stimulates Intranucleosomal Demethylation by the LSD1-CoREST Complex.
[So] Source:ACS Chem Biol;12(9):2275-2280, 2017 Sep 15.
[Is] ISSN:1554-8937
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lysine-specific demethylase 1 (LSD1) downregulates eukaryotic gene activity by demethylating mono- and dimethylated Lys4 in histone H3. Elucidating the biochemical crosstalk of LSD1 with histone post-translational modifications (PTMs) is essential for developing LSD1-targeted therapeutics in human cancers. We interrogated the small ubiquitin-like modifier (SUMO)-driven regulation of LSD1 activity with semisynthetic nucleosomes containing site-specifically methylated and sumoylated histones. We discovered that nucleosomes containing sumoylated histone H4 (suH4), a modification associated with gene repression, stimulate LSD1 activity by a mechanism dependent upon the SUMO-interaction motif in CoREST. Furthermore, the stimulatory effect of suH4 was spatially limited and did not extend to the demethylation of adjacent nonsumoylated nucleosomes. Thus, we have identified histone modification by SUMO as the first PTM that stimulates intranucleosomal demethylation by the developmentally critical LSD1-CoREST complex.
[Mh] Termos MeSH primário: Proteínas Correpressoras/metabolismo
Histona Desmetilases/metabolismo
Histonas/metabolismo
Proteínas do Tecido Nervoso/metabolismo
Sumoilação
[Mh] Termos MeSH secundário: Seres Humanos
Metilação
Simulação de Acoplamento Molecular
Nucleossomos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Co-Repressor Proteins); 0 (Histones); 0 (Nerve Tissue Proteins); 0 (Nucleosomes); 0 (RCOR1 protein, human); EC 1.14.11.- (Histone Demethylases); EC 1.5.- (KDM1A protein, human)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170824
[St] Status:MEDLINE
[do] DOI:10.1021/acschembio.7b00716


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[PMID]:28803779
[Au] Autor:Liu S; Yu H; Liu Y; Liu X; Zhang Y; Bu C; Yuan S; Chen Z; Xie G; Li W; Xu B; Yang J; He L; Jin T; Xiong Y; Sun L; Liu X; Han C; Cheng Z; Liang J; Shang Y
[Ad] Endereço:Key Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing 100191, China; Department of Biochemistry and Molecular Biology, School of Basic M
[Ti] Título:Chromodomain Protein CDYL Acts as a Crotonyl-CoA Hydratase to Regulate Histone Crotonylation and Spermatogenesis.
[So] Source:Mol Cell;67(5):853-866.e5, 2017 Sep 07.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lysine crotonylation (Kcr) is a newly identified histone modification that is associated with active transcription in mammalian cells. Here we report that the chromodomain Y-like transcription corepressor CDYL negatively regulates histone Kcr by acting as a crotonyl-CoA hydratase to convert crotonyl-CoA to ß-hydroxybutyryl-CoA. We showed that the negative regulation of histone Kcr by CDYL is intrinsically linked to its transcription repression activity and functionally implemented in the reactivation of sex chromosome-linked genes in round spermatids and genome-wide histone replacement in elongating spermatids. Significantly, Cdyl transgenic mice manifest dysregulation of histone Kcr and reduction of male fertility with a decreased epididymal sperm count and sperm cell motility. Our study uncovers a biochemical pathway in the regulation of histone Kcr and implicates CDYL-regulated histone Kcr in spermatogenesis, adding to the understanding of the physiology of male reproduction and the mechanism of the spermatogenic failure in AZFc (Azoospermia Factor c)-deleted infertile men.
