Base de dados : MEDLINE
Pesquisa : A11.284.430.214.190.875.811.740 [Categoria DeCS]
Referências encontradas : 5934 [refinar]
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[PMID]:27773672
[Au] Autor:Dankert JF; Rona G; Clijsters L; Geter P; Skaar JR; Bermudez-Hernandez K; Sassani E; Fenyö D; Ueberheide B; Schneider R; Pagano M
[Ad] Endereço:Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, 522 First Avenue, SRB 1107, New York, NY 10016, USA; Perlmutter NYU Cancer Center, New York University School of Medicine, 522 First Avenue, SRB 1107, New York, NY 10016, USA.
[Ti] Título:Cyclin F-Mediated Degradation of SLBP Limits H2A.X Accumulation and Apoptosis upon Genotoxic Stress in G2.
[So] Source:Mol Cell;64(3):507-519, 2016 Nov 03.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:SLBP (stem-loop binding protein) is a highly conserved factor necessary for the processing, translation, and degradation of H2AFX and canonical histone mRNAs. We identified the F-box protein cyclin F, a substrate recognition subunit of an SCF (Skp1-Cul1-F-box protein) complex, as the G2 ubiquitin ligase for SLBP. SLBP interacts with cyclin F via an atypical CY motif, and mutation of this motif prevents SLBP degradation in G2. Expression of an SLBP stable mutant results in increased loading of H2AFX mRNA onto polyribosomes, resulting in increased expression of H2A.X (encoded by H2AFX). Upon genotoxic stress in G2, high levels of H2A.X lead to persistent γH2A.X signaling, high levels of H2A.X phosphorylated on Tyr142, high levels of p53, and induction of apoptosis. We propose that cyclin F co-evolved with the appearance of stem-loops in vertebrate H2AFX mRNA to mediate SLBP degradation, thereby limiting H2A.X synthesis and cell death upon genotoxic stress.
[Mh] Termos MeSH primário: Ciclinas/genética
Dano ao DNA
Pontos de Checagem da Fase G2 do Ciclo Celular/genética
Histonas/genética
Proteínas Nucleares/genética
RNA Mensageiro/genética
Fatores de Poliadenilação e Clivagem de mRNA/genética
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Animais
Apoptose
Sítios de Ligação
Linhagem Celular Tumoral
Ciclinas/metabolismo
Regulação da Expressão Gênica
Células HEK293
Células HeLa
Histonas/metabolismo
Seres Humanos
Camundongos
Proteínas Nucleares/metabolismo
Fosforilação
Polirribossomos/genética
Polirribossomos/metabolismo
Ligação Proteica
Proteólise
RNA Mensageiro/metabolismo
Ratos
Transdução de Sinais
Xenopus laevis
Peixe-Zebra
Fatores de Poliadenilação e Clivagem de mRNA/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CCNF protein, human); 0 (Cyclins); 0 (H2AFX protein, human); 0 (Histones); 0 (Nuclear Proteins); 0 (RNA, Messenger); 0 (SLBP protein, human); 0 (mRNA Cleavage and Polyadenylation Factors)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:180119
[Lr] Data última revisão:
180119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161105
[St] Status:MEDLINE


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[PMID]:28977579
[Au] Autor:Belhabich-Baumas K; Joret C; Jády BE; Plisson-Chastang C; Shayan R; Klopp C; Henras AK; Henry Y; Mougin A
[Ad] Endereço:Laboratoire de Biologie Moléculaire Eucaryote, Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, UPS, 31000 Toulouse, France.
[Ti] Título:The Rio1p ATPase hinders premature entry into translation of late pre-40S pre-ribosomal particles.
