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[PMID]:29381712
[Au] Autor:Gallie DR
[Ad] Endereço:Department of Biochemistry, University of California, Riverside, CA, United States of America.
[Ti] Título:Plant growth and fertility requires functional interactions between specific PABP and eIF4G gene family members.
[So] Source:PLoS One;13(1):e0191474, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The initiation of protein synthesis requires the involvement of the eukaryotic translation initiation factor (eIF) 4G to promote assembly of the factors needed to recruit a 40S ribosomal subunit to an mRNA. Although many eukaryotes express two eIF4G isoforms that are highly similar, those in plants, referred to as eIF4G and eIFiso4G, are highly divergent in size, sequence, and domain organization. Species of the Brassicaceae and the Cleomaceae also express a divergent eIFiso4G isoform, referred to as eIFiso4G2, not found elsewhere in the plant kingdom. Despite their divergence, eIF4G and eIFiso4G interact with eIF4A, eIF4B, and eIF4E isoforms needed for binding an mRNA. eIF4G and eIFiso4G also interact with the poly(A)-binding protein (PABP) which promotes ribosome recruitment to an mRNA. Increasing the complexity of such an interaction, however, Arabidopsis also expresses three PABP isoforms (PAB2, PAB4, and PAB8) in vegetative and reproductive tissues. In this study, the functional interactions among the eIF4G and the widely-expressed PABP isoforms were examined. Loss of PAB2 or PAB8 in combination with loss of eIF4G or eIFiso4G had little to no effect on growth or fertility whereas pab2 pab8 eif4g or pab2 pab8 eifiso4g1/2 mutants exhibited smaller stature and reduced fertility. Although the pab4 eifiso4g1 mutant grows normally and is fertile, pab4 eif4g or pab4 eifiso4g2 mutants could not be isolated. Even pab4/PAB4 eif4g/eIF4G heterozygous plants exhibited growth defects and low fertility. Mutant co-inheritance analysis in reciprocal crosses with wild-type plants revealed that most ovaries and pollen from pab4/PAB4 eif4g/eIF4G plants were PAB4 eif4g. Similarly, co-inheritance studies with pab4/PAB4 eifiso4g2/eIFiso4G2 plants suggested most ovaries were PAB4 eifiso4g2. These results suggest that a functional interaction between PAB4 and eIF4G and between PAB4 and eIFiso4G2 is required for growth and normal fertility.
[Mh] Termos MeSH primário: Arabidopsis/genética
Fator de Iniciação 4G em Eucariotos/metabolismo
Fertilidade
Desenvolvimento Vegetal
Proteínas de Plantas/fisiologia
Proteínas de Ligação a Poli(A)/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Plantas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, P.H.S.
[Nm] Nome de substância:
0 (Eukaryotic Initiation Factor-4G); 0 (Plant Proteins); 0 (Poly(A)-Binding Proteins)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180131
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191474


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[PMID]:29295980
[Au] Autor:Barragán-Iglesias P; Lou TF; Bhat VD; Megat S; Burton MD; Price TJ; Campbell ZT
[Ad] Endereço:School of Behavioral and Brain Sciences, University of Texas at Dallas, Richardson, TX, 75080, USA.
[Ti] Título:Inhibition of Poly(A)-binding protein with a synthetic RNA mimic reduces pain sensitization in mice.
[So] Source:Nat Commun;9(1):10, 2018 01 02.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Nociceptors rely on cap-dependent translation to rapidly induce protein synthesis in response to pro-inflammatory signals. Comparatively little is known regarding the role of the regulatory factors bound to the 3' end of mRNA in nociceptor sensitization. Poly(A)-binding protein (PABP) stimulates translation initiation by bridging the Poly(A) tail to the eukaryotic initiation factor 4F complex associated with the mRNA cap. Here, we use unbiased assessment of PABP binding specificity to generate a chemically modified RNA-based competitive inhibitor of PABP. The resulting RNA mimic, which we designated as the Poly(A) SPOT-ON, is more stable than unmodified RNA and binds PABP with high affinity and selectivity in vitro. We show that injection of the Poly(A) SPOT-ON at the site of an injury can attenuate behavioral response to pain. Collectively, these results suggest that PABP is integral for nociceptive plasticity. The general strategy described here provides a broad new source of mechanism-based inhibitors for RNA-binding proteins and is applicable for in vivo studies.