[Mh] Termos MeSH primário: Acil Coenzima A/metabolismo
Proteínas Correpressoras/metabolismo
Enoil-CoA Hidratase/metabolismo
Histona Acetiltransferases/metabolismo
Histonas/metabolismo
Infertilidade Masculina/enzimologia
Processamento de Proteína Pós-Traducional
Proteínas/metabolismo
Espermatogênese
Espermatozoides/enzimologia
Testículo/enzimologia
[Mh] Termos MeSH secundário: Animais
Proteínas Correpressoras/genética
Enoil-CoA Hidratase/genética
Fertilidade
Predisposição Genética para Doença
Células HeLa
Histona Acetiltransferases/genética
Seres Humanos
Infertilidade Masculina/genética
Infertilidade Masculina/patologia
Infertilidade Masculina/fisiopatologia
Cinética
Lisina
Masculino
Camundongos Endogâmicos C57BL
Camundongos Transgênicos
Fenótipo
Domínios Proteicos
Proteínas/genética
Interferência de RNA
Células Sf9
Contagem de Espermatozoides
Motilidade Espermática
Espermatozoides/patologia
Testículo/patologia
Testículo/fisiopatologia
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (CDYL protein, human); 0 (Co-Repressor Proteins); 0 (Histones); 0 (Proteins); 2871-66-1 (3-hydroxybutyryl-coenzyme A); 992-67-6 (crotonyl-coenzyme A); EC 2.3.1.48 (Cdyl protein, mouse); EC 2.3.1.48 (Histone Acetyltransferases); EC 4.2.1.17 (Enoyl-CoA Hydratase); K3Z4F929H6 (Lysine)
[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:170815
[St] Status:MEDLINE


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[PMID]:28689657
[Au] Autor:Flack JE; Mieszczanek J; Novcic N; Bienz M
[Ad] Endereço:MRC Laboratory of Molecular Biology, Cambridge Biomedical Campus, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
[Ti] Título:Wnt-Dependent Inactivation of the Groucho/TLE Co-repressor by the HECT E3 Ubiquitin Ligase Hyd/UBR5.
[So] Source:Mol Cell;67(2):181-193.e5, 2017 Jul 20.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Extracellular signals are transduced to the cell nucleus by effectors that bind to enhancer complexes to operate transcriptional switches. For example, the Wnt enhanceosome is a multiprotein complex associated with Wnt-responsive enhancers through T cell factors (TCF) and kept silent by Groucho/TLE co-repressors. Wnt-activated ß-catenin binds to TCF to overcome this repression, but how it achieves this is unknown. Here, we discover that this process depends on the HECT E3 ubiquitin ligase Hyd/UBR5, which is required for Wnt signal responses in Drosophila and human cell lines downstream of activated Armadillo/ß-catenin. We identify Groucho/TLE as a functionally relevant substrate, whose ubiquitylation by UBR5 is induced by Wnt signaling and conferred by ß-catenin. Inactivation of TLE by UBR5-dependent ubiquitylation also involves VCP/p97, an AAA ATPase regulating the folding of various cellular substrates including ubiquitylated chromatin proteins. Thus, Groucho/TLE ubiquitylation by Hyd/UBR5 is a key prerequisite that enables Armadillo/ß-catenin to activate transcription.
[Mh] Termos MeSH primário: Fatores de Transcrição Hélice-Alça-Hélice Básicos/metabolismo
Proteínas Correpressoras/metabolismo
Proteínas de Drosophila/metabolismo
Drosophila melanogaster/enzimologia
Proteínas Repressoras/metabolismo
Transcrição Genética
Ubiquitina-Proteína Ligases/metabolismo
Via de Sinalização Wnt
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/genética
Adenosina Trifosfatases/metabolismo
Animais
Animais Geneticamente Modificados
Proteínas do Domínio Armadillo/genética
Proteínas do Domínio Armadillo/metabolismo
Fatores de Transcrição Hélice-Alça-Hélice Básicos/genética
Sistemas CRISPR-Cas
Proteínas de Ciclo Celular/genética
Proteínas de Ciclo Celular/metabolismo
Proteínas Correpressoras/genética
Proteínas de Drosophila/genética
Drosophila melanogaster/genética
Técnicas de Silenciamento de Genes
Células HCT116
Células HEK293
Células HeLa
Seres Humanos
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Estabilidade Proteica
Proteólise
Proteínas Repressoras/genética
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
Ativação Transcricional
Transfecção
Ubiquitina-Proteína Ligases/genética
Ubiquitinação
Proteína com Valosina
beta Catenina/genética
beta Catenina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Armadillo Domain Proteins); 0 (Basic Helix-Loop-Helix Transcription Factors); 0 (CTNNB1 protein, human); 0 (Cell Cycle Proteins); 0 (Co-Repressor Proteins); 0 (Drosophila Proteins); 0 (Repressor Proteins); 0 (TLE3 protein, human); 0 (Transcription Factors); 0 (armadillo protein, Drosophila); 0 (beta Catenin); 0 (groucho protein, Drosophila); EC 2.3.2.26 (UBR5 protein, human); EC 2.3.2.26 (hyperplastic discs protein, Drosophila); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.4.6 (VCP protein, human); EC 3.6.4.6 (Valosin Containing Protein); EC 3.6.4.6 (ter94 protein, Drosophila)
[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:170711
[St] Status:MEDLINE


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[PMID]:28607151
[Au] Autor:Kokabu S; Nakatomi C; Matsubara T; Ono Y; Addison WN; Lowery JW; Urata M; Hudnall AM; Hitomi S; Nakatomi M; Sato T; Osawa K; Yoda T; Rosen V; Jimi E
[Ad] Endereço:From the Divisions of Molecular Signaling and Biochemistry, r14kokabu@fa.kyu-dent.ac.jp.
