Base de dados : MEDLINE
Pesquisa : D08.811.913.050.134.415.500.575 [Categoria DeCS]
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[PMID]:29232376
[Au] Autor:Caliskan G; Baris IC; Ayaydin F; Dobson MJ; Senarisoy M; Boros IM; Topcu Z; Zencir S
[Ad] Endereço:Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Ege University, Izmir, Turkey.
[Ti] Título:Che1/AATF interacts with subunits of the histone acetyltransferase core module of SAGA complexes.
[So] Source:PLoS One;12(12):e0189193, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:General Control Non-derepressible 5 (GCN5) and Alteration/Deficiency in Activation 2 and 3 proteins (ADA2 and ADA3, respectively) are subunits of the Histone AcetylTransferase (HAT) module of SAGA- and ATAC-type co-activators. We previously reported four new interacting partners of human ADA3 identified by screening a human fetal brain cDNA library using yeast two hybrid technology. One of these partners was Apoptosis-Antagonizing Transcription Factor (AATF), also known as Che-1, an RNA polymerase II-binding protein with a number of roles in different cellular processes including regulation of transcription, cell proliferation, cell cycle control, DNA damage responses and apoptosis. Che-1/AATF is a potential therapeutic target for cancer treatments. In this study, we aimed to identify whether besides ADA3, other components of the HAT modules of SAGA and ATAC complexes, human ADA2 and GCN5 also interact with Che-1/AATF. Co-immunoprecipitation and co-localization experiments were used to demonstrate association of AATF both with two ADA2 isoforms, ADA2A and ADA2B and with GCN5 proteins in human cells and yeast two-hybrid assays to delineate domains in the ADA2 and GCN5 proteins required for these interactions. These findings provide new insights into the pathways regulated by ADA-containing protein complexes.
[Mh] Termos MeSH primário: Histona Acetiltransferases/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
Transativadores/metabolismo
[Mh] Termos MeSH secundário: Acetiltransferases/metabolismo
Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Seres Humanos
Ligação Proteica
Fatores de Transcrição/metabolismo
Ativação Transcricional
Fatores de Transcrição de p300-CBP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (SAGA complex, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (TADA2A protein, human); 0 (TADA2B protein, human); 0 (Trans-Activators); 0 (Transcription Factors); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.- (Sgf29 protein, human); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.48 (p300-CBP Transcription Factors); EC 2.3.1.48 (p300-CBP-associated factor)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180104
[Lr] Data última revisão:
180104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171213
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189193


  2 / 1566 MEDLINE  
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[PMID]:29033323
[Au] Autor:Wan W; You Z; Xu Y; Zhou L; Guan Z; Peng C; Wong CCL; Su H; Zhou T; Xia H; Liu W
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Program in Molecular and Cell Biology, Zhejiang University School of Medicine, Hangzhou 310058, China.
[Ti] Título:mTORC1 Phosphorylates Acetyltransferase p300 to Regulate Autophagy and Lipogenesis.
[So] Source:Mol Cell;68(2):323-335.e6, 2017 Oct 19.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Acetylation is increasingly recognized as one of the major post-translational mechanisms for the regulation of multiple cellular functions in mammalian cells. Acetyltransferase p300, which acetylates histone and non-histone proteins, has been intensively studied in its role in cell growth and metabolism. However, the mechanism underlying the activation of p300 in cells remains largely unknown. Here, we identify the homeostatic sensor mTORC1 as a direct activator of p300. Activated mTORC1 interacts with p300 and phosphorylates p300 at 4 serine residues in the C-terminal domain. Mechanistically, phosphorylation of p300 by mTORC1 prevents the catalytic HAT domain from binding to the RING domain, thereby eliminating intra-molecular inhibition. Functionally, mTORC1-dependent phosphorylation of p300 suppresses cell-starvation-induced autophagy and activates cell lipogenesis. These results uncover p300 as a direct target of mTORC1 and suggest that the mTORC1-p300 pathway plays a pivotal role in cell metabolism by coordinately controlling cell anabolism and catabolism.
[Mh] Termos MeSH primário: Autofagia
Lipogênese
Complexos Multiproteicos/metabolismo
Serina-Treonina Quinases TOR/metabolismo
Fatores de Transcrição de p300-CBP/metabolismo
[Mh] Termos MeSH secundário: Animais
Células HEK293
Células HeLa
Células Hep G2
Seres Humanos
Alvo Mecanístico do Complexo 1 de Rapamicina
Camundongos
Complexos Multiproteicos/genética
Fosforilação/genética
Domínios Proteicos
Serina-Treonina Quinases TOR/genética
Fatores de Transcrição de p300-CBP/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Multiprotein Complexes); EC 2.3.1.48 (p300-CBP Transcription Factors); EC 2.3.1.48 (p300-CBP-associated factor); EC 2.7.1.1 (TOR Serine-Threonine Kinases); EC 2.7.11.1 (Mechanistic Target of Rapamycin Complex 1)
[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:171017
[St] Status:MEDLINE


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[PMID]:29016683
[Au] Autor:de Jong RCM; Ewing MM; de Vries MR; Karper JC; Bastiaansen AJNM; Peters HAB; Baghana F; van den Elsen PJ; Gongora C; Jukema JW; Quax PHA
[Ad] Endereço:Department of Surgery, Leiden University Medical Center (LUMC), Leiden, The Netherlands.
[Ti] Título:The epigenetic factor PCAF regulates vascular inflammation and is essential for intimal hyperplasia development.
[So] Source:PLoS One;12(10):e0185820, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: Genetic P300/CBP-associated factor (PCAF) variation affects restenosis-risk in patients. PCAF has lysine acetyltransferase activity and promotes nuclear factor kappa-beta (NFκB)-mediated inflammation, which drives post-interventional intimal hyperplasia development. We studied the contributing role of PCAF in post-interventional intimal hyperplasia. METHODS AND RESULTS: PCAF contribution to inflammation and intimal hyperplasia was assessed in leukocytes, macrophages and vascular smooth muscle cells (vSMCs) in vitro and in a mouse model for intimal hyperplasia, in which a cuff is placed around the femoral artery. PCAF deficiency downregulate CCL2, IL-6 and TNF-alpha expression, as demonstrated on cultured vSMCs, leukocytes and macrophages. PCAF KO mice showed a 71.8% reduction of vSMC-rich intimal hyperplasia, a 73.4% reduction of intima/media ratio and a 63.7% reduction of luminal stenosis after femoral artery cuff placement compared to wild type (WT) mice. The association of PCAF and vascular inflammation was further investigated using the potent natural PCAF inhibitor garcinol. Garcinol treatment reduced CCL2 and TNF-alpha expression, as demonstrated on cultured vSMCs and leukocytes. To assess the effect of garcinol treatment on vascular inflammation we used hypercholesterolemic ApoE*3-Leiden mice. After cuff placement, garcinol treatment resulted in reduced arterial leukocyte and macrophage adherence and infiltration after three days compared to untreated animals. CONCLUSIONS: These results identify a vital role for the lysine acetyltransferase PCAF in the regulation of local inflammation after arterial injury and likely the subsequent vSMC proliferation, responsible for intimal hyperplasia.
[Mh] Termos MeSH primário: Epigênese Genética
Hiperplasia/prevenção & controle
Terpenos/farmacologia
Vasculite/prevenção & controle
Fatores de Transcrição de p300-CBP/genética
[Mh] Termos MeSH secundário: Animais
Apolipoproteínas E/genética
Apolipoproteínas E/metabolismo
Adesão Celular/efeitos dos fármacos
Quimiocina CCL2/genética
Quimiocina CCL2/metabolismo
Modelos Animais de Doenças
Artéria Femoral/efeitos dos fármacos
Artéria Femoral/metabolismo
Artéria Femoral/patologia
Seres Humanos
Hiperplasia/genética
Hiperplasia/metabolismo
Hiperplasia/patologia
Interleucina-6/genética
Interleucina-6/metabolismo
Leucócitos/efeitos dos fármacos
Leucócitos/metabolismo
Leucócitos/patologia
Macrófagos/efeitos dos fármacos
Macrófagos/metabolismo
Macrófagos/patologia
Masculino
Camundongos
Camundongos Knockout
Miócitos de Músculo Liso/efeitos dos fármacos
Miócitos de Músculo Liso/metabolismo
Miócitos de Músculo Liso/patologia
NF-kappa B/genética
NF-kappa B/metabolismo
Cultura Primária de Células
Transdução de Sinais
Fator de Necrose Tumoral alfa/genética
Fator de Necrose Tumoral alfa/metabolismo
Túnica Íntima/efeitos dos fármacos
Túnica Íntima/metabolismo
Túnica Íntima/patologia
Vasculite/genética
Vasculite/metabolismo
Vasculite/patologia
Fatores de Transcrição de p300-CBP/antagonistas & inibidores
Fatores de Transcrição de p300-CBP/deficiência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apolipoproteins E); 0 (Ccl2 protein, mouse); 0 (Chemokine CCL2); 0 (Interleukin-6); 0 (NF-kappa B); 0 (Terpenes); 0 (Tumor Necrosis Factor-alpha); 0 (interleukin-6, mouse); EC 2.3.1.48 (p300-CBP Transcription Factors); EC 2.3.1.48 (p300-CBP-associated factor); TR1VR1V71B (garcinol)
[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:171011
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185820


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[PMID]:28928281
[Au] Autor:Luo L; Siah CK; Cai Y
[Ad] Endereço:Temasek Life Sciences Laboratory, National University of Singapore, 117604 Singapore.
[Ti] Título:Engrailed acts with Nejire to control expression in the ovarian stem cell niche.
[So] Source:Development;144(18):3224-3231, 2017 09 15.
[Is] ISSN:1477-9129
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Homeostasis of adult tissues is maintained by a small number of stem cells, which are sustained by their niches. In the female germline stem cell (GSC) niche, Decapentaplegic (Dpp) is the primary factor that promotes GSC self-renewal. However, the mechanism regulating expression in the niche is largely unknown. Here, we identify a 2.0 kb fragment located in a 5' -regulatory region of the locus containing enhancer activity that drives its expression in the niche. This region is distinct from a previously characterized 3' -regulatory enhancer responsible for expression in imaginal discs. Our data demonstrate that Engrailed, a homeodomain-containing transcription factor that serves as a cap cell marker, binds to this region and regulates expression in cap cells. Further data suggest that En forms a complex with Nejire (Nej), the ortholog of histone acetyltransferase CBP/p300, and directs Nej to this -regulatory region where Nej functions as the co-activator for expression. Therefore, our study defines the molecular pathway controlling expression in the ovarian stem cell niche.
[Mh] Termos MeSH primário: Proteínas de Drosophila/metabolismo
Drosophila melanogaster/citologia
Drosophila melanogaster/metabolismo
Proteínas de Homeodomínio/metabolismo
Ovário/citologia
Ovário/metabolismo
Nicho de Células-Tronco
Fatores de Transcrição/metabolismo
Fatores de Transcrição de p300-CBP/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas de Drosophila/genética
Feminino
Regulação da Expressão Gênica
Genes Reporter
Ligação Proteica
Sequências Reguladoras de Ácido Nucleico/genética
Nicho de Células-Tronco/genética
Células-Tronco/citologia
Células-Tronco/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (Homeodomain Proteins); 0 (Transcription Factors); 0 (dpp protein, Drosophila); 0 (engrail protein, Drosophila); EC 2.3.1.48 (nejire protein, Drosophila); EC 2.3.1.48 (p300-CBP Transcription Factors)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171126
[Lr] Data última revisão:
171126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170921
[St] Status:MEDLINE
[do] DOI:10.1242/dev.145474


  5 / 1566 MEDLINE  
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[PMID]:28844862
[Au] Autor:Su H; Yang F; Wang Q; Shen Q; Huang J; Peng C; Zhang Y; Wan W; Wong CCL; Sun Q; Wang F; Zhou T; Liu W
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Program in Molecular and Cell Biology, Zhejiang University School of Medicine, Hangzhou 310058, China.
[Ti] Título:VPS34 Acetylation Controls Its Lipid Kinase Activity and the Initiation of Canonical and Non-canonical Autophagy.
[So] Source:Mol Cell;67(6):907-921.e7, 2017 Sep 21.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The class III phosphoinositide 3-kinase VPS34 plays a key role in the regulation of vesicular trafficking and macroautophagy. So far, we know little about the molecular mechanism of VPS34 activation besides its interaction with regulatory proteins to form complexes. Here, we report that VPS34 is specifically acetylated by the acetyltransferase p300, and p300-mediated acetylation represses VPS34 activity. Acetylation at K771 directly diminishes the affinity of VPS34 for its substrate PI, while acetylation at K29 hinders the VPS34-Beclin 1 core complex formation. Inactivation of p300 induces VPS34 deacetylation, PI3P production, and autophagy, even in AMPK , TSC2 , or ULK1 cells. In fasting mice, liver autophagy correlates well with p300 inactivation/VPS34 deacetylation, which facilitates the clearance of lipid droplets in hepatocytes. Thus, p300-dependent VPS34 acetylation/deacetylation is the physiological key to VPS34 activation, which controls the initiation of canonical autophagy and of non-canonical autophagy in which the upstream kinases of VPS34 can be bypassed.
[Mh] Termos MeSH primário: Autofagia
Classe III de Fosfatidilinositol 3-Quinases/metabolismo
Hepatócitos/enzimologia
Metabolismo dos Lipídeos
Fígado/enzimologia
Fosfatidilinositol 3-Quinases/metabolismo
Processamento de Proteína Pós-Traducional
Estresse Fisiológico
Fatores de Transcrição de p300-CBP/metabolismo
[Mh] Termos MeSH secundário: Proteínas Quinases Ativadas por AMP/genética
Proteínas Quinases Ativadas por AMP/metabolismo
Acetilação
Animais
Proteína Homóloga à Proteína-1 Relacionada à Autofagia/genética
Proteína Homóloga à Proteína-1 Relacionada à Autofagia/metabolismo
Beclina-1/metabolismo
Classe III de Fosfatidilinositol 3-Quinases/genética
Ativação Enzimática
Feminino
Células HEK293
Células HeLa
Hepatócitos/patologia
Seres Humanos
Peptídeos e Proteínas de Sinalização Intracelular/genética
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Fígado/patologia
Camundongos Endogâmicos C57BL
Fosfatidilinositol 3-Quinases/genética
Fosfatos de Fosfatidilinositol/metabolismo
Ligação Proteica
Interferência de RNA
Transdução de Sinais
Transfecção
Proteínas Supressoras de Tumor/genética
Proteínas Supressoras de Tumor/metabolismo
Fatores de Transcrição de p300-CBP/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (BECN1 protein, human); 0 (Beclin-1); 0 (Intracellular Signaling Peptides and Proteins); 0 (Phosphatidylinositol Phosphates); 0 (Tumor Suppressor Proteins); 0 (phosphatidylinositol 3-phosphate); 4JG2LF96VF (tuberous sclerosis complex 2 protein); EC 2.3.1.48 (p300-CBP Transcription Factors); EC 2.3.1.48 (p300-CBP-associated factor); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 2.7.1.137 (Class III Phosphatidylinositol 3-Kinases); EC 2.7.1.137 (PIK3C3 protein, mouse); EC 2.7.11.1 (Autophagy-Related Protein-1 Homolog); EC 2.7.11.1 (ULK1 protein, human); EC 2.7.11.1 (Ulk1 protein, mouse); EC 2.7.11.31 (AMP-Activated Protein Kinases)
[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:170829
[St] Status:MEDLINE


  6 / 1566 MEDLINE  
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[PMID]:28756022
[Au] Autor:Bhan A; Deb P; Shihabeddin N; Ansari KI; Brotto M; Mandal SS
[Ad] Endereço:Department of Chemistry and Biochemistry, The University of Texas at Arlington, Arlington, TX 76019, United States.
[Ti] Título:Histone methylase MLL1 coordinates with HIF and regulate lncRNA HOTAIR expression under hypoxia.
[So] Source:Gene;629:16-28, 2017 Sep 20.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Hypoxia signaling plays a critical role in tumor growth, angiogenesis, metastasis cancer, and aging. Under hypoxia, hypoxia-inducible factors (HIFs) are stabilized and they coordinate the process of hypoxia-induced gene expression and cell signaling leading to increased tumor growth. Recent studies indicate that non-coding RNAs which are closely associated with cancer are abnormally expressed under hypoxia. Here, we have investigated the transcriptional regulation of a cancer associated long non-coding RNA (lncRNA), HOTAIR, under hypoxic conditions. Our studies demonstrate that HOTAIR expression is upregulated under hypoxia in colon cancer and several other types of cancer cells. HOTAIR transcription is regulated by HIF1α which binds to the hypoxia response elements (HRE) present in the HOTAIR promoter under hypoxia. HIF1α knockdown results in decreased HOTAIR expression under hypoxia. Along with HIF1α, histone methylases MLL1 and histone acetylase p300 are enriched at the HOTAIR promoter under hypoxia. The levels of H3K4-trimethylation and histone acetylation are also enriched at the HOTAIR promoter. Furthermore, knockdown of MLL1 downregulated the hypoxia-induced HOTAIR expression, indicating key roles of MLL1 in hypoxia-induced HOTAIR expression. Overall, our studies demonstrate that histone methyl-transferase MLL1 coordinates with HIF1α and histone acetyltransferase p300 and regulate hypoxia-induced HOTAIR expression. The hypoxia-induced upregulation of HOTAIR expression may contribute to its roles in tumorigenesis.
[Mh] Termos MeSH primário: Carcinogênese
Histona-Lisina N-Metiltransferase/metabolismo
Subunidade alfa do Fator 1 Induzível por Hipóxia/metabolismo
Hipóxia/metabolismo
Proteína de Leucina Linfoide-Mieloide/metabolismo
RNA Longo não Codificante/genética
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Regiões Promotoras Genéticas
Transcrição Genética
Fatores de Transcrição de p300-CBP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (HIF1A protein, human); 0 (HOTAIR long untranslated RNA, human); 0 (Hypoxia-Inducible Factor 1, alpha Subunit); 0 (MLL protein, human); 0 (RNA, Long Noncoding); 149025-06-9 (Myeloid-Lymphoid Leukemia Protein); EC 2.1.1.43 (Histone-Lysine N-Methyltransferase); EC 2.3.1.48 (p300-CBP Transcription Factors); EC 2.3.1.48 (p300-CBP-associated factor)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170828
[Lr] Data última revisão:
170828
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170731
[St] Status:MEDLINE


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[PMID]:28652407
[Au] Autor:Tikhanovich I; Zhao J; Bridges B; Kumer S; Roberts B; Weinman SA
[Ad] Endereço:From the Department of Internal Medicine.
[Ti] Título:Arginine methylation regulates c-Myc-dependent transcription by altering promoter recruitment of the acetyltransferase p300.
[So] Source:J Biol Chem;292(32):13333-13344, 2017 Aug 11.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Protein arginine methyltransferase 1 (PRMT1) is an essential enzyme controlling about 85% of the total cellular arginine methylation in proteins. We have shown previously that PRMT1 is an important regulator of innate immune responses and that it is required for M2 macrophage differentiation. c-Myc is a transcription factor that is critical in regulating cell proliferation and also regulates the M2 transcriptional program in macrophages. Here, we sought to determine whether c-Myc in myeloid cells is regulated by PRMT1-dependent arginine methylation. We found that PRMT1 activity was necessary for c-Myc binding to the acetyltransferase p300. PRMT1 inhibition decreased p300 recruitment to c-Myc target promoters and increased histone deacetylase 1 (HDAC1) recruitment, thereby decreasing transcription at these sites. Moreover, PRMT1 inhibition blocked c-Myc-mediated induction of several of its target genes, including peroxisome proliferator-activated receptor γ ( ) and mannose receptor C-type 1 ( ), suggesting that PRMT1 is necessary for c-Myc function in M2 macrophage differentiation. Of note, in primary human blood monocytes, p300-c-Myc binding was strongly correlated with PRMT1 expression, and in liver sections, PRMT1, c-Myc, and M2 macrophage levels were strongly correlated with each other. Both PRMT1 levels and M2 macrophage numbers were significantly lower in livers from individuals with a history of spontaneous bacterial peritonitis, known to have defective cellular immunity. In conclusion, our findings demonstrate that PRMT1 is an important regulator of c-Myc function in myeloid cells. PRMT1 loss in individuals with cirrhosis may contribute to their immune defects.
[Mh] Termos MeSH primário: Células Mieloides/metabolismo
Regiões Promotoras Genéticas
Processamento de Proteína Pós-Traducional
Proteína-Arginina N-Metiltransferases/metabolismo
Proteínas Proto-Oncogênicas c-myc/metabolismo
Transcrição Genética
Fatores de Transcrição de p300-CBP/metabolismo
[Mh] Termos MeSH secundário: Transporte Ativo do Núcleo Celular/efeitos dos fármacos
Animais
Arginina/metabolismo
Linhagem Celular Tumoral
Células Cultivadas
Imunoprecipitação da Cromatina
Inibidores Enzimáticos/farmacologia
Histona Desacetilase 1/metabolismo
Seres Humanos
Fígado/imunologia
Fígado/metabolismo
Fígado/patologia
Cirrose Hepática/imunologia
Cirrose Hepática/metabolismo
Cirrose Hepática/patologia
Metilação/efeitos dos fármacos
Camundongos Knockout
Células Mieloides/efeitos dos fármacos
Células Mieloides/imunologia
Células Mieloides/patologia
Regiões Promotoras Genéticas/efeitos dos fármacos
Processamento de Proteína Pós-Traducional/efeitos dos fármacos
Proteína-Arginina N-Metiltransferases/antagonistas & inibidores
Proteína-Arginina N-Metiltransferases/genética
Transcrição Genética/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Myc protein, mouse); 0 (Proto-Oncogene Proteins c-myc); 94ZLA3W45F (Arginine); EC 2.1.1.319 (Prmt1 protein, mouse); EC 2.1.1.319 (Protein-Arginine N-Methyltransferases); EC 2.3.1.48 (p300-CBP Transcription Factors); EC 2.3.1.48 (p300-CBP-associated factor); EC 3.5.1.98 (Hdac1 protein, mouse); EC 3.5.1.98 (Histone Deacetylase 1)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170628
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.797928


  8 / 1566 MEDLINE  
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[PMID]:28642327
[Au] Autor:Jing H; Liao L; Su X; Shuai Y; Zhang X; Deng Z; Jin Y
[Ad] Endereço:State Key Laboratory of Military Stomatology, Center for Tissue Engineering, School of Stomatology, Fourth Military Medical University, Xi'an, China.
[Ti] Título:Declining histone acetyltransferase GCN5 represses BMSC-mediated angiogenesis during osteoporosis.
[So] Source:FASEB J;31(10):4422-4433, 2017 Oct.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Angiogenesis is disrupted in age-related and postmenopausal osteoporosis. However, the mechanisms of the disorder remain elusive. We confirmed in this study that, in accordance with the decrease of H-type vessels, the proangiogenic potential of bone marrow-derived mesenchymal stem cells (BMSCs) declined during osteoporosis. Screening of the histone acetyltransferase family revealed that GCN5 decreased in BMSCs derived from osteoporotic femur. Further analysis identified that GCN5 plays important roles in regulating the proangiogenic potential of BMSCs. GCN5 promoted BMSC-mediated angiogenesis by enhancing H3K9ac levels on the promoter of The decrease of GCN5 in osteoporotic BMSCs led to the decline of proangiogenic capacity. Accordingly, overexpression of GCN5 enhanced the proangiogenic potency of osteoporotic BMSCs. Furthermore, recovering GCN5 expression by lentiviral expression vector significantly attenuated the loss of angiogenesis in ovariectomized mouse femurs. Our study results revealed an epigenetic mechanism controlling BMSC-mediated angiogenesis and provided a novel therapeutic target for osteoporosis treatment.-Jing, H., Liao, L., Su, X., Shuai, Y. Zhang, X., Deng, Z., Jin, Y. Declining histone acetyltransferase GCN5 represses BMSC-mediated angiogenesis during osteoporosis.
[Mh] Termos MeSH primário: Células da Medula Óssea/metabolismo
Histona Acetiltransferases/metabolismo
Células Mesenquimais Estromais/metabolismo
Osteogênese/fisiologia
Osteoporose/metabolismo
Fatores de Transcrição de p300-CBP/metabolismo
[Mh] Termos MeSH secundário: Animais
Diferenciação Celular/fisiologia
Células Cultivadas
Feminino
Transplante de Células-Tronco Mesenquimais/métodos
Camundongos Endogâmicos C57BL
Neovascularização Patológica/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.48 (p300-CBP Transcription Factors); EC 2.3.1.48 (p300-CBP-associated factor)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170624
[St] Status:MEDLINE
[do] DOI:10.1096/fj.201700118R


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[PMID]:28571745
[Au] Autor:Yu L; Li Z; Fang M; Xu Y
[Ad] Endereço:Department of Pathophysiology, Key Laboratory of Cardiovascular Disease and Molecular Intervention, Nanjing Medical University, Nanjing, China.
[Ti] Título:Acetylation of MKL1 by PCAF regulates pro-inflammatory transcription.
[So] Source:Biochim Biophys Acta;1860(8):839-847, 2017 08.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Inflammation is considered a fundamental host defense mechanism and, when aberrantly activated, contributes to a host of human diseases. Previously we have reported that the transcriptional regulator megakaryocytic leukemia 1 (MKL1) plays a role programming cellular inflammatory response by modulating NF-κB activity. Here we report that MKL1 was acetylated in vivo and pro-inflammatory stimuli (TNF-α and LPS) augmented MKL1 acetylation accompanying increased MKL1 binding to NF-κB target promoters. Further analysis revealed that the lysine acetyltransferase PCAF mediated MKL1 acetylation: TNF-α and LPS promoted the interaction between MKL1 and PCAF whereas depletion of PCAF abrogated the induction of MKL1 acetylation by TNF-α and LPS. Acetylation of MKL1 was necessary for MKL1 to activate the transcription of pro-inflammatory genes because mutation of four conserved lysine residues in MKL1 attenuated its capacity as a trans-activator of NF-κB target genes. Mechanistically, MKL1 acetylation served to promote MKL1 nuclear enrichment, to enhance the MKL1-NF-κB interaction, and to stabilize the binding of MKL1 on target promoters. In conclusion, our data unveil an important pathway that contributes to the transcriptional regulation of inflammatory response.
[Mh] Termos MeSH primário: Inflamação/genética
Transativadores/genética
Transcrição Genética/genética
Fatores de Transcrição de p300-CBP/genética
[Mh] Termos MeSH secundário: Acetilação
Linhagem Celular
Regulação da Expressão Gênica/genética
Células HEK293
Seres Humanos
Lisina/genética
NF-kappa B/genética
Regiões Promotoras Genéticas/genética
Ligação Proteica/genética
Fator de Necrose Tumoral alfa/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (MKL1 protein, human); 0 (NF-kappa B); 0 (Trans-Activators); 0 (Tumor Necrosis Factor-alpha); EC 2.3.1.48 (p300-CBP Transcription Factors); EC 2.3.1.48 (p300-CBP-associated factor); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170603
[St] Status:MEDLINE


  10 / 1566 MEDLINE  
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[PMID]:28559430
[Au] Autor:Zhou SR; Guo L; Wang X; Liu Y; Peng WQ; Liu Y; Wei XB; Dou X; Ding M; Lei QY; Qian SW; Li X; Tang QQ
[Ad] Endereço:Key Laboratory of Metabolism and Molecular Medicine, Ministry of Education, and Department of Biochemistry and Molecular Biology, Fudan University Shanghai Medical College, Shanghai, People's Republic of China.
[Ti] Título:Acetylation of Cavin-1 Promotes Lipolysis in White Adipose Tissue.
[So] Source:Mol Cell Biol;37(16), 2017 Aug 15.
[Is] ISSN:1098-5549
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:White adipose tissue (WAT) serves as a reversible energy storage depot in the form of lipids in response to nutritional status. Cavin-1, an essential component in the biogenesis of caveolae, is a positive regulator of lipolysis in adipocytes. However, molecular mechanisms of cavin-1 in the modulation of lipolysis remain poorly understood. Here, we showed that cavin-1 was acetylated at lysines 291, 293, and 298 (3K), which were under nutritional regulation in WAT. We further identified GCN5 as the acetyltransferase and Sirt1 as the deacetylase of cavin-1. Acetylation-mimetic 3Q mutants of cavin-1 augmented fat mobilization in 3T3-L1 adipocytes and zebrafish. Mechanistically, acetylated cavin-1 preferentially interacted with hormone-sensitive lipase and recruited it to the caveolae, thereby promoting lipolysis. Our findings shed light on the essential role of cavin-1 in regulating lipolysis in an acetylation-dependent manner in WAT.
[Mh] Termos MeSH primário: Tecido Adiposo Branco/metabolismo
Lipólise
Proteínas de Membrana/metabolismo
Proteínas de Ligação a RNA/metabolismo
[Mh] Termos MeSH secundário: Células 3T3-L1
Acetilação/efeitos dos fármacos
Tecido Adiposo Branco/efeitos dos fármacos
Sequência de Aminoácidos
Animais
Membrana Celular/efeitos dos fármacos
Membrana Celular/metabolismo
Células HEK293
Seres Humanos
Lipase/metabolismo
Lipólise/efeitos dos fármacos
Lisina/metabolismo
Masculino
Proteínas de Membrana/química
Camundongos
Camundongos Endogâmicos C57BL
Niacinamida/farmacologia
Ligação Proteica/efeitos dos fármacos
Proteínas de Ligação a RNA/química
Sirtuína 1/metabolismo
Peixe-Zebra
Fatores de Transcrição de p300-CBP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Membrane Proteins); 0 (Ptrf protein, mouse); 0 (RNA-Binding Proteins); 25X51I8RD4 (Niacinamide); EC 2.3.1.48 (p300-CBP Transcription Factors); EC 2.3.1.48 (p300-CBP-associated factor); EC 3.1.1.3 (Lipase); EC 3.5.1.- (Sirtuin 1); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170828
[Lr] Data última revisão:
170828
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170601
[St] Status:MEDLINE



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