[So] Source:Nucleic Acids Res;45(18):10824-10836, 2017 Oct 13.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cytoplasmic maturation of precursors to the small ribosomal subunit in yeast requires the intervention of a dozen assembly factors (AFs), the precise roles of which remain elusive. One of these is Rio1p that seems to intervene at a late step of pre-40S particle maturation. We have investigated the role played by Rio1p in the dynamic association and dissociation of AFs with and from pre-40S particles. Our results indicate that Rio1p depletion leads to the stalling of at least 4 AFs (Nob1p, Tsr1p, Pno1p/Dim2p and Fap7p) in 80S-like particles. We conclude that Rio1p is important for the timely release of these factors from 80S-like particles. In addition, we present immunoprecipitation and electron microscopy evidence suggesting that when Rio1p is depleted, a subset of Nob1p-containing pre-40S particles associate with translating polysomes. Using Nob1p as bait, we purified pre-40S particles from cells lacking Rio1p and performed ribosome profiling experiments which suggest that immature 40S subunits can carry out translation elongation. We conclude that lack of Rio1p allows premature entry of pre-40S particles in the translation process and that the presence of Nob1p and of the 18S rRNA 3' extension in the 20S pre-rRNA is not incompatible with translation elongation.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/fisiologia
Biossíntese de Proteínas
Proteínas Serina-Treonina Quinases/fisiologia
Subunidades Ribossômicas Menores de Eucariotos/metabolismo
Proteínas de Saccharomyces cerevisiae/fisiologia
[Mh] Termos MeSH secundário: Proteínas Nucleares/metabolismo
Elongação Traducional da Cadeia Peptídica
Polirribossomos/metabolismo
Proteínas Ribossômicas/metabolismo
Ribossomos/metabolismo
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (LTV1 protein, S cerevisiae); 0 (NOB1 protein, S cerevisiae); 0 (Nuclear Proteins); 0 (Ribosomal Proteins); 0 (Saccharomyces cerevisiae Proteins); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.1 (Rio1 protein, S cerevisiae); EC 3.6.1.- (Adenosine Triphosphatases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171005
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx734


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[PMID]:28934492
[Au] Autor:Du Z; Alekhina OM; Vassilenko KS; Simon AE
[Ad] Endereço:Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, MD 20742, USA.
[Ti] Título:Concerted action of two 3' cap-independent translation enhancers increases the competitive strength of translated viral genomes.
[So] Source:Nucleic Acids Res;45(16):9558-9572, 2017 Sep 19.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Several families of plant viruses evolved cap-independent translation enhancers (3'CITE) in the 3' untranslated regions of their genomic (g)RNAs to compete with ongoing cap-dependent translation of cellular mRNAs. Umbravirus Pea enation mosaic virus (PEMV)2 is the only example where three 3'CITEs enhance translation: the eIF4E-binding Panicum mosaic virus-like translational enhancer (PTE) and ribosome-binding 3' T-shaped structure (TSS) have been found in viruses of different genera, while the ribosome-binding kl-TSS that provides a long-distance interaction with the 5' end is unique. We report that the PTE is the key translation promoting element, but inhibits translation in cis and in trans in the absence of the kl-TSS by sequestering initiation factor eIF4G. PEMV2 strongly outcompeted a cellular mRNA mimic for translation, indicating that the combination of kl-TSS and PTE is highly efficient. Transferring the 3'-5' interaction from the kl-TSS to the PTE (to fulfill its functionality as found in other viruses) supported translationin vitro, but gRNA did not accumulate to detectable levels in protoplasts in the absence of the kl-TSS. It was shown that the PTE in conjunction with the kl-TSS did not markedly affect the translation initiation rate but rather increased the number of gRNAs available for translation. A model is proposed to explain how 3'CITE-based regulation of ribosome recruitment enhances virus fitness.
[Mh] Termos MeSH primário: Elementos Facilitadores Genéticos
Genoma Viral
Luteoviridae/genética
Capuzes de RNA/genética
[Mh] Termos MeSH secundário: Arabidopsis/virologia
Códon de Iniciação
Fator de Iniciação 4G em Eucariotos/genética
Fator de Iniciação 4G em Eucariotos/metabolismo
Luteoviridae/metabolismo
Polirribossomos/metabolismo
Biossíntese de Proteínas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Codon, Initiator); 0 (Eukaryotic Initiation Factor-4G); 0 (RNA Caps)
[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/gkx643


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[PMID]:28842509
[Au] Autor:Sbarrato T; Spriggs RV; Wilson L; Jones C; Dudek K; Bastide A; Pichon X; Pöyry T; Willis AE
[Ad] Endereço:Medical Research Council Toxicology Unit, Leicester LE1 9HN, United Kingdom thomas.sbarrato@inserm.fr rvs3@leicester.ac.uk.
[Ti] Título:An improved analysis methodology for translational profiling by microarray.
[So] Source:RNA;23(11):1601-1613, 2017 Nov.