[Mh] Termos MeSH primário: Dor/metabolismo
Poli A/metabolismo
Proteínas de Ligação a Poli(A)/metabolismo
RNA/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Células Cultivadas
Gânglios Espinais/citologia
Seres Humanos
Camundongos
Neurônios/efeitos dos fármacos
Neurônios/metabolismo
Dor Nociceptiva/metabolismo
Dor Nociceptiva/prevenção & controle
Dor/prevenção & controle
Medição da Dor
Poli A/química
Poli A/farmacologia
Proteínas de Ligação a Poli(A)/química
Ligação Proteica
RNA/química
RNA/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Poly(A)-Binding Proteins); 24937-83-5 (Poly A); 63231-63-0 (RNA)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180104
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02449-5


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[PMID]:28467675
[Au] Autor:Urakov VN; Mitkevich OV; Safenkova IV; Ter-Avanesyan MD
[Ad] Endereço:Federal Research Center 'Fundamentals of Biotechnology' of the Russian Academy of Sciences, Bach Institute of Biochemistry, Moscow, Russia.
[Ti] Título:Ribosome-bound Pub1 modulates stop codon decoding during translation termination in yeast.
[So] Source:FEBS J;284(12):1914-1930, 2017 06.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In eukaryotes, termination of translation is controlled by polypeptide chain release factors eRF1 and eRF3, of which the former recognizes nonsense codons, while the latter interacts with eRF1 and stimulates polypeptide release from the ribosome in a GTP- dependent manner, and ABCE1, which facilitates ribosome recycling. In this work, we demonstrate that Pub1, a yeast protein known to be involved in stress granule formation, regulation of gene expression, and organization of the tubulin cytoskeleton, also plays a role in translation termination. Pub1 was shown to bind to ribosomes independent of eRF1 and eRF3 and to interact with the N-terminal glutamine-/asparagine-rich prion domain of eRF3 via its short C-terminal glutamine-rich tract. High velocity sedimentation in sucrose gradient demonstrated that Pub1 was preferentially associated with heavy polysomes enriched with terminating ribosomes. Lack of Pub1 decreased efficiency of nonsense readthrough at a majority but not all tetranucleotide stop signals. This distinguishes Pub1 from most other known binding partners of the release factors which were shown to modulate readthrough of all nonsense codons uniformly. The obtained data show that Pub1 can act as an accessory translation factor involved in fine-tuning of translation termination.
[Mh] Termos MeSH primário: Fatores de Terminação de Peptídeos/metabolismo
Proteínas de Ligação a Poli(A)/metabolismo
Ribossomos/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Códon de Terminação
Terminação Traducional da Cadeia Peptídica
Fatores de Terminação de Peptídeos/genética
Proteínas de Ligação a Poli(A)/genética
Ribossomos/genética
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/crescimento & desenvolvimento
Proteínas de Saccharomyces cerevisiae/genética
Deleção de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Codon, Terminator); 0 (PUB1 protein, S cerevisiae); 0 (Peptide Termination Factors); 0 (Poly(A)-Binding Proteins); 0 (Saccharomyces cerevisiae Proteins); 0 (peptide-chain-release factor 3)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1111/febs.14099


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[PMID]:28817800
[Au] Autor:Mackenzie IR; Nicholson AM; Sarkar M; Messing J; Purice MD; Pottier C; Annu K; Baker M; Perkerson RB; Kurti A; Matchett BJ; Mittag T; Temirov J; Hsiung GR; Krieger C; Murray ME; Kato M; Fryer JD; Petrucelli L; Zinman L; Weintraub S; Mesulam M; Keith J; Zivkovic SA; Hirsch-Reinshagen V; Roos RP; Züchner S; Graff-Radford NR; Petersen RC; Caselli RJ; Wszolek ZK; Finger E; Lippa C; Lacomis D; Stewart H; Dickson DW; Kim HJ; Rogaeva E; Bigio E; Boylan KB; Taylor JP; Rademakers R
[Ad] Endereço:Department of Pathology and Laboratory Medicine, Vancouver Coastal Health and the University of British Colombia, Vancouver, BC V6T 2B5, Canada.
