Base de dados : MEDLINE
Pesquisa : G03.143.850 [Categoria DeCS]
Referências encontradas : 972 [refinar]
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[PMID]:29180807
[Au] Autor:Chiang JJ; Sparrer KMJ; van Gent M; Lässig C; Huang T; Osterrieder N; Hopfner KP; Gack MU
[Ad] Endereço:Department of Microbiology and Immunobiology, Harvard Medical School, Boston, MA, USA.
[Ti] Título:Viral unmasking of cellular 5S rRNA pseudogene transcripts induces RIG-I-mediated immunity.
[So] Source:Nat Immunol;19(1):53-62, 2018 Jan.
[Is] ISSN:1529-2916
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The sensor RIG-I detects double-stranded RNA derived from RNA viruses. Although RIG-I is also known to have a role in the antiviral response to DNA viruses, physiological RNA species recognized by RIG-I during infection with a DNA virus are largely unknown. Using next-generation RNA sequencing (RNAseq), we found that host-derived RNAs, most prominently 5S ribosomal RNA pseudogene 141 (RNA5SP141), bound to RIG-I during infection with herpes simplex virus 1 (HSV-1). Infection with HSV-1 induced relocalization of RNA5SP141 from the nucleus to the cytoplasm, and virus-induced shutoff of host protein synthesis downregulated the abundance of RNA5SP141-interacting proteins, which allowed RNA5SP141 to bind RIG-I and induce the expression of type I interferons. Silencing of RNA5SP141 strongly dampened the antiviral response to HSV-1 and the related virus Epstein-Barr virus (EBV), as well as influenza A virus (IAV). Our findings reveal that antiviral immunity can be triggered by host RNAs that are unshielded following depletion of their respective binding proteins by the virus.
[Mh] Termos MeSH primário: Proteína DEAD-box 58/imunologia
Herpesvirus Humano 1/imunologia
Imunidade/imunologia
RNA Ribossômico 5S/imunologia
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Cercopithecus aethiops
Proteína DEAD-box 58/metabolismo
Expressão Gênica/imunologia
Células HEK293
Herpesvirus Humano 1/fisiologia
Interações Hospedeiro-Patógeno/imunologia
Seres Humanos
Interferon Tipo I/genética
Interferon Tipo I/imunologia
Interferon Tipo I/metabolismo
Camundongos Knockout
Pseudogenes/genética
Transporte de RNA/imunologia
RNA Ribossômico 5S/genética
RNA Ribossômico 5S/metabolismo
Células Vero
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Interferon Type I); 0 (RNA, Ribosomal, 5S); EC 3.6.1.- (DDX58 protein, human); EC 3.6.4.13 (DEAD Box Protein 58)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171129
[St] Status:MEDLINE
[do] DOI:10.1038/s41590-017-0005-y


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[PMID]:28934468
[Au] Autor:Shi M; Zhang H; Wu X; He Z; Wang L; Yin S; Tian B; Li G; Cheng H
[Ad] Endereço:State Key Laboratory of Molecular Biology, Shanghai Key Laboratory of Molecular Andrology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China.
[Ti] Título:ALYREF mainly binds to the 5' and the 3' regions of the mRNA in vivo.
[So] Source:Nucleic Acids Res;45(16):9640-9653, 2017 Sep 19.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The TREX complex (TREX) plays key roles in nuclear export of mRNAs. However, little is known about its transcriptome-wide binding targets. We used individual cross-linking and immunoprecipitation (iCLIP) to identify the binding sites of ALYREF, an mRNA export adaptor in TREX, in human cells. Consistent with previous in vitro studies, ALYREF binds to a region near the 5' end of the mRNA in a CBP80-dependent manner. Unexpectedly, we identified PABPN1-dependent ALYREF binding near the 3' end of the mRNA. Furthermore, the 3' processing factor CstF64 directly interacts with ALYREF and is required for the overall binding of ALYREF on the mRNA. In addition, we found that numerous middle exons harbor ALYREF binding sites and identified ALYREF-binding motifs that promote nuclear export of intronless mRNAs. Together, our study defines enrichment of ALYREF binding sites at the 5' and the 3' regions of the mRNA in vivo, identifies export-promoting ALYREF-binding motifs, and reveals CstF64- and PABPN1-mediated coupling of mRNA nuclear export to 3' processing.