[Is] ISSN:1469-9001
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Translational regulation plays a central role in the global gene expression of a cell, and detection of such regulation has allowed deciphering of critical biological mechanisms. Genome-wide studies of the regulation of translation (translatome) performed on microarrays represent a substantial proportion of studies, alongside with recent advances in deep-sequencing methods. However, there has been a lack of development in specific processing methodologies that deal with the distinct nature of translatome array data. In this study, we confirm that polysome profiling yields skewed data and thus violates the conventional transcriptome analysis assumptions. Using a comprehensive simulation of translatome array data varying the percentage and symmetry of deregulation, we show that conventional analysis methods (Quantile and LOESS normalizations) and statistical tests failed, respectively, to correctly normalize the data and to identify correctly deregulated genes (DEGs). We thus propose a novel analysis methodology available as a CRAN package; Internal Control Analysis of Translatome (INCATome) based on a normalization tied to a group of invariant controls. We confirm that INCATome outperforms the other normalization methods and allows a stringent identification of DEGs. More importantly, INCATome implementation on a biological translatome data set (cells silenced for splicing factor PSF) resulted in the best normalization performance and an improved validation concordance for identification of true positive DEGs. Finally, we provide evidence that INCATome is able to infer novel biological pathways with superior discovery potential, thus confirming the benefits for researchers of implementing INCATome for future translatome studies as well as for existing data sets to generate novel avenues for research.
[Mh] Termos MeSH primário: Perfilação da Expressão Gênica/métodos
Análise de Sequência com Séries de Oligonucleotídeos/métodos
Biossíntese de Proteínas
[Mh] Termos MeSH secundário: Biologia Computacional/métodos
Simulação por Computador
Perfilação da Expressão Gênica/estatística & dados numéricos
Regulação da Expressão Gênica
Células HeLa
Sequenciamento de Nucleotídeos em Larga Escala
Seres Humanos
Análise de Sequência com Séries de Oligonucleotídeos/estatística & dados numéricos
Polirribossomos/metabolismo
Análise de Sequência de RNA
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170827
[St] Status:MEDLINE
[do] DOI:10.1261/rna.060525.116


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[PMID]:28821679
[Au] Autor:Graber TE; Freemantle E; Anadolu MN; Hébert-Seropian S; MacAdam RL; Shin U; Hoang HD; Alain T; Lacaille JC; Sossin WS
[Ad] Endereço:Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada.
[Ti] Título:UPF1 Governs Synaptic Plasticity through Association with a STAU2 RNA Granule.
[So] Source:J Neurosci;37(38):9116-9131, 2017 Sep 20.
[Is] ISSN:1529-2401
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Neuronal mRNAs can be packaged in reversibly stalled polysome granules before their transport to distant synaptic locales. Stimulation of synaptic metabotropic glutamate receptors (mGluRs) reactivates translation of these particular mRNAs to produce plasticity-related protein; a phenomenon exhibited during mGluR-mediated LTD. This form of plasticity is deregulated in Fragile X Syndrome, a monogenic form of autism in humans, and understanding the stalling and reactivation mechanism could reveal new approaches to therapies. Here, we demonstrate that UPF1, known to stall peptide release during nonsense-mediated RNA decay, is critical for assembly of stalled polysomes in rat hippocampal neurons derived from embryos of either sex. Moreover, UPF1 and its interaction with the RNA binding protein STAU2 are necessary for proper transport and local translation from a prototypical RNA granule substrate and for mGluR-LTD in hippocampal neurons. These data highlight a new, neuronal role for UPF1, distinct from its RNA decay functions, in regulating transport and/or translation of mRNAs that are critical for synaptic plasticity. The elongation and/or termination steps of mRNA translation are emerging as important control points in mGluR-LTD, a form of synaptic plasticity that is compromised in a severe monogenic form of autism, Fragile X Syndrome. Deciphering the molecular mechanisms controlling this type of plasticity may thus open new therapeutic opportunities. Here, we describe a new role for the ATP-dependent helicase UPF1 and its interaction with the RNA localization protein STAU2 in mediating mGluR-LTD through the regulation of mRNA translation complexes stalled at the level of elongation and/or termination.
[Mh] Termos MeSH primário: Hipocampo/fisiologia
Plasticidade Neuronal/fisiologia
Neurônios/fisiologia
Polirribossomos/metabolismo
RNA Mensageiro/metabolismo
Proteínas de Ligação a RNA/metabolismo
Transmissão Sináptica/fisiologia
Transativadores/metabolismo
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Grânulos Citoplasmáticos/metabolismo
Feminino
Masculino
Ratos
Ratos Sprague-Dawley
Sinapses/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Messenger); 0 (RNA-Binding Proteins); 0 (Stau2 protein, rat); 0 (Trans-Activators); 0 (UPF1 protein, rat)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170820
[St] Status:MEDLINE
[do] DOI:10.1523/JNEUROSCI.0088-17.2017


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[PMID]:28606931
[Au] Autor:Wawiórka L; Molestak E; Szajwaj M; Michalec-Wawiórka B; Molon M; Borkiewicz L; Grela P; Boguszewska A; Tchórzewski M
[Ad] Endereço:Department of Molecular Biology, Maria Curie-Sklodowska University, Lublin, Poland mniak11@hektor.umcs.lublin.pl maro@hektor.umcs.lublin.pl.