[Ti] Título:The transcriptional co-repressor TLE3 regulates myogenic differentiation by repressing the activity of the MyoD transcription factor.
[So] Source:J Biol Chem;292(31):12885-12894, 2017 Aug 04.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Satellite cells are skeletal muscle stem cells that provide myonuclei for postnatal muscle growth, maintenance, and repair/regeneration in adults. Normally, satellite cells are mitotically quiescent, but they are activated in response to muscle injury, in which case they proliferate extensively and exhibit up-regulated expression of the transcription factor MyoD, a master regulator of myogenesis. MyoD forms a heterodimer with E proteins through their basic helix-loop-helix domain, binds to E boxes in the genome and thereby activates transcription at muscle-specific promoters. The central role of MyoD in muscle differentiation has increased interest in finding potential MyoD regulators. Here we identified transducin-like enhancer of split (TLE3), one of the Groucho/TLE family members, as a regulator of MyoD function during myogenesis. TLE3 was expressed in activated and proliferative satellite cells in which increased TLE3 levels suppressed myogenic differentiation, and, conversely, reduced TLE3 levels promoted myogenesis with a concomitant increase in proliferation. We found that, via its glutamine- and serine/proline-rich domains, TLE3 interferes with MyoD function by disrupting the association between the basic helix-loop-helix domain of MyoD and E proteins. Our findings indicate that TLE3 participates in skeletal muscle homeostasis by dampening satellite cell differentiation via repression of MyoD transcriptional activity.
[Mh] Termos MeSH primário: Proteínas Correpressoras/metabolismo
Regulação da Expressão Gênica no Desenvolvimento
Desenvolvimento Muscular
Fibras Musculares Esqueléticas/metabolismo
Proteína MyoD/antagonistas & inibidores
Mioblastos/metabolismo
Células Satélites de Músculo Esquelético/metabolismo
[Mh] Termos MeSH secundário: Fator 3 Ativador da Transcrição/química
Fator 3 Ativador da Transcrição/genética
Fator 3 Ativador da Transcrição/metabolismo
Animais
Proliferação Celular
Células Cultivadas
Proteínas Correpressoras/antagonistas & inibidores
Proteínas Correpressoras/química
Proteínas Correpressoras/genética
Deleção de Genes
Sequências Hélice-Alça-Hélice
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Fibras Musculares Esqueléticas/citologia
Proteína MyoD/química
Proteína MyoD/genética
Proteína MyoD/metabolismo
Mioblastos/citologia
Fragmentos de Peptídeos/antagonistas & inibidores
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Interferência de RNA
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Células Satélites de Músculo Esquelético/citologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Activating Transcription Factor 3); 0 (Atf3 protein, mouse); 0 (Co-Repressor Proteins); 0 (MyoD Protein); 0 (MyoD1 myogenic differentiation protein); 0 (Peptide Fragments); 0 (Recombinant Fusion Proteins); 0 (Recombinant Proteins); 0 (Tle3 protein, mouse)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170825
[Lr] Data última revisão:
170825
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170614
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.774570


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[PMID]:28478957
[Au] Autor:Gupta P; Sheikh T; Sen E
[Ad] Endereço:National Brain Research Centre, Manesar, Haryana 122051, India.