[Mh] Termos MeSH primário: Proteínas Nucleares/metabolismo
RNA Mensageiro/metabolismo
Proteínas de Ligação a RNA/metabolismo
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
Fator Estimulador de Clivagem/genética
Fator Estimulador de Clivagem/metabolismo
Células HeLa
Seres Humanos
Complexo Proteico Nuclear de Ligação ao Cap/metabolismo
Proteínas Nucleares/genética
Proteína I de Ligação a Poli(A)/metabolismo
Transporte de RNA
RNA Mensageiro/química
Proteínas de Ligação a RNA/genética
Fatores de Transcrição/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ALYREF protein, human); 0 (Cleavage Stimulation Factor); 0 (Nuclear Cap-Binding Protein Complex); 0 (Nuclear Proteins); 0 (PABPN1 protein, human); 0 (Poly(A)-Binding Protein I); 0 (RNA, Messenger); 0 (RNA-Binding Proteins); 0 (Transcription Factors)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170922
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx597


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[PMID]:28916264
[Au] Autor:Nguyen TA; Smith BRC; Tate MD; Belz GT; Barrios MH; Elgass KD; Weisman AS; Baker PJ; Preston SP; Whitehead L; Garnham A; Lundie RJ; Smyth GK; Pellegrini M; O'Keeffe M; Wicks IP; Masters SL; Hunter CP; Pang KC
[Ad] Endereço:The Walter and Eliza Hall Institute of Medical Research, Parkville, VIC, Australia; Department of Medical Biology, University of Melbourne, Parkville, VIC, Australia.
[Ti] Título:SIDT2 Transports Extracellular dsRNA into the Cytoplasm for Innate Immune Recognition.
[So] Source:Immunity;47(3):498-509.e6, 2017 Sep 19.
[Is] ISSN:1097-4180
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Double-stranded RNA (dsRNA) is a common by-product of viral infections and acts as a potent trigger of antiviral immunity. In the nematode C. elegans, sid-1 encodes a dsRNA transporter that is highly conserved throughout animal evolution, but the physiological role of SID-1 and its orthologs remains unclear. Here, we show that the mammalian SID-1 ortholog, SIDT2, is required to transport internalized extracellular dsRNA from endocytic compartments into the cytoplasm for immune activation. Sidt2-deficient mice exposed to extracellular dsRNA, encephalomyocarditis virus (EMCV), and herpes simplex virus 1 (HSV-1) show impaired production of antiviral cytokines and-in the case of EMCV and HSV-1-reduced survival. Thus, SIDT2 has retained the dsRNA transport activity of its C. elegans ortholog, and this transport is important for antiviral immunity.
