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Pesquisa : D12.776.835.725 [Categoria DeCS]
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[PMID]:29030484
[Au] Autor:Rojas-Ríos P; Chartier A; Pierson S; Simonelig M
[Ad] Endereço:mRNA Regulation and Development, Institute of Human Genetics, UMR9002 CNRS-Université de Montpellier, Montpellier Cedex 5, France.
[Ti] Título:Aubergine and piRNAs promote germline stem cell self-renewal by repressing the proto-oncogene .
[So] Source:EMBO J;36(21):3194-3211, 2017 Nov 02.
[Is] ISSN:1460-2075
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:PIWI proteins play essential roles in germ cells and stem cell lineages. In , Piwi is required in somatic niche cells and germline stem cells (GSCs) to support GSC self-renewal and differentiation. Whether and how other PIWI proteins are involved in GSC biology remains unknown. Here, we show that Aubergine (Aub), another PIWI protein, is intrinsically required in GSCs for their self-renewal and differentiation. Aub needs to be loaded with piRNAs to control GSC self-renewal and acts through direct mRNA regulation. We identify the proto-oncogene, a regulator of mammalian hematopoietic stem cells, as a novel GSC differentiation factor. Aub stimulates GSC self-renewal by repressing mRNA translation and does so in part through recruitment of the CCR4-NOT complex. This study reveals the role of piRNAs and PIWI proteins in controlling stem cell homeostasis via translational repression and highlights piRNAs as major post-transcriptional regulators in key developmental decisions.
[Mh] Termos MeSH primário: Proteínas de Drosophila/genética
Drosophila melanogaster/genética
Células Germinativas/metabolismo
Fatores de Iniciação de Peptídeos/genética
Proteínas Proto-Oncogênicas c-cbl/genética
RNA Interferente Pequeno/genética
Células-Tronco/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas Argonauta/genética
Proteínas Argonauta/metabolismo
Sequência de Bases
Proteínas de Transporte/genética
Proteínas de Transporte/metabolismo
Diferenciação Celular
Linhagem da Célula/genética
Proteínas de Drosophila/metabolismo
Drosophila melanogaster/crescimento & desenvolvimento
Drosophila melanogaster/metabolismo
Embrião não Mamífero
Regulação da Expressão Gênica no Desenvolvimento
Células Germinativas/crescimento & desenvolvimento
Fatores de Iniciação de Peptídeos/metabolismo
Proteínas Proto-Oncogênicas c-cbl/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
RNA Interferente Pequeno/metabolismo
Ribonucleases/genética
Ribonucleases/metabolismo
Células-Tronco/citologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Argonaute Proteins); 0 (Carrier Proteins); 0 (Drosophila Proteins); 0 (NOT1 protein, Drosophila); 0 (Peptide Initiation Factors); 0 (RNA, Messenger); 0 (RNA, Small Interfering); 0 (aubergine protein, Drosophila); 0 (piwi protein, Drosophila); EC 2.3.2.27 (Proto-Oncogene Proteins c-cbl); EC 3.1.- (CCR4 protein, Drosophila); EC 3.1.- (Ribonucleases); EC 6.3.2.- (Cbl protein, Drosophila)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171015
[St] Status:MEDLINE
[do] DOI:10.15252/embj.201797259


  2 / 3590 MEDLINE  
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[PMID]:28669455
[Au] Autor:Mateyak MK; Kinzy TG
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School, Rutgers, the State University of New Jersey, 675 Hoes Lane, Piscataway, NJ 08854, USA.
[Ti] Título:Breaking the Silos of Protein Synthesis.
[So] Source:Trends Biochem Sci;42(8):587-588, 2017 Aug.
[Is] ISSN:0968-0004
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Protein synthesis requires factors that are proposed to enhance discrete steps. Eukaryotic initiation factor eIF5A was initially thought to affect initiation; however, it was later shown to facilitate translation elongation at polyproline. Recent work by Schuller et al. demonstrates that eIF5A facilitates both general elongation and termination in yeast, challenging these steps as silos.