[Ti] Título:SIRT6 regulated nucleosomal occupancy affects Hexokinase 2 expression.
[So] Source:Exp Cell Res;357(1):98-106, 2017 Aug 01.
[Is] ISSN:1090-2422
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:To understand the molecular association between inflammation and dysregulated metabolism in glioblastoma, the effect of IL-1ß on Hexokinase 2 (HK2) expression was investigated. IL-1ß induced HK2 expression was accompanied by heightened SIRT6 and MZF1 levels. IL-1ß mediated overall decrease in chromatin compactness on HK2 promoter involved diminished nucleosomal occupancy around the most labile region bearing MZF1 sites. Importantly, SIRT6 and MZF1 served as negative regulators of HK2. Ectopic SIRT6 induced formation and recruitment of MZF1-SIRT6 complex to MZF1 site was concomitant with increased nucleosomal occupancy. The function of SIRT6 as co-repressor of MZF1 was inconspicuous in cells treated with IL-1ß alone, as IL-1ß-induced HIF-1α prevented SIRT6 availability for interaction with MZF1. Taken together, SIRT6 over-expression establishes a condition whereby reconfiguration of the HK2 promoter chromatin structure makes it receptive to interaction with MZF1/SIRT6 complex, thereby favouring a regulatory state conducive to diminished transcription.
[Mh] Termos MeSH primário: Regulação Neoplásica da Expressão Gênica/fisiologia
Hexoquinase/metabolismo
Fatores de Transcrição Kruppel-Like/metabolismo
Nucleossomos/metabolismo
Sirtuínas/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Proteínas Correpressoras/metabolismo
Seres Humanos
Subunidade alfa do Fator 1 Induzível por Hipóxia/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Co-Repressor Proteins); 0 (Hypoxia-Inducible Factor 1, alpha Subunit); 0 (Kruppel-Like Transcription Factors); 0 (MZF1 protein, human); 0 (Nucleosomes); EC 2.7.1.1 (Hexokinase); EC 2.7.1.1 (hexokinase 2, human); EC 3.5.1.- (SIRT6 protein, human); EC 3.5.1.- (Sirtuins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171003
[Lr] Data última revisão:
171003
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170509
[St] Status:MEDLINE


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[PMID]:28325473
[Au] Autor:Charney RM; Forouzmand E; Cho JS; Cheung J; Paraiso KD; Yasuoka Y; Takahashi S; Taira M; Blitz IL; Xie X; Cho KW
[Ad] Endereço:Department of Developmental and Cell Biology, Ayala School of Biological Sciences, University of California, Irvine, CA 92697, USA.
[Ti] Título:Foxh1 Occupies cis-Regulatory Modules Prior to Dynamic Transcription Factor Interactions Controlling the Mesendoderm Gene Program.
[So] Source:Dev Cell;40(6):595-607.e4, 2017 Mar 27.
[Is] ISSN:1878-1551
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The interplay between transcription factors and chromatin dictates gene regulatory network activity. Germ layer specification is tightly coupled with zygotic gene activation and, in most metazoans, is dependent upon maternal factors. We explore the dynamic genome-wide interactions of Foxh1, a maternal transcription factor that mediates Nodal/TGF-ß signaling, with cis-regulatory modules (CRMs) during mesendodermal specification. Foxh1 marks CRMs during cleavage stages and recruits the co-repressor Tle/Groucho in the early blastula. We highlight a population of CRMs that are continuously occupied by Foxh1 and show that they are marked by H3K4me1, Ep300, and Fox/Sox/Smad motifs, suggesting interplay between these factors in gene regulation. We also propose a molecular "hand-off" between maternal Foxh1 and zygotic Foxa at these CRMs to maintain enhancer activation. Our findings suggest that Foxh1 functions at the top of a hierarchy of interactions by marking developmental genes for activation, beginning with the onset of zygotic gene expression.