[Mh] Termos MeSH primário: Imunidade Inata
Proteínas de Membrana/metabolismo
Transporte de RNA
RNA de Cadeia Dupla/imunologia
RNA de Cadeia Dupla/metabolismo
[Mh] Termos MeSH secundário: Animais
Infecções por Cardiovirus/genética
Infecções por Cardiovirus/imunologia
Linhagem Celular
Citoplasma
Proteína DEAD-box 58/metabolismo
Modelos Animais de Doenças
Vírus da Encefalomiocardite/genética
Vírus da Encefalomiocardite/imunologia
Endossomos/metabolismo
Feminino
Expressão Gênica
Técnicas de Inativação de Genes
Herpes Simples/genética
Herpes Simples/imunologia
Herpesvirus Humano 1/genética
Herpesvirus Humano 1/imunologia
Interações Hospedeiro-Patógeno/genética
Interações Hospedeiro-Patógeno/imunologia
Lisossomos/metabolismo
Proteínas de Membrana/genética
Camundongos
Camundongos Knockout
Ligação Proteica
Transporte Proteico
RNA Viral/genética
RNA Viral/metabolismo
Transdução de Sinais
Receptor 3 Toll-Like/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Membrane Proteins); 0 (RNA, Double-Stranded); 0 (RNA, Viral); 0 (Sidt2 protein, mouse); 0 (Toll-Like Receptor 3); EC 3.6.4.13 (DEAD Box Protein 58)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171110
[Lr] Data última revisão:
171110
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170917
[St] Status:MEDLINE


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[PMID]:28846086
[Au] Autor:Zheng Q; Hou J; Zhou Y; Li Z; Cao X
[Ad] Endereço:Department of Immunology &Center for Immunotherapy, CAMS-Oxford University International Center for Translational Immunology, Institute of Basic Medical Sciences, Peking Union Medical College, Chinese Academy of Medical Sciences, Beijing, China.
[Ti] Título:The RNA helicase DDX46 inhibits innate immunity by entrapping m A-demethylated antiviral transcripts in the nucleus.
[So] Source:Nat Immunol;18(10):1094-1103, 2017 Oct.
[Is] ISSN:1529-2916
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:DEAD-box (DDX) helicases are vital for the recognition of RNA and metabolism and are critical for the initiation of antiviral innate immunity. Modification of RNA is involved in many biological processes; however, its role in antiviral innate immunity has remained unclear. Here we found that nuclear DDX member DDX46 inhibited the production of type I interferons after viral infection. DDX46 bound Mavs, Traf3 and Traf6 transcripts (which encode signaling molecules involved in antiviral responses) via their conserved CCGGUU element. After viral infection, DDX46 recruited ALKBH5, an 'eraser' of the RNA modification N -methyladenosine (m A), via DDX46's DEAD helicase domain to demethylate those m A-modified antiviral transcripts. It consequently enforced their retention in the nucleus and therefore prevented their translation and inhibited interferon production. DDX46 also suppressed antiviral innate immunity in vivo. Thus, DDX46 inhibits antiviral innate responses by entrapping selected antiviral transcripts in the nucleus by erasing their m A modification, a modification normally required for export from the nucleus and translation.
[Mh] Termos MeSH primário: Adenina/análogos & derivados
RNA Helicases DEAD-box/genética
RNA Helicases DEAD-box/metabolismo
Imunidade Inata/genética
Transcrição Genética
[Mh] Termos MeSH secundário: Adenina/metabolismo
Homólogo AlkB 5 da RNA Desmetilase/genética
Homólogo AlkB 5 da RNA Desmetilase/metabolismo
Animais
Sítios de Ligação
Linhagem Celular
Núcleo Celular/metabolismo
Expressão Gênica
Técnicas de Silenciamento de Genes
Seres Humanos
Interferon Tipo I/biossíntese
Macrófagos/imunologia
Macrófagos/metabolismo
Camundongos
Camundongos Knockout
Motivos de Nucleotídeos
Ligação Proteica
Transporte de RNA
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Estomatite Vesicular/genética
Estomatite Vesicular/imunologia
Estomatite Vesicular/metabolismo
Vesiculovirus/fisiologia
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Interferon Type I); 0 (RNA, Messenger); EC 1.14.11.- (AlkB Homolog 5, RNA Demethylase); EC 3.6.4.13 (DEAD-box RNA Helicases); JAC85A2161 (Adenine); W7IBY2BGAX (6-methyladenine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171120
[Lr] Data última revisão:
171120
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170829
[St] Status:MEDLINE
[do] DOI:10.1038/ni.3830


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[PMID]:28801509
[Au] Autor:Fan J; Kuai B; Wu G; Wu X; Chi B; Wang L; Wang K; Shi Z; Zhang H; Chen S; He Z; Wang S; Zhou Z; Li G; Cheng H
[Ad] Endereço:State Key Laboratory of Molecular Biology, Shanghai Key Laboratory of Molecular Andrology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, University of Chinese Academy of Sciences, Chinese Academy of Sciences, Shanghai, China.