[Mh] Termos MeSH primário: Fatores de Iniciação de Peptídeos/genética
Proteínas de Ligação a RNA/genética
[Mh] Termos MeSH secundário: Biossíntese de Proteínas
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptide Initiation Factors); 0 (RNA-Binding Proteins); 0 (Saccharomyces cerevisiae Proteins)
[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:170704
[St] Status:MEDLINE


  3 / 3590 MEDLINE  
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[PMID]:28646650
[Au] Autor:Tajima Y; Iwakawa HO; Hyodo K; Kaido M; Mise K; Okuno T
[Ad] Endereço:Laboratory of Plant Pathology, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
[Ti] Título:Requirement for eukaryotic translation initiation factors in cap-independent translation differs between bipartite genomic RNAs of red clover necrotic mosaic virus.
[So] Source:Virology;509:152-158, 2017 Sep.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The bipartite genomic RNAs of red clover necrotic mosaic virus (RCNMV) lack a 5' cap and a 3' poly(A) tail. RNA1 encodes viral replication proteins, and RNA2 encodes a movement protein (MP). These proteins are translated in a cap-independent manner. We previously identified two cis-acting RNA elements that cooperatively recruit eukaryotic translation initiation factor (eIF) complex eIF4F or eIFiso4F to RNA1. Such cis-acting RNA elements and host factors have not been identified in RNA2. Here we found that translation of RNA1 was significantly compromised in Arabidopsis thaliana carrying eif4f mutation. RNA1 replicated efficiently in eifiso4f1 mutants, suggesting vigorous translation of the replication proteins from RNA1 in the plants. In contrast, MP accumulation was decreased in eifiso4f1 mutants but not in eif4f mutants. Collectively, these results suggest that RCNMV uses different eIF complexes for translation of its bipartite genomic RNAs, which may contribute to fine-tuning viral gene expression during infection.
[Mh] Termos MeSH primário: Fatores de Iniciação de Peptídeos/metabolismo
Biossíntese de Proteínas
RNA Viral/metabolismo
Tombusviridae/genética
Tombusviridae/fisiologia
Replicação Viral
[Mh] Termos MeSH secundário: Arabidopsis
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptide Initiation Factors); 0 (RNA, Viral)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170721
[Lr] Data última revisão:
170721
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170625
[St] Status:MEDLINE


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[PMID]:28637321
[Au] Autor:Shin BS; Katoh T; Gutierrez E; Kim JR; Suga H; Dever TE
[Ad] Endereço:Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.
[Ti] Título:Amino acid substrates impose polyamine, eIF5A, or hypusine requirement for peptide synthesis.
[So] Source:Nucleic Acids Res;45(14):8392-8402, 2017 Aug 21.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Whereas ribosomes efficiently catalyze peptide bond synthesis by most amino acids, the imino acid proline is a poor substrate for protein synthesis. Previous studies have shown that the translation factor eIF5A and its bacterial ortholog EF-P bind in the E site of the ribosome where they contact the peptidyl-tRNA in the P site and play a critical role in promoting the synthesis of polyproline peptides. Using misacylated Pro-tRNAPhe and Phe-tRNAPro, we show that the imino acid proline and not tRNAPro imposes the primary eIF5A requirement for polyproline synthesis. Though most proline analogs require eIF5A for efficient peptide synthesis, azetidine-2-caboxylic acid, a more flexible four-membered ring derivative of proline, shows relaxed eIF5A dependency, indicating that the structural rigidity of proline might contribute to the requirement for eIF5A. Finally, we examine the interplay between eIF5A and polyamines in promoting translation elongation. We show that eIF5A can obviate the polyamine requirement for general translation elongation, and that this activity is independent of the conserved hypusine modification on eIF5A. Thus, we propose that the body of eIF5A functionally substitutes for polyamines to promote general protein synthesis and that the hypusine modification on eIF5A is critically important for poor substrates like proline.