[Mh] Termos MeSH primário: Endoderma/metabolismo
Fatores de Transcrição Forkhead/metabolismo
Regulação da Expressão Gênica no Desenvolvimento
Mesoderma/metabolismo
Fatores de Transcrição/metabolismo
Proteínas de Xenopus/metabolismo
Xenopus/embriologia
Xenopus/genética
[Mh] Termos MeSH secundário: Animais
Blástula/metabolismo
Fase de Clivagem do Zigoto/metabolismo
Proteínas Correpressoras/metabolismo
Embrião não Mamífero/metabolismo
Endoderma/embriologia
Elementos Facilitadores Genéticos/genética
Fatores de Transcrição Forkhead/genética
Genoma
Histonas/metabolismo
Lisina/metabolismo
Mesoderma/embriologia
Metilação
Proteína Nodal/metabolismo
Ligação Proteica/genética
RNA Polimerase II/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Sequências Reguladoras de Ácido Nucleico/genética
Análise de Sequência de RNA
Transdução de Sinais/genética
Transcrição Genética
Xenopus/metabolismo
Proteínas de Xenopus/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Co-Repressor Proteins); 0 (FOXH1 protein, Xenopus); 0 (Forkhead Transcription Factors); 0 (Histones); 0 (Nodal Protein); 0 (RNA, Messenger); 0 (Transcription Factors); 0 (Xenopus Proteins); EC 2.7.7.- (RNA Polymerase II); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170619
[Lr] Data última revisão:
170619
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170323
[St] Status:MEDLINE


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[PMID]:28279208
[Au] Autor:Du L; Ning Z; Zhang H; Liu F
[Ad] Endereço:Cancer Research Center, Shantou University Medical College, Shantou, 515031, Guangdong, P. R. China.
[Ti] Título:Corepressor metastasis-associated protein 3 modulates epithelial-to-mesenchymal transition and metastasis.
[So] Source:Chin J Cancer;36(1):28, 2017 Mar 09.
[Is] ISSN:1944-446X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Worldwide, metastasis is the leading cause of more than 90% of cancer-related deaths. Currently, no specific therapies effectively impede metastasis. Metastatic processes are controlled by complex regulatory networks and transcriptional hierarchy. Corepressor metastasis-associated protein 3 (MTA3) has been confirmed as a novel component of nucleosome remodeling and histone deacetylation (NuRD). Increasing evidence supports the theory that, in the recruitment of transcription factors, coregulators function as master regulators rather than passive passengers. As a master regulator, MTA3 governs the target selection for NuRD and functions as a transcriptional repressor. MTA3 dysregulation is associated with tumor progression, invasion, and metastasis in various cancers. MTA3 is also a key regulator of E-cadherin expression and epithelial-to-mesenchymal transition. Elucidating the functions of MTA3 might help to find additional therapeutic approaches for targeting components of NuRD.
[Mh] Termos MeSH primário: Proteínas Correpressoras/fisiologia
Transição Epitelial-Mesenquimal
Metástase Neoplásica/fisiopatologia
Proteínas de Neoplasias/fisiologia
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Neoplasias/patologia
Neoplasias/fisiopatologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Co-Repressor Proteins); 0 (MTA3 protein, human); 0 (Neoplasm Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170311
[St] Status:MEDLINE
[do] DOI:10.1186/s40880-017-0193-8


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[PMID]:28181322
[Au] Autor:Geng X; Horst WJ; Golz JF; Lee JE; Ding Z; Yang ZB
[Ad] Endereço:The Key Laboratory of Plant Cell Engineering and Germplasm Innovation, Ministry of Education, School of Life Science, Shandong University, Jinan, 250100, China.
[Ti] Título:LEUNIG_HOMOLOG transcriptional co-repressor mediates aluminium sensitivity through PECTIN METHYLESTERASE46-modulated root cell wall pectin methylesterification in Arabidopsis.
[So] Source:Plant J;90(3):491-504, 2017 May.