[Ti] Título:Exosome cofactor hMTR4 competes with export adaptor ALYREF to ensure balanced nuclear RNA pools for degradation and export.
[So] Source:EMBO J;36(19):2870-2886, 2017 Oct 02.
[Is] ISSN:1460-2075
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The exosome is a key RNA machine that functions in the degradation of unwanted RNAs. Here, we found that significant fractions of precursors and mature forms of mRNAs and long noncoding RNAs are degraded by the nuclear exosome in normal human cells. Exosome-mediated degradation of these RNAs requires its cofactor hMTR4. Significantly, hMTR4 plays a key role in specifically recruiting the exosome to its targets. Furthermore, we provide several lines of evidence indicating that hMTR4 executes this role by directly competing with the mRNA export adaptor ALYREF for associating with ARS2, a component of the cap-binding complex (CBC), and this competition is critical for determining whether an RNA is degraded or exported to the cytoplasm. Together, our results indicate that the competition between hMTR4 and ALYREF determines exosome recruitment and functions in creating balanced nuclear RNA pools for degradation and export.
[Mh] Termos MeSH primário: Proteínas Nucleares/metabolismo
RNA Helicases/metabolismo
Estabilidade de RNA
Transporte de RNA/genética
RNA Nuclear/metabolismo
Proteínas de Ligação a RNA/metabolismo
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Transporte Ativo do Núcleo Celular/genética
Complexo Multienzimático de Ribonucleases do Exossomo/genética
Complexo Multienzimático de Ribonucleases do Exossomo/metabolismo
Exossomos/genética
Exossomos/metabolismo
Técnicas de Silenciamento de Genes
Células HEK293
Células HeLa
Seres Humanos
Proteínas Nucleares/genética
Ligação Proteica
RNA Helicases/genética
Estabilidade de RNA/genética
RNA Longo não Codificante/metabolismo
RNA Mensageiro/metabolismo
Proteínas de Ligação a RNA/genética
Fatores de Transcrição/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ALYREF protein, human); 0 (Nuclear Proteins); 0 (RNA, Long Noncoding); 0 (RNA, Messenger); 0 (RNA, Nuclear); 0 (RNA-Binding Proteins); 0 (Transcription Factors); EC 3.1.- (Exosome Multienzyme Ribonuclease Complex); EC 3.6.1.- (SKIV2L2 protein, human); EC 3.6.4.13 (RNA Helicases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170813
[St] Status:MEDLINE
[do] DOI:10.15252/embj.201696139


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[PMID]:28423324
[Au] Autor:Pitchiaya S; Heinicke LA; Park JI; Cameron EL; Walter NG
[Ad] Endereço:Single Molecule Analysis Group, Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USA.
[Ti] Título:Resolving Subcellular miRNA Trafficking and Turnover at Single-Molecule Resolution.
[So] Source:Cell Rep;19(3):630-642, 2017 Apr 18.
[Is] ISSN:2211-1247
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Regulation of microRNA (miRNA) localization and stability is critical for their extensive cytoplasmic RNA silencing activity and emerging nuclear functions. Here, we have developed single-molecule fluorescence-based tools to assess the subcellular trafficking, integrity, and activity of miRNAs. We find that seed-matched RNA targets protect miRNAs against degradation and enhance their nuclear retention. While target-stabilized, functional, cytoplasmic miRNAs reside in high-molecular-weight complexes, nuclear miRNAs, as well as cytoplasmic miRNAs targeted by complementary anti-miRNAs, are sequestered stably within significantly lower-molecular-weight complexes and rendered repression incompetent. miRNA stability and activity depend on Argonaute protein abundance, whereas miRNA strand selection, unwinding, and nuclear retention depend on Argonaute identity. Taken together, our results show that miRNA degradation competes with Argonaute loading and target binding to control subcellular miRNA abundance for gene silencing surveillance. Probing single cells for miRNA activity, trafficking, and metabolism promises to facilitate screening for effective miRNA mimics and anti-miRNA drugs.