[Ti] Título:TIA1 Mutations in Amyotrophic Lateral Sclerosis and Frontotemporal Dementia Promote Phase Separation and Alter Stress Granule Dynamics.
[So] Source:Neuron;95(4):808-816.e9, 2017 Aug 16.
[Is] ISSN:1097-4199
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) are age-related neurodegenerative disorders with shared genetic etiologies and overlapping clinical and pathological features. Here we studied a novel ALS/FTD family and identified the P362L mutation in the low-complexity domain (LCD) of T cell-restricted intracellular antigen-1 (TIA1). Subsequent genetic association analyses showed an increased burden of TIA1 LCD mutations in ALS patients compared to controls (p = 8.7 × 10 ). Postmortem neuropathology of five TIA1 mutations carriers showed a consistent pathological signature with numerous round, hyaline, TAR DNA-binding protein 43 (TDP-43)-positive inclusions. TIA1 mutations significantly increased the propensity of TIA1 protein to undergo phase transition. In live cells, TIA1 mutations delayed stress granule (SG) disassembly and promoted the accumulation of non-dynamic SGs that harbored TDP-43. Moreover, TDP-43 in SGs became less mobile and insoluble. The identification of TIA1 mutations in ALS/FTD reinforces the importance of RNA metabolism and SG dynamics in ALS/FTD pathogenesis.
[Mh] Termos MeSH primário: Esclerose Amiotrófica Lateral/genética
Esclerose Amiotrófica Lateral/patologia
Demência Frontotemporal/genética
Demência Frontotemporal/patologia
Mutação/genética
Proteínas de Ligação a Poli(A)/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
Proteínas de Ligação a DNA/metabolismo
Saúde da Família
Feminino
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Células HeLa
Ribonucleoproteína Nuclear Heterogênea A1
Ribonucleoproteínas Nucleares Heterogêneas Grupo A-B/metabolismo
Seres Humanos
Masculino
Microscopia Confocal
Meia-Idade
Proteína FUS de Ligação a RNA/metabolismo
Estresse Fisiológico/fisiologia
Antígeno-1 Intracelular de Células T
Fatores de Tempo
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (FUS protein, human); 0 (Heterogeneous Nuclear Ribonucleoprotein A1); 0 (Heterogeneous-Nuclear Ribonucleoprotein Group A-B); 0 (Poly(A)-Binding Proteins); 0 (RNA-Binding Protein FUS); 0 (T-Cell Intracellular Antigen-1); 0 (TDP-43 protein, human); 0 (TIA1 protein, human); 147336-22-9 (Green Fluorescent Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170818
[St] Status:MEDLINE


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[PMID]:28738064
[Au] Autor:Contreras-Treviño HI; Reyna-Rosas E; León-Rodríguez R; Ruiz-Ordaz BH; Dinkova TD; Cevallos AM; Padilla-Noriega L
[Ad] Endereço:Programa de Maestría y Doctorado en Ciencias Bioquímicas, Universidad Nacional Autónoma de México, Mexico City, Mexico.
[Ti] Título:Species A rotavirus NSP3 acquires its translation inhibitory function prior to stable dimer formation.