[Ti] Título:Multiplication of Ribosomal P-Stalk Proteins Contributes to the Fidelity of Translation.
[So] Source:Mol Cell Biol;37(17), 2017 Sep 01.
[Is] ISSN:1098-5549
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The P-stalk represents a vital element within the ribosomal GTPase-associated center, which represents a landing platform for translational GTPases. The eukaryotic P-stalk exists as a uL10-(P1-P2) pentameric complex, which contains five identical C-terminal domains, one within each protein, and the presence of only one such element is sufficient to stimulate factor-dependent GTP hydrolysis and to sustain cell viability. The functional contribution of the P-stalk to the performance of the translational machinery , especially the role of P-protein multiplication, has never been explored. Here, we show that ribosomes depleted of P1/P2 proteins exhibit reduced translation fidelity at elongation and termination steps. The elevated rate of the decoding error is inversely correlated with the number of the P-proteins present on the ribosome. Unexpectedly, the lack of P1/P2 has little effect on the efficiency of other translational GTPase (trGTPase)-dependent steps of protein synthesis, including translocation. We have shown that loss of accuracy of decoding caused by P1/P2 depletion is the major cause of translation slowdown, which in turn affects the metabolic fitness of the yeast cell. We postulate that the multiplication of P-proteins is functionally coupled with the qualitative aspect of ribosome action, i.e., the recoding phenomenon shaping the cellular proteome.
[Mh] Termos MeSH primário: Polirribossomos/metabolismo
Proteínas Ribossômicas/metabolismo
Ribossomos/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: GTP Fosfo-Hidrolases/metabolismo
Fosfoproteínas/metabolismo
Estrutura Terciária de Proteína/fisiologia
Proteoma/metabolismo
Proteínas Ribossômicas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Phosphoproteins); 0 (Proteome); 0 (Ribosomal Proteins); EC 3.6.1.- (GTP Phosphohydrolases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170927
[Lr] Data última revisão:
170927
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170614
[St] Status:MEDLINE


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[PMID]:28558053
[Au] Autor:Bonnin P; Kern N; Young NT; Stansfield I; Romano MC
[Ad] Endereço:Institute for Complex Systems and Mathematical Biology, Physics Department, University of Aberdeen, Aberdeen, UK.
[Ti] Título:Novel mRNA-specific effects of ribosome drop-off on translation rate and polysome profile.
[So] Source:PLoS Comput Biol;13(5):e1005555, 2017 May.
[Is] ISSN:1553-7358
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The well established phenomenon of ribosome drop-off plays crucial roles in translational accuracy and nutrient starvation responses during protein translation. When cells are under stress conditions, such as amino acid starvation or aminoacyl-tRNA depletion due to a high level of recombinant protein expression, ribosome drop-off can substantially affect the efficiency of protein expression. Here we introduce a mathematical model that describes the effects of ribosome drop-off on the ribosome density along the mRNA and on the concomitant protein synthesis rate. Our results show that ribosome premature termination may lead to non-intuitive ribosome density profiles, such as a ribosome density which increases from the 5' to the 3' end. Importantly, the model predicts that the effects of ribosome drop-off on the translation rate are mRNA-specific, and we quantify their resilience to drop-off, showing that the mRNAs which present ribosome queues are much less affected by ribosome drop-off than those which do not. Moreover, among those mRNAs that do not present ribosome queues, resilience to drop-off correlates positively with the elongation rate, so that sequences using fast codons are expected to be less affected by ribosome drop-off. This result is consistent with a genome-wide analysis of S. cerevisiae, which reveals that under favourable growth conditions mRNAs coding for proteins involved in the translation machinery, known to be highly codon biased and using preferentially fast codons, are highly resilient to ribosome drop-off. Moreover, in physiological conditions, the translation rate of mRNAs coding for regulatory, stress-related proteins, is less resilient to ribosome drop-off. This model therefore allows analysis of variations in the translational efficiency of individual mRNAs by accounting for the full range of known ribosome behaviours, as well as explaining mRNA-specific variations in ribosome density emerging from ribosome profiling studies.