[Mh] Termos MeSH primário: MicroRNAs/metabolismo
Imagem Individual de Molécula/métodos
[Mh] Termos MeSH secundário: Animais
Proteínas Argonauta/metabolismo
Contagem de Células
Linhagem Celular Tumoral
Núcleo Celular/metabolismo
Seres Humanos
Espaço Intracelular/metabolismo
Camundongos
MicroRNAs/genética
Modelos Biológicos
Sondas Moleculares/metabolismo
Estabilidade de RNA
Transporte de RNA
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Reprodutibilidade dos Testes
Frações Subcelulares/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Argonaute Proteins); 0 (MicroRNAs); 0 (Molecular Probes); 0 (RNA, Messenger)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170714
[Lr] Data última revisão:
170714
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170420
[St] Status:MEDLINE


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[PMID]:28422978
[Au] Autor:Haag C; Pohlmann T; Feldbrügge M
[Ad] Endereço:Heinrich Heine University Düsseldorf, Institute for Microbiology, Cluster of Excellence on Plant Sciences, Düsseldorf, Germany.
[Ti] Título:The ESCRT regulator Did2 maintains the balance between long-distance endosomal transport and endocytic trafficking.
[So] Source:PLoS Genet;13(4):e1006734, 2017 Apr.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In highly polarised cells, like fungal hyphae, early endosomes function in both endocytosis as well as long-distance transport of various cargo including mRNA and protein complexes. However, knowledge on the crosstalk between these seemingly different trafficking processes is scarce. Here, we demonstrate that the ESCRT regulator Did2 coordinates endosomal transport in fungal hyphae of Ustilago maydis. Loss of Did2 results in defective vacuolar targeting, less processive long-distance transport and abnormal shuttling of early endosomes. Importantly, the late endosomal protein Rab7 and vacuolar protease Prc1 exhibit increased shuttling on these aberrant endosomes suggesting defects in endosomal maturation and identity. Consistently, molecular motors fail to attach efficiently explaining the disturbed processive movement. Furthermore, the endosomal mRNP linker protein Upa1 is hardly present on endosomes resulting in defects in long-distance mRNA transport. In conclusion, the ESCRT regulator Did2 coordinates precise maturation of endosomes and thus provides the correct membrane identity for efficient endosomal long-distance transport.
[Mh] Termos MeSH primário: Complexos Endossomais de Distribuição Requeridos para Transporte/genética
Endossomos/genética
Transporte Proteico/genética
Transporte de RNA/genética
Proteínas de Saccharomyces cerevisiae/genética
Ustilago/genética
[Mh] Termos MeSH secundário: Catepsina A/genética
Polaridade Celular/genética
Endocitose/genética
Complexos Endossomais de Distribuição Requeridos para Transporte/metabolismo
Endossomos/metabolismo
Hifas/genética
Hifas/crescimento & desenvolvimento
Hifas/metabolismo
RNA Mensageiro/metabolismo
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/crescimento & desenvolvimento
Proteínas de Saccharomyces cerevisiae/metabolismo
Vesículas Transportadoras/genética
Vesículas Transportadoras/metabolismo
Ustilago/crescimento & desenvolvimento
Proteínas rab de Ligação ao GTP/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DID2 protein, S cerevisiae); 0 (Endosomal Sorting Complexes Required for Transport); 0 (RNA, Messenger); 0 (Saccharomyces cerevisiae Proteins); 152989-05-4 (rab7 protein); EC 3.4.16.5 (Cathepsin A); EC 3.4.16.5 (PRC1 protein, S cerevisiae); EC 3.6.5.2 (rab GTP-Binding Proteins)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170601
[Lr] Data última revisão:
170601
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170420
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006734


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[PMID]:28404748
[Au] Autor:Mitsumori K; Takei Y; Hirokawa N
[Ad] Endereço:Department of Cell Biology and Anatomy, Graduate School of Medicine, University of Tokyo, Hongo 7-3-1, Bunkyo-ku, Tokyo 113-0033, Japan.