[Mh] Termos MeSH primário: Aminoácidos/metabolismo
Lisina/análogos & derivados
Biossíntese Peptídica
Fatores de Iniciação de Peptídeos/metabolismo
Poliaminas/metabolismo
Proteínas de Ligação a RNA/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Sequência de Bases
Lisina/metabolismo
Conformação de Ácido Nucleico
Fatores de Iniciação de Peptídeos/química
Peptídeos/metabolismo
Prolina/análogos & derivados
Prolina/química
Prolina/metabolismo
RNA de Transferência de Fenilalanina/química
RNA de Transferência de Fenilalanina/metabolismo
RNA de Transferência de Prolina/química
RNA de Transferência de Prolina/metabolismo
Proteínas de Ligação a RNA/química
Ribossomos/metabolismo
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (Peptide Initiation Factors); 0 (Peptides); 0 (Polyamines); 0 (RNA, Transfer, Phe); 0 (RNA, Transfer, Pro); 0 (RNA-Binding Proteins); 0 (Saccharomyces cerevisiae Proteins); 0 (eukaryotic translation initiation factor 5A); 25191-13-3 (polyproline); 3874VXF092 (hypusine); 9DLQ4CIU6V (Proline); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170623
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx532


  5 / 3590 MEDLINE  
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[PMID]:28605466
[Au] Autor:Gulappa T; Menon B; Menon KMJ
[Ad] Endereço:Department of Obstetrics/Gynecology, University of Michigan Medical School, Ann Arbor, Michigan 48109.
[Ti] Título:LHCGR Expression During Follicle Stimulating Hormone-Induced Follicle Growth Is Negatively Regulated by Eukaryotic Initiation Factor 5A.
[So] Source:Endocrinology;158(8):2672-2679, 2017 Aug 01.
[Is] ISSN:1945-7170
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We have shown that the transient changes in the expression of luteinizing hormone/choriogonadotropin receptor (LHCGR) messenger RNA (mRNA) during the ovarian cycle occurs, at least in part, through a posttranscriptional mechanism involving an LHCGR mRNA-binding protein (LRBP). Eukaryotic initiation factor 5A (eIF5A), an LRBP-interacting protein, participates in this process. eIF5A undergoes hypusination, a unique posttranslational modification that is necessary for its functions. This study examined the role of eIF5A in follicle-stimulating hormone (FSH)-induced LHCGR expression during follicular growth. Treatment of primary cultures of rat granulosa cells with FSH and 17ß-estradiol (E2) showed a time-dependent increase in LHCGR mRNA expression. Conversely, inhibition of endogenous hypusination of eIF5A using N1-guanyl-1,7-diaminoheptane (GC7), a hypusination inhibitor, showed a greater increase in LHCGR mRNA expression over that produced by FSH and E2 alone. Further studies were carried out to determine the mechanism by which inhibition of hypusination of eIF5A causes an increase in LHCGR mRNA expression. Because LHCGR expression is negatively regulated by LRBP, the effect of inhibiting hypusination of eIF5A on LRBP expression was examined. The results showed a decrease in the expression of LRBP mRNA and protein when hypusination of eIF5A was inhibited by GC7. Because LRBP promotes LHCGR mRNA degradation, the results of this study support the notion that by inhibiting eIF5A hypusination, FSH reduces the expression of LRBP. This increases LHCGR mRNA expression by abrogating the inhibitory action of LRBP.
[Mh] Termos MeSH primário: Hormônio Foliculoestimulante/farmacologia
Fatores de Iniciação de Peptídeos/metabolismo
Proteínas de Ligação a RNA/metabolismo
Receptores do LH/metabolismo
[Mh] Termos MeSH secundário: Animais
Feminino
Regulação da Expressão Gênica/fisiologia
Células da Granulosa/fisiologia
Fatores de Iniciação de Peptídeos/genética
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Proteínas de Ligação a RNA/genética
Ratos
Ratos Sprague-Dawley
Receptores do LH/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (LHCGR protein, rat); 0 (Peptide Initiation Factors); 0 (RNA, Messenger); 0 (RNA-Binding Proteins); 0 (Receptors, LH); 0 (eukaryotic translation initiation factor 5A); 9002-68-0 (Follicle Stimulating Hormone)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170613
[St] Status:MEDLINE
[do] DOI:10.1210/en.2017-00113


  6 / 3590 MEDLINE  
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[PMID]:28549188
[Au] Autor:Pelechano V; Alepuz P
[Ad] Endereço:SciLifeLab, Department of Microbiology, Tumor and Cell Biology. Karolinska Institutet, P-Box 1031. 171 21 Solna, Sweden.
[Ti] Título:eIF5A facilitates translation termination globally and promotes the elongation of many non polyproline-specific tripeptide sequences.