[So] Source:PLoS One;12(7):e0181871, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Species A rotavirus non-structural protein 3 (NSP3) is a translational regulator that inhibits or, under some conditions, enhances host cell translation. NSP3 binds to the translation initiation factor eIF4G1 and evicts poly-(A) binding protein (PABP) from eIF4G1, thus inhibiting translation of polyadenylated mRNAs, presumably by disrupting the effect of PABP bound to their 3'-ends. NSP3 has a long coiled-coil region involved in dimerization that includes a chaperone Hsp90-binding domain (HS90BD). We aimed to study the role in NSP3 dimerization of a segment of the coiled-coil region adjoining the HS90BD. We used a vaccinia virus system to express NSP3 with point mutations in conserved amino acids in the coiled-coil region and determined the effects of these mutations on translation by metabolic labeling of proteins as well as on accumulation of stable NSP3 dimers by non-dissociating Western blot, a method that separates stable NSP3 dimers from the monomer/dimerization intermediate forms of the protein. Four of five mutations reduced the total yield of NSP3 and the formation of stable dimers (W170A, K171E, R173E and R187E:K191E), whereas one mutation had the opposite effects (Y192A). Treatment with the proteasome inhibitor MG132 revealed that stable NSP3 dimers and monomers/dimerization intermediates are susceptible to proteasome degradation. Surprisingly, mutants severely impaired in the formation of stable dimers were still able to inhibit host cell translation, suggesting that NSP3 dimerization intermediates are functional. Our results demonstrate that rotavirus NSP3 acquires its function prior to stable dimer formation and remain as a proteasome target throughout dimerization.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/genética
Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Biossíntese de Proteínas/genética
Multimerização Proteica/genética
Proteínas não Estruturais Virais/genética
Proteínas não Estruturais Virais/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sítios de Ligação/genética
Linhagem Celular
Cercopithecus aethiops
Fator de Iniciação 4G em Eucariotos/genética
Fator de Iniciação 4G em Eucariotos/metabolismo
Mutação Puntual/genética
Proteínas de Ligação a Poli(A)/genética
Ligação Proteica/genética
RNA Mensageiro/genética
RNA Viral/genética
Rotavirus/genética
Infecções por Rotavirus/virologia
Alinhamento de Sequência
Replicação Viral/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Eukaryotic Initiation Factor-4G); 0 (Poly(A)-Binding Proteins); 0 (RNA, Messenger); 0 (RNA, Viral); 0 (Viral Nonstructural Proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170921
[Lr] Data última revisão:
170921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170725
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0181871


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[PMID]:28630277
[Au] Autor:Carrascoso I; Alcalde J; Sánchez-Jiménez C; González-Sánchez P; Izquierdo JM
[Ad] Endereço:Centro de Biología Molecular Severo Ochoa, Consejo Superior de Investigaciones Científicas, Universidad Autónoma de Madrid, Madrid, Spain.
[Ti] Título:T-Cell Intracellular Antigens and Hu Antigen R Antagonistically Modulate Mitochondrial Activity and Dynamics by Regulating Optic Atrophy 1 Gene Expression.
[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:Mitochondria undergo frequent morphological changes to control their function. We show here that T-cell intracellular antigens (TIA1b/TIARb) and Hu antigen R (HuR) have antagonistic roles in mitochondrial function by modulating the expression of mitochondrial shaping proteins. Expression of TIA1b/TIARb alters the mitochondrial dynamic network by enhancing fission and clustering, which is accompanied by a decrease in respiration. In contrast, HuR expression promotes fusion and cristae remodeling and increases respiratory activity. Mechanistically, TIA proteins downregulate the expression of optic atrophy 1 (OPA1) protein via switching of the splicing patterns of OPA1 to facilitate the production of OPA1 variant 5 (OPA1v5). Conversely, HuR enhances the expression of OPA1 mRNA isoforms through increasing steady-state levels and targeting translational efficiency at the 3' untranslated region. Knockdown of TIA1/TIAR or HuR partially reversed the expression profile of OPA1, whereas knockdown of OPA1 or overexpression of OPA1v5 provoked mitochondrial clustering. Middle-term expression of TIA1b/TIARb triggers reactive oxygen species production and mitochondrial DNA damage, which is accompanied by mitophagy, autophagy, and apoptosis. In contrast, HuR expression promotes mitochondrion-dependent cell proliferation. Collectively, these results provide molecular insights into the antagonistic functions of TIA1b/TIARb and HuR in mitochondrial activity dynamics and suggest that their balance might contribute to mitochondrial physiopathology.