[Ti] Título:Components of RNA granules affect their localization and dynamics in neuronal dendrites.
[So] Source:Mol Biol Cell;28(11):1412-1417, 2017 Jun 01.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In neurons, RNA transport is important for local protein synthesis. mRNAs are transported along dendrites as large RNA granules. The localization and dynamics of Puralpha and Staufen1 (Stau1), major components of RNA transport granules, were investigated in cultured hippocampal neurons. Puralpha-positive granules were localized in both the shafts and spines of dendrites. In contrast, Stau1-positive granules tended to be localized mainly in dendritic shafts. More than 90% of Puralpha-positive granules were positive for Stau1 in immature dendrites, while only half were positive in mature dendrites. Stau1-negative Puralpha granules tended to be stationary with fewer anterograde and retrograde movements than Stau1-positive Puralpha granules. After metabotropic glutamate receptor 5 activation, Stau1-positive granules remained in the dendritic shafts, while Puralpha granules translocated from the shaft to the spine. The translocation of Puralpha granules was dependent on myosin Va, an actin-based molecular motor protein. Collectively our findings suggest the possibility that the loss of Stau1 in Puralpha-positive RNA granules might promote their activity-dependent translocation into dendritic spines, which could underlie the regulation of protein synthesis in synapses.
[Mh] Termos MeSH primário: Proteínas de Ligação a DNA/metabolismo
Proteínas do Tecido Nervoso/metabolismo
RNA Mensageiro/metabolismo
Proteínas de Ligação a RNA/metabolismo
[Mh] Termos MeSH secundário: Animais
Transporte Biológico
Células Cultivadas
Dendritos/metabolismo
Espinhas Dendríticas/metabolismo
Hipocampo/metabolismo
Camundongos
Camundongos Endogâmicos ICR/embriologia
Neurônios/metabolismo
Transporte de RNA/fisiologia
RNA Interferente Pequeno/metabolismo
Sinapses/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (Nerve Tissue Proteins); 0 (Pura protein, mouse); 0 (RNA, Messenger); 0 (RNA, Small Interfering); 0 (RNA-Binding Proteins); 0 (Stau1 protein, mouse)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170414
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E16-07-0497


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[PMID]:28335522
[Au] Autor:Kouwaki T; Okamoto M; Tsukamoto H; Fukushima Y; Oshiumi H
[Ad] Endereço:Department of Immunology, Graduate School of Medical Sciences, Faculty of Life Sciences, Kumamoto University, 1-1-1 Honjo, Chuo-ku, Kumamoto 860-8556, Japan. kouwaki@kumamoto-u.ac.jp.
[Ti] Título:Extracellular Vesicles Deliver Host and Virus RNA and Regulate Innate Immune Response.
[So] Source:Int J Mol Sci;18(3), 2017 Mar 20.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The innate immune system plays a crucial role in controlling viral infection. Pattern recognition receptors (PRRs), such as Toll-like receptors and RIG-I-like receptors, sense viral components called pathogen-associated molecular patterns (PAMPs) and trigger signals to induce innate immune responses. Extracellular vesicles (EVs), including exosomes and microvesicles, deliver functional RNA and mediate intercellular communications. Recent studies have revealed that EVs released from virus-infected cells deliver viral RNA to dendritic cells and macrophages, thereby activating PRRs in recipient cells, which results in the expression of type I interferon and pro-inflammatory cytokines. On the other hand, EVs transfer not only viral RNA but also host microRNAs to recipient cells. Recently, infection of hepatocytes with hepatitis B virus (HBV) was shown to affect microRNA levels in EVs released from virus-infected cells, leading to attenuation of host innate immune response. This suggests that the virus utilizes the EVs and host microRNAs to counteract the antiviral innate immune responses. In this review, we summarize recent findings related to the role of EVs in antiviral innate immune responses.