[So] Source:Nucleic Acids Res;45(12):7326-7338, 2017 Jul 07.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:eIF5A is an essential protein involved in protein synthesis, cell proliferation and animal development. High eIF5A expression is observed in many tumor types and has been linked to cancer metastasis. Recent studies have shown that eIF5A facilitates the translation elongation of stretches of consecutive prolines. Activated eIF5A binds to the empty E-site of stalled ribosomes, where it is thought to interact with the peptidyl-tRNA situated at the P-site. Here, we report a genome-wide analysis of ribosome stalling in Saccharomyces cerevisiae eIF5A depleted cells using 5Pseq. We confirm that, in the absence of eIF5A, ribosomes stall at proline stretches, and extend previous studies by identifying eIF5A-dependent ribosome pauses at termination and at >200 tripeptide motifs. We show that presence of proline, glycine and charged amino acids at the peptidyl transferase center and at the beginning of the peptide exit tunnel arrest ribosomes in eIF5A-depleted cells. Lack of eIF5A also renders ribosome accumulation at the stop codons. Our data indicate specific protein functional groups under the control of eIF5A, including ER-coupled translation and GTPases in yeast and cytoskeleton organization, collagen metabolism and cell differentiation in humans. Our results support a broad mRNA-specific role of eIF5A in translation and identify the conserved motifs that affect translation elongation from yeast to humans.
[Mh] Termos MeSH primário: Genoma Fúngico
Elongação Traducional da Cadeia Peptídica
Fatores de Iniciação de Peptídeos/genética
Proteínas de Ligação a RNA/genética
Ribossomos/genética
Saccharomyces cerevisiae/genética
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Sítios de Ligação
GTP Fosfo-Hidrolases/genética
GTP Fosfo-Hidrolases/metabolismo
Regulação Fúngica da Expressão Gênica
Seres Humanos
Interações Hidrofóbicas e Hidrofílicas
Fatores de Iniciação de Peptídeos/metabolismo
Prolina/metabolismo
Ligação Proteica
Proteínas de Ligação a RNA/metabolismo
Ribossomos/metabolismo
Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptide Initiation Factors); 0 (RNA-Binding Proteins); 0 (eukaryotic translation initiation factor 5A); 9DLQ4CIU6V (Proline); EC 3.6.1.- (GTP Phosphohydrolases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170527
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx479


  7 / 3590 MEDLINE  
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[PMID]:28441530
[Au] Autor:Ma X; Zhu X; Han Y; Story B; Do T; Song X; Wang S; Zhang Y; Blanchette M; Gogol M; Hall K; Peak A; Anoja P; Xie T
[Ad] Endereço:Stowers Institute for Medical Research, 1000 East 50th Street, Kansas City, MO 64110, USA; Department of Cell Biology and Anatomy, University of Kansas Medical Center, Kansas City, KS 66160, USA.
[Ti] Título:Aubergine Controls Germline Stem Cell Self-Renewal and Progeny Differentiation via Distinct Mechanisms.
[So] Source:Dev Cell;41(2):157-169.e5, 2017 Apr 24.
[Is] ISSN:1878-1551
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Piwi family protein Aubergine (Aub) maintains genome integrity in late germ cells of the Drosophila ovary through Piwi-associated RNA-mediated repression of transposon activities. Although it is highly expressed in germline stem cells (GSCs) and early progeny, it remains unclear whether it plays any roles in early GSC lineage development. Here we report that Aub promotes GSC self-renewal and GSC progeny differentiation. RNA-iCLIP results show that Aub binds the mRNAs encoding self-renewal and differentiation factors in cultured GSCs. Aub controls GSC self-renewal by preventing DNA-damage-induced Chk2 activation and by translationally controlling the expression of self-renewal factors. It promotes GSC progeny differentiation by translationally controlling the expression of differentiation factors, including Bam. Therefore, this study reveals a function of Aub in GSCs and their progeny, which promotes translation of self-renewal and differentiation factors by directly binding to its target mRNAs and interacting with translational initiation factors.