[Mh] Termos MeSH primário: Polirribossomos/genética
Biossíntese de Proteínas/fisiologia
RNA Mensageiro/genética
Ribossomos/genética
[Mh] Termos MeSH secundário: Biologia Computacional
Polirribossomos/metabolismo
RNA Fúngico/genética
RNA Fúngico/metabolismo
RNA Mensageiro/metabolismo
Ribossomos/metabolismo
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Fungal); 0 (RNA, Messenger)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170627
[Lr] Data última revisão:
170627
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170531
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pcbi.1005555


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[PMID]:28487214
[Au] Autor:Min KW; Davila S; Zealy RW; Lloyd LT; Lee IY; Lee R; Roh KH; Jung A; Jemielity J; Choi EJ; Chang JH; Yoon JH
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC 29425, USA.
[Ti] Título:eIF4E phosphorylation by MST1 reduces translation of a subset of mRNAs, but increases lncRNA translation.
[So] Source:Biochim Biophys Acta;1860(7):761-772, 2017 07.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Post-transcriptional gene regulation is an important step in eukaryotic gene expression. The last step to govern production of nascent peptides is during the process of mRNA translation. mRNA translation is controlled by many translation initiation factors that are susceptible to post-translational modifications. Here we report that one of the translation initiation factors, eIF4E, is phosphorylated by Mammalian Ste20-like kinase (MST1). Upon phosphorylation, eIF4E weakly interacts with the 5' CAP to inhibit mRNA translation. Simultaneously, active polyribosome is more associated with long noncoding RNAs (lncRNAs). Moreover, the linc00689-derived micropeptide, STORM (Stress- and TNF-α-activated ORF Micropeptide), is triggered by TNF-α-induced and MST1-mediated eIF4E phosphorylation, which exhibits molecular mimicry of SRP19 and, thus, competes for 7SL RNA. Our findings have uncovered a novel function of MST1 in mRNA and lncRNA translation by direct phosphorylation of eIF4E. This novel signaling pathway will provide new platforms for regulation of mRNA translation via post-translational protein modification.
[Mh] Termos MeSH primário: Fator de Iniciação 4E em Eucariotos/metabolismo
Fator de Crescimento de Hepatócito/metabolismo
Fosforilação/fisiologia
Biossíntese de Proteínas/fisiologia
Proteínas Proto-Oncogênicas/metabolismo
RNA Longo não Codificante/metabolismo
RNA Mensageiro/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Linhagem Celular
Linhagem Celular Tumoral
Regulação da Expressão Gênica/fisiologia
Células HeLa
Seres Humanos
Camundongos
Polirribossomos/metabolismo
Processamento de Proteína Pós-Traducional/fisiologia
Capuzes de RNA/metabolismo
Transdução de Sinais/fisiologia
Fator de Necrose Tumoral alfa/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., INTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Eukaryotic Initiation Factor-4E); 0 (Proto-Oncogene Proteins); 0 (RNA Caps); 0 (RNA, Long Noncoding); 0 (RNA, Messenger); 0 (Tumor Necrosis Factor-alpha); 0 (macrophage stimulating protein); 67256-21-7 (Hepatocyte Growth Factor)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170511
[St] Status:MEDLINE


  9 / 5934 MEDLINE  
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[PMID]:28446607
[Au] Autor:Wang JL; Saha TT; Zhang Y; Zhang C; Raikhel AS
[Ad] Endereço:From the Department of Entomology, University of California, Riverside, California 92521.
[Ti] Título:Juvenile hormone and its receptor methoprene-tolerant promote ribosomal biogenesis and vitellogenesis in the mosquito.
[So] Source:J Biol Chem;292(24):10306-10315, 2017 Jun 16.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Juvenile hormone (JH) controls many biological activities in insects, including development, metamorphosis, and reproduction. In the mosquito, a vector of dengue, yellow fever, chikungunya, and zika viruses, the metabolic tissue (the fat body, which is an analogue of the vertebrate liver) produces yolk proteins for developing oocytes. JH is important for the fat body to acquire competence for yolk protein production. However, the molecular mechanisms of how JH promotes mosquito reproduction are not completely understood. In this study we show that stimulation of the JH receptor methoprene-tolerant (Met) activates expression of genes encoding the regulator of ribosome synthesis 1 (RRS1) and six ribosomal proteins (two ribosomal large subunit proteins, two ribosomal small subunit proteins, and two mitochondrial ribosomal proteins). Moreover, RNAi-mediated depletion of decreased biosynthesis of the ribosomal protein L32 (RpL32). Depletion of , , or led to retardation of ovarian growth and reduced mosquito fecundity, which may at least in part have resulted from decreased vitellogenin protein production in the fat body. In summary, our results indicate that JH is critical for inducing the expression of ribosomal protein genes and demonstrate that RRS1 mediates the JH signal to enhance both ribosomal biogenesis and vitellogenesis.