[Mh] Termos MeSH primário: Vesículas Extracelulares/metabolismo
Interações Hospedeiro-Patógeno
Imunidade Inata
Imunomodulação
Transporte de RNA
RNA/metabolismo
Viroses/imunologia
Viroses/metabolismo
[Mh] Termos MeSH secundário: Animais
Transporte Biológico
Micropartículas Derivadas de Células/metabolismo
Células Dendríticas/imunologia
Células Dendríticas/metabolismo
Exossomos/metabolismo
Interações Hospedeiro-Patógeno/genética
Interações Hospedeiro-Patógeno/imunologia
Seres Humanos
Macrófagos/imunologia
Macrófagos/metabolismo
MicroRNAs/genética
MicroRNAs/metabolismo
Ligação Proteica
RNA/genética
RNA Viral/genética
RNA Viral/metabolismo
Receptores de Reconhecimento de Padrão/metabolismo
Viroses/genética
Viroses/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (MicroRNAs); 0 (RNA, Viral); 0 (Receptors, Pattern Recognition); 63231-63-0 (RNA)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170420
[Lr] Data última revisão:
170420
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170325
[St] Status:MEDLINE


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[PMID]:28325845
[Au] Autor:Li R; Harvey AR; Hodgetts SI; Fox AH
[Ad] Endereço:Harry Perkins Institute of Medical Research, QEII Medical Centre and Centre for Medical Research, The University of Western Australia, Nedlands, Western Australia 6009, Australia.
[Ti] Título:Functional dissection of NEAT1 using genome editing reveals substantial localization of the NEAT1_1 isoform outside paraspeckles.
[So] Source:RNA;23(6):872-881, 2017 Jun.
[Is] ISSN:1469-9001
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Large numbers of long noncoding RNAs have been discovered in recent years, but only a few have been characterized. NEAT1 (nuclear paraspeckle assembly transcript 1) is a mammalian long noncoding RNA that is important for the reproductive physiology of mice, cancer development, and the formation of subnuclear bodies termed paraspeckles. The two major isoforms of NEAT1 (3.7 kb NEAT1_1 and 23 kb NEAT1_2 in human) are generated from a common promoter and are produced through the use of alternative transcription termination sites. This gene structure has made the functional relationship between the two isoforms difficult to dissect. Here we used CRISPR-Cas9 genome editing to create several different cell lines: total NEAT1 knockout cells, cells that only express the short form NEAT1_1, and cells with twofold more NEAT1_2. Using these reagents, we obtained evidence that NEAT1_1 is not a major component of paraspeckles. In addition, our data suggest NEAT1_1 localizes in numerous nonparaspeckle foci we termed "microspeckles," which may carry paraspeckle-independent functions. This study highlights the complexity of lncRNA and showcases how genome editing tools are useful in dissecting the structural and functional roles of overlapping transcripts.
[Mh] Termos MeSH primário: Edição de Genes
RNA Longo não Codificante/genética
[Mh] Termos MeSH secundário: Sistemas CRISPR-Cas
Linhagem Celular
Núcleo Celular/metabolismo
Repetições Palindrômicas Curtas Agrupadas e Regularmente Espaçadas
Técnicas de Inativação de Genes
Seres Humanos
Isoformas de RNA
Fatores de Processamento de RNA/metabolismo
Transporte de RNA
RNA Guia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (NEAT1 long non-coding RNA, human); 0 (RNA Isoforms); 0 (RNA Splicing Factors); 0 (RNA, Guide); 0 (RNA, Long Noncoding)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170911
[Lr] Data última revisão:
170911
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170323
[St] Status:MEDLINE
[do] DOI:10.1261/rna.059477.116



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