[Mh] Termos MeSH primário: Divisão Celular Assimétrica/fisiologia
Diferenciação Celular/fisiologia
Autorrenovação Celular/fisiologia
Proteínas de Drosophila/metabolismo
Drosophila melanogaster/metabolismo
Células Germinativas/metabolismo
Fatores de Iniciação de Peptídeos/metabolismo
Células-Tronco/citologia
[Mh] Termos MeSH secundário: Animais
Quinase do Ponto de Checagem 2/metabolismo
Drosophila melanogaster/citologia
Feminino
Ovário/citologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (Peptide Initiation Factors); 0 (aubergine protein, Drosophila); EC 2.7.1.11 (Checkpoint Kinase 2); EC 2.7.11.1 (lok protein, Drosophila)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170915
[Lr] Data última revisão:
170915
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170426
[St] Status:MEDLINE


  8 / 3590 MEDLINE  
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[PMID]:28392174
[Au] Autor:Schuller AP; Wu CC; Dever TE; Buskirk AR; Green R
[Ad] Endereço:Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
[Ti] Título:eIF5A Functions Globally in Translation Elongation and Termination.
[So] Source:Mol Cell;66(2):194-205.e5, 2017 Apr 20.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The eukaryotic translation factor eIF5A, originally identified as an initiation factor, was later shown to promote translation elongation of iterated proline sequences. Using a combination of ribosome profiling and in vitro biochemistry, we report a much broader role for eIF5A in elongation and uncover a critical function for eIF5A in termination. Ribosome profiling of an eIF5A-depleted strain reveals a global elongation defect, with abundant ribosomes stalling at many sequences, not limited to proline stretches. Our data also show ribosome accumulation at stop codons and in the 3' UTR, suggesting a global defect in termination in the absence of eIF5A. Using an in vitro reconstituted translation system, we find that eIF5A strongly promotes the translation of the stalling sequences identified by profiling and increases the rate of peptidyl-tRNA hydrolysis more than 17-fold. We conclude that eIF5A functions broadly in elongation and termination, rationalizing its high cellular abundance and essential nature.
[Mh] Termos MeSH primário: Elongação Traducional da Cadeia Peptídica
Terminação Traducional da Cadeia Peptídica
Fatores de Iniciação de Peptídeos/metabolismo
Proteínas de Ligação a RNA/metabolismo
Ribossomos/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas
Motivos de Aminoácidos
Códon de Terminação
Perfilação da Expressão Gênica/métodos
Hidrólise
Cinética
Fatores de Iniciação de Peptídeos/genética
Fatores de Terminação de Peptídeos/genética
Fatores de Terminação de Peptídeos/metabolismo
Peptídeos/metabolismo
Peptidil Transferases/genética
Peptidil Transferases/metabolismo
RNA Fúngico/genética
RNA Fúngico/metabolismo
Aminoacil-RNA de Transferência/genética
Aminoacil-RNA de Transferência/metabolismo
Proteínas de Ligação a RNA/genética
Ribossomos/genética
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (Codon, Terminator); 0 (Peptide Initiation Factors); 0 (Peptide Termination Factors); 0 (Peptides); 0 (RNA, Fungal); 0 (RNA, Transfer, Amino Acyl); 0 (RNA-Binding Proteins); 0 (SUP45 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (eukaryotic translation initiation factor 5A); 0 (tRNA, peptidyl-); 25191-13-3 (polyproline); EC 2.3.2.12 (Peptidyl Transferases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170908
[Lr] Data última revisão:
170908
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170411
[St] Status:MEDLINE


  9 / 3590 MEDLINE  
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[PMID]:28385532
[Au] Autor:Antony A C; Alone PV
[Ad] Endereço:School of Biological Sciences, National Institute of Science Education and Research Bhubaneswar, Constituent Institutes of Homi Bhabha National Institute (HBNI), P.O Jatni, Khurda 752050 India.
[Ti] Título:Defect in the GTPase activating protein (GAP) function of eIF5 causes repression of GCN4 translation.
[So] Source:Biochem Biophys Res Commun;486(4):1110-1115, 2017 May 13.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In eukaryotes, the eIF5 protein plays an important role in translation start site selection by providing the GAP (GTPase activating protein) function. However, in yeast translation initiation fidelity defective eIF5 mutant causes preferential utilization of UUG as initiation codon and is termed as Suppressor of initiation codon (Sui ) phenotype due to its hyper GTPase activity. The eIF5 mutant dominantly represses GCN4 expression and confers sensitivity to 3-Amino-1,2,4-Trizole (3AT) induced starvation. The down-regulation of the GCN4 expression (Gcn phenotype) in the eIF5 mutant was not because of leaky scanning defects; rather was due to