[Mh] Termos MeSH primário: Aedes/metabolismo
Proteínas de Insetos/agonistas
Hormônios Juvenis/metabolismo
Biogênese de Organelas
Proteínas Ribossômicas/agonistas
Ribossomos/metabolismo
Vitelogênese
[Mh] Termos MeSH secundário: Aedes/crescimento & desenvolvimento
Animais
Corpo Adiposo/crescimento & desenvolvimento
Corpo Adiposo/metabolismo
Feminino
Perfilação da Expressão Gênica
Regulação da Expressão Gênica no Desenvolvimento
Proteínas de Insetos/antagonistas & inibidores
Proteínas de Insetos/genética
Proteínas de Insetos/metabolismo
Resistência a Inseticidas
Proteínas Mitocondriais/agonistas
Proteínas Mitocondriais/genética
Proteínas Mitocondriais/metabolismo
Técnicas de Cultura de Órgãos
Ovário/crescimento & desenvolvimento
Ovário/metabolismo
Polirribossomos/metabolismo
Interferência de RNA
Proteínas Ribossômicas/antagonistas & inibidores
Proteínas Ribossômicas/genética
Proteínas Ribossômicas/metabolismo
Transdução de Sinais
Vitelogeninas/antagonistas & inibidores
Vitelogeninas/genética
Vitelogeninas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Insect Proteins); 0 (Juvenile Hormones); 0 (Mitochondrial Proteins); 0 (Ribosomal Proteins); 0 (Vitellogenins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170706
[Lr] Data última revisão:
170706
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.761387


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[PMID]:28379492
[Au] Autor:Rossi A; Moro A; Tebaldi T; Cornella N; Gasperini L; Lunelli L; Quattrone A; Viero G; Macchi P
[Ad] Endereço:Laboratory of Molecular and Cellular Neurobiology, Centre for Integrative Biology, University of Trento, via Sommarive 9, 38123 Trento (TN), Italy.
[Ti] Título:Identification and dynamic changes of RNAs isolated from RALY-containing ribonucleoprotein complexes.
[So] Source:Nucleic Acids Res;45(11):6775-6792, 2017 Jun 20.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:RALY is a member of the heterogeneous nuclear ribonucleoprotein family (hnRNP), a large family of RNA-binding proteins involved in many aspects of RNA metabolism. Although RALY interactome has been recently characterized, a comprehensive global analysis of RALY-associated RNAs is lacking and the biological function of RALY remains elusive. Here, we performed RIP-seq analysis to identify RALY interacting RNAs and assessed the role of RALY in gene expression. We demonstrate that RALY binds specific coding and non-coding RNAs and associates with translating mRNAs of mammalian cells. Among the identified transcripts, we focused on ANXA1 and H1FX mRNAs, encoding for Annexin A1 and for the linker variant of the histone H1X, respectively. Both proteins are differentially expressed by proliferating cells and are considered as markers for tumorigenesis. We demonstrate that cells lacking RALY expression exhibit changes in the levels of H1FX and ANXA1 mRNAs and proteins in an opposite manner. We also provide evidence for a direct binding of RALY to the U-rich elements present within the 3΄UTR of both transcripts. Thus, our results identify RALY as a poly-U binding protein and as a regulator of H1FX and ANXA1 in mammalian cells.
[Mh] Termos MeSH primário: Ribonucleoproteínas Nucleares Heterogêneas Grupo C/fisiologia
RNA Mensageiro/metabolismo
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas
Anexina A1/genética
Anexina A1/metabolismo
Carcinogênese/genética
Carcinogênese/metabolismo
Ciclo Celular
Regulação Neoplásica da Expressão Gênica
Células HEK293
Células HeLa
Seres Humanos
Células Jurkat
Células MCF-7
Polirribossomos/metabolismo
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (Annexin A1); 0 (Heterogeneous-Nuclear Ribonucleoprotein Group C); 0 (RALY protein, human); 0 (RNA, Messenger)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170406
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx235



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