[Is] ISSN:1365-313X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A major factor determining aluminium (Al) sensitivity in higher plants is the binding of Al to root cell walls. The Al binding capacity of cell walls is closely linked to the extent of pectin methylesterification, as the presence of methyl groups attached to the pectin backbone reduces the net negative charge of this polymer and hence limits Al binding. Despite recent progress in understanding the molecular basis of Al resistance in a wide range of plants, it is not well understood how the methylation status of pectin is mediated in response to Al stress. Here we show in Arabidopsis that mutants lacking the gene LEUNIG_HOMOLOG (LUH), a member of the Groucho-like family of transcriptional co-repressor, are less sensitive to Al-mediated repression of root growth. This phenotype is correlated with increased levels of methylated pectin in the cell walls of luh roots as well as altered expression of cell wall-related genes. Among the LUH-repressed genes, PECTIN METHYLESTERASE46 (PME46) was identified as reducing Al binding to cell walls and hence alleviating Al-induced root growth inhibition by decreasing PME enzyme activity. seuss-like2 (slk2) mutants responded to Al in a similar way as luh mutants suggesting that a LUH-SLK2 complex represses the expression of PME46. The data are integrated into a model in which it is proposed that PME46 is a major inhibitor of pectin methylesterase activity within root cell walls.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/metabolismo
Hidrolases de Éster Carboxílico/metabolismo
Parede Celular/metabolismo
Proteínas Correpressoras/metabolismo
Pectinas/metabolismo
Raízes de Plantas/metabolismo
Proteínas Repressoras/metabolismo
[Mh] Termos MeSH secundário: Arabidopsis/genética
Proteínas de Arabidopsis/genética
Hidrolases de Éster Carboxílico/genética
Proteínas Correpressoras/genética
Regulação da Expressão Gênica de Plantas
Raízes de Plantas/genética
Plantas Geneticamente Modificadas
Proteínas Repressoras/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Co-Repressor Proteins); 0 (LUH protein, Arabidopsis); 0 (Pectins); 0 (Repressor Proteins); 89NA02M4RX (pectin); EC 3.1.1.- (Carboxylic Ester Hydrolases); EC 3.1.1.11 (pectinesterase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170628
[Lr] Data última revisão:
170628
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170210
[St] Status:MEDLINE
[do] DOI:10.1111/tpj.13506


  9 / 530 MEDLINE  
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[PMID]:28107193
[Au] Autor:Guan H; Liu C; Fang F; Huang Y; Tao T; Ling Z; You Z; Han X; Chen S; Xu B; Chen M
[Ad] Endereço:Department of Urology, Affiliated Zhongda Hospital of Southeast University, Nanjing, China.
[Ti] Título:MicroRNA-744 promotes prostate cancer progression through aberrantly activating Wnt/ß-catenin signaling.
[So] Source:Oncotarget;8(9):14693-14707, 2017 Feb 28.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Accumulated evidence indicate that miR-744 functions as either tumor suppressor or oncogene in the progression of a variety of tumors, with a tumor type-specific way. However, little is known about how miR-744 impacts on the tumorigenesis of human prostate cancer. In this study, employing the analyses of microarray, qRT-PCR and re-analysis of MSKCC data, we found that CRPC tissues expressed much more miR-744 than ADPC tissues did, and the expression level of miR-744 was inversely associated with survival of CRPC patients. In vitro studies revealed that miR-744 promotes PCa cells proliferation, enhances migration, invasion; in vivo results demonstrated that silencing of miR-744 mediated by shRNA dramatically reduces PCa xenograft tumor growth. Importantly, through human gene expression array, pathway enrichment analysis and Western blot, we identified that miR-744 dramatically activated Wnt/ß-catenin pathway by targeting multiple negative regulators of Wnt/ß-catenin signaling, including SFRP1, GSK3ß, TLE3 and NKD1. At molecular level, we further defined that NKD1 is a major functional target of miR-744. Our findings indicate that miR-744 acts as one of oncogenic factor in the progression of CRPC by recruiting a mechanism of aberrant activation of Wnt/ß-catenin signaling.