[Mh] Termos MeSH primário: Proteína Semelhante a ELAV 1/metabolismo
Expressão Gênica/fisiologia
Mitocôndrias/metabolismo
Membranas Mitocondriais/metabolismo
Atrofia Óptica Autossômica Dominante/genética
Atrofia Óptica Autossômica Dominante/metabolismo
Proteínas de Ligação a Poli(A)/metabolismo
[Mh] Termos MeSH secundário: Proliferação Celular
Citoplasma/metabolismo
GTP Fosfo-Hidrolases/metabolismo
Seres Humanos
Mitocôndrias/genética
Dinâmica Mitocondrial/genética
Proteínas Mitocondriais/genética
Proteínas Mitocondriais/metabolismo
RNA Mensageiro/genética
Antígeno-1 Intracelular de Células T
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ELAV-Like Protein 1); 0 (ELAVL1 protein, human); 0 (Mitochondrial Proteins); 0 (Poly(A)-Binding Proteins); 0 (RNA, Messenger); 0 (T-Cell Intracellular Antigen-1); 0 (TIA1 protein, human); EC 3.6.1.- (GTP Phosphohydrolases)
[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:170621
[St] Status:MEDLINE


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[PMID]:28298474
[Au] Autor:Motohashi H; Mukudai Y; Ito C; Kato K; Shimane T; Kondo S; Shirota T
[Ad] Endereço:Department of Oral and Maxillofacial Surgery, School of Dentistry, Showa University, 2-1-1 Kitasenzoku, Ota-ku, Tokyo 145-8515, Japan.
[Ti] Título:Tumor protein D52 expression is post-transcriptionally regulated by T-cell intercellular antigen (TIA) 1 and TIA-related protein via mRNA stability.
[So] Source:Biochem J;474(10):1669-1687, 2017 May 04.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Although tumor protein D52 (TPD52) family proteins were first identified nearly 20 years ago, their molecular regulatory mechanisms remain unclear. Therefore, we investigated the post-transcriptional regulation of TPD52 family genes. An RNA immunoprecipitation (RIP) assay showed the potential binding ability of TPD52 family mRNAs to several RNA-binding proteins, and an RNA degradation assay revealed that TPD52 is subject to more prominent post-transcriptional regulation than are TPD53 and TPD54. We subsequently focused on the 3'-untranslated region (3'-UTR) of TPD52 as a -acting element in post-transcriptional gene regulation. Several deletion mutants of the 3'-UTR of TPD52 mRNA were constructed and ligated to the 3'-end of a reporter green fluorescence protein gene. An RNA degradation assay revealed that a minimal -acting region, located in the 78-280 region of the 5'-proximal region of the 3'-UTR, stabilized the reporter mRNA. Biotin pull-down and RIP assays revealed specific binding of the region to T-cell intracellular antigen 1 (TIA-1) and TIA-1-related protein (TIAR). Knockdown of TIA-1/TIAR decreased not only the expression, but also the stability of TPD52 mRNA; it also decreased the expression and stability of the reporter gene ligated to the 3'-end of the 78-280 fragment. Stimulation of transforming growth factor-ß and epidermal growth factor decreased the binding ability of these factors, resulting in decreased mRNA stability. These results indicate that the 78-280 fragment and TIA-1/TIAR concordantly contribute to mRNA stability as a -acting element and -acting factor(s), respectively. Thus, we here report the specific interactions between these elements in the post-transcriptional regulation of the TPD52 gene.
[Mh] Termos MeSH primário: Regulação Neoplásica da Expressão Gênica
Proteínas de Neoplasias/metabolismo
Proteínas de Ligação a Poli(A)/metabolismo
RNA Mensageiro/metabolismo
RNA Neoplásico/metabolismo
Proteínas de Ligação a RNA/metabolismo
Elementos de Resposta
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas
Linhagem Celular Tumoral
Células Cultivadas
Técnicas de Silenciamento de Genes
Genes Reporter
Seres Humanos
Imunoprecipitação
Proteínas de Neoplasias/antagonistas & inibidores
Proteínas de Neoplasias/química
Proteínas de Neoplasias/genética
Fragmentos de Peptídeos/antagonistas & inibidores
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Proteínas de Ligação a Poli(A)/antagonistas & inibidores
Proteínas de Ligação a Poli(A)/genética
Interferência de RNA
Estabilidade de RNA
RNA Mensageiro/antagonistas & inibidores
RNA Mensageiro/química
RNA Neoplásico/antagonistas & inibidores
RNA Neoplásico/química
Proteínas de Ligação a RNA/antagonistas & inibidores
Proteínas de Ligação a RNA/genética
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Deleção de Sequência
Antígeno-1 Intracelular de Células T
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (Neoplasm Proteins); 0 (Peptide Fragments); 0 (Poly(A)-Binding Proteins); 0 (RNA, Messenger); 0 (RNA, Neoplasm); 0 (RNA-Binding Proteins); 0 (Recombinant Proteins); 0 (T-Cell Intracellular Antigen-1); 0 (TIA1 protein, human); 0 (TPD52 protein, human); 0 (TPD52L1 protein, human); 0 (TPD52L2 protein, human); 148592-68-1 (TIAL1 protein, human)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170317
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20160942


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[PMID]:28283065
[Au] Autor:Kroschwald S; Alberti S
[Ad] Endereço:Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
[Ti] Título:Gel or Die: Phase Separation as a Survival Strategy.
[So] Source:Cell;168(6):947-948, 2017 03 09.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Stress conditions trigger protein assembly by demixing from the cytoplasm, but the biological significance is still unclear. In this issue of Cell, Riback et al. report that the yeast poly(A)-binding protein 1 (Pab1) is a phase-separating stress sensor that boosts organismal fitness under physiological stress conditions.
[Mh] Termos MeSH primário: Proteína I de Ligação a Poli(A)/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Citoplasma/metabolismo
Proteínas de Ligação a Poli(A)/metabolismo
Proteínas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; COMMENT
[Nm] Nome de substância:
0 (Poly(A)-Binding Protein I); 0 (Poly(A)-Binding Proteins); 0 (Proteins)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170623
[Lr] Data última revisão:
170623
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170312
[St] Status:MEDLINE


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[PMID]:28283059
[Au] Autor:Riback JA; Katanski CD; Kear-Scott JL; Pilipenko EV; Rojek AE; Sosnick TR; Drummond DA
[Ad] Endereço:Graduate Program in the Biophysical Sciences, University of Chicago, Chicago, IL 60673, USA.
[Ti] Título:Stress-Triggered Phase Separation Is an Adaptive, Evolutionarily Tuned Response.
[So] Source:Cell;168(6):1028-1040.e19, 2017 Mar 09.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In eukaryotic cells, diverse stresses trigger coalescence of RNA-binding proteins into stress granules. In vitro, stress-granule-associated proteins can demix to form liquids, hydrogels, and other assemblies lacking fixed stoichiometry. Observing these phenomena has generally required conditions far removed from physiological stresses. We show that poly(A)-binding protein (Pab1 in yeast), a defining marker of stress granules, phase separates and forms hydrogels in vitro upon exposure to physiological stress conditions. Other RNA-binding proteins depend upon low-complexity regions (LCRs) or RNA for phase separation, whereas Pab1's LCR is not required for demixing, and RNA inhibits it. Based on unique evolutionary patterns, we create LCR mutations, which systematically tune its biophysical properties and Pab1 phase separation in vitro and in vivo. Mutations that impede phase separation reduce organism fitness during prolonged stress. Poly(A)-binding protein thus acts as a physiological stress sensor, exploiting phase separation to precisely mark stress onset, a broadly generalizable mechanism.
[Mh] Termos MeSH primário: Grânulos Citoplasmáticos/metabolismo
Proteínas de Ligação a Poli(A)/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/citologia
Saccharomyces cerevisiae/fisiologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Grânulos Citoplasmáticos/química
Temperatura Alta
Concentração de Íons de Hidrogênio
Interações Hidrofóbicas e Hidrofílicas
Proteínas Intrinsicamente Desordenadas/química
Proteínas Intrinsicamente Desordenadas/metabolismo
Mutagênese
Proteínas de Ligação a Poli(A)/química
Proteínas de Ligação a Poli(A)/genética
Prolina/análise
Prolina/metabolismo
Domínios Proteicos
Ribonucleases/metabolismo
Saccharomyces cerevisiae/crescimento & desenvolvimento
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/genética
Alinhamento de Sequência
Estresse Fisiológico
[Pt] Tipo de publicação:JOURNAL ARTICLE; COMMENT
[Nm] Nome de substância:
0 (Intrinsically Disordered Proteins); 0 (Poly(A)-Binding Proteins); 0 (Saccharomyces cerevisiae Proteins); 0 (pab1 protein, S cerevisiae); 9DLQ4CIU6V (Proline); EC 3.1.- (Ribonucleases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170714
[Lr] Data última revisão:
170714
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170312
[St] Status:MEDLINE


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[PMID]:28257633
[Au] Autor:Liu Y; Liu R; Yang F; Cheng R; Chen X; Cui S; Gu Y; Sun W; You C; Liu Z; Sun F; Wang Y; Fu Z; Ye C; Zhang C; Li J; Chen X
[Ad] Endereço:State Key Laboratory of Pharmaceutical Biotechnology, Collaborative Innovation Center of Chemistry for Life Sciences, Jiangsu Engineering Research Center for MicroRNA Biology and Biotechnology, NJU Advanced Institute for Life Sciences (NAILS), School of Life Sciences, Nanjing University, 163 Xianlin
[Ti] Título:miR-19a promotes colorectal cancer proliferation and migration by targeting TIA1.
[So] Source:Mol Cancer;16(1):53, 2017 Mar 04.
[Is] ISSN:1476-4598
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Colorectal cancer (CRC) is a major worldwide health problem due to its high prevalence and mortality rate. T-cell intracellular antigen 1 (TIA1) is an important tumor suppressor involved in many aspects of carcinogenesis and cancer development. How TIA1 expression is regulated during CRC development remains to be carefully elucidated. METHODS: In CRC tissue sample pairs, TIA1 protein and mRNA levels were monitored by Western blot and qRT-PCR, respectively. Combining meta-analysis and miRNA target prediction software, we could predict microRNAs that targeted TIA1. Next, three CRC cell lines (SW480, Caco2 and HT29) were used to demonstrate the direct targeting of TIA1 by miR-19a. In addition, we investigated the biological effects of TIA1 inhibition by miR-19a both in vitro by CCK-8, EdU, Transwell, Ki67 immunofluorescence and Colony formation assays and in vivo by a xenograft mice model. RESULTS: In colorectal cancer (CRC), we found that TIA1 protein, but not its mRNA, was downregulated. We predicted that TIA1 was a target of miR-19a and validated that miR-19a binded directly to the 3'-UTR of TIA1 mRNA. miR-19a could promote cell proliferation and migration in CRC cells and accelerated tumor growth in xenograft mice by targeting TIA1. CONCLUSIONS: This study highlights an oncomiR role for miR-19a in regulating TIA1 in CRC and suggests that miR-19a may be a novel molecular therapeutic target for CRC.
[Mh] Termos MeSH primário: Neoplasias Colorretais/genética
MicroRNAs/genética
Proteínas de Ligação a Poli(A)/genética
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas
Animais
Proteínas Reguladoras de Apoptose/genética
Sítios de Ligação
Linhagem Celular Tumoral
Movimento Celular/genética
Proliferação Celular/genética
Neoplasias Colorretais/metabolismo
Neoplasias Colorretais/patologia
Modelos Animais de Doenças
Perfilação da Expressão Gênica
Regulação Neoplásica da Expressão Gênica
Genes myc
Xenoenxertos
Seres Humanos
Masculino
Metanálise como Assunto
Camundongos
Proteínas de Ligação a Poli(A)/metabolismo
Interferência de RNA
Processamento Pós-Transcricional do RNA
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Proteínas de Ligação a RNA/genética
Antígeno-1 Intracelular de Células T
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (Apoptosis Regulatory Proteins); 0 (MIRN19 microRNA, human); 0 (MicroRNAs); 0 (PDCD4 protein, human); 0 (Poly(A)-Binding Proteins); 0 (RNA, Messenger); 0 (RNA-Binding Proteins); 0 (T-Cell Intracellular Antigen-1); 0 (TIA1 protein, human)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170305
[St] Status:MEDLINE
[do] DOI:10.1186/s12943-017-0625-8



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