[Mh] Termos MeSH primário: Regulação Neoplásica da Expressão Gênica
MicroRNAs/genética
Neoplasias da Próstata/genética
Via de Sinalização Wnt/genética
[Mh] Termos MeSH secundário: Animais
Apoptose/genética
Sequência de Bases
Western Blotting
Proteínas de Transporte/genética
Proteínas de Transporte/metabolismo
Linhagem Celular Tumoral
Proteínas Correpressoras/genética
Proteínas Correpressoras/metabolismo
Progressão da Doença
Feminino
Perfilação da Expressão Gênica/métodos
Glicogênio Sintase Quinase 3 beta/genética
Glicogênio Sintase Quinase 3 beta/metabolismo
Peptídeos e Proteínas de Sinalização Intercelular/genética
Peptídeos e Proteínas de Sinalização Intercelular/metabolismo
Masculino
Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
Camundongos Endogâmicos BALB C
Camundongos Nus
Neoplasias da Próstata/metabolismo
Neoplasias da Próstata/patologia
Interferência de RNA
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Homologia de Sequência do Ácido Nucleico
Transplante Heterólogo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Co-Repressor Proteins); 0 (Intercellular Signaling Peptides and Proteins); 0 (MIRN744 microRNA, human); 0 (Membrane Proteins); 0 (MicroRNAs); 0 (NKD1 protein, human); 0 (SFRP1 protein, human); 0 (TLE3 protein, human); EC 2.7.11.1 (Glycogen Synthase Kinase 3 beta)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170818
[Lr] Data última revisão:
170818
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170121
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.14711


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[PMID]:28095483
[Au] Autor:Wu S; Teng MS; Er LK; Hsiao WY; Hsu LA; Yeh CH; Lin JF; Lin YY; Su CW; Ko YL
[Ad] Endereço:Department of Life Science, Chinese Culture University, Taipei, Taiwan.
[Ti] Título:Association between NF-κB Pathway Gene Variants and sICAM1 Levels in Taiwanese.
[So] Source:PLoS One;12(1):e0169516, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Intercellular adhesion molecule-1 (ICAM1) is crucial to the development and progression of atherosclerosis. Recent genome-wide association studies (GWAS) have revealed that single nucleotide polymorphisms (SNPs) in two of the nuclear factor-κB (NF-κB) pathway genes, NFKBIK and RELA, are associated with soluble ICAM1 (sICAM1) levels. However, neither of these two gene variants is found in the Asian populations. This study aimed to elucidate whether other candidate gene variants involved in the NF-κB pathway may be associated with sICAM1 levels in Taiwanese. After excluding carriers of the ICAM1 rs5491-T allele, three SNPs in the ICAM1 gene and eight SNPs in six of the NF-κB pathway genes (NFKB1, PDCD11, TNFAIP3, NKAPL, IKBKE, and PRKCB) were analyzed for their association with sICAM1 levels in 480 individuals. Our data showed that two SNPs, rs5498 of ICAM1 and rs1635 of NKAPL, were significantly associated with sICAM1 levels (P = 0.002 and 0.004, respectively) in the Taiwanese population. Using a multivariate analysis, rs5498 and rs1635 as well as the previously reported ABO genotypes and rs12051272 of the CDH13 gene were independently associated with sICAM1 levels (P = 0.001, 0.001, 0.006 and 0.031, respectively). An analysis with combined risk alleles of four candidate SNPs in the ICAM1, NKAPL, ABO, and CDH13 genes showed an increase in sICAM1 levels with added numbers of risk alleles and weighted genetic risk score. Our findings thus expanded the repertoire of gene variants responsible for the regulation of sICAM1 levels in the Asian populations.
[Mh] Termos MeSH primário: Doenças Cardiovasculares/genética
Proteínas Correpressoras/genética
Diabetes Mellitus/genética
Molécula 1 de Adesão Intercelular/sangue
Molécula 1 de Adesão Intercelular/genética
NF-kappa B/genética
Proteínas Nucleares/genética
Polimorfismo de Nucleotídeo Único/genética
[Mh] Termos MeSH secundário: Adulto
Biomarcadores/metabolismo
Doenças Cardiovasculares/sangue
Doenças Cardiovasculares/epidemiologia
Diabetes Mellitus/sangue
Diabetes Mellitus/epidemiologia
Feminino
Seres Humanos
Masculino
Meia-Idade
Taiwan/epidemiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Co-Repressor Proteins); 0 (ICAM1 protein, human); 0 (NF-kappa B); 0 (NKAPL protein, human); 0 (Nuclear Proteins); 126547-89-5 (Intercellular Adhesion Molecule-1)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170118
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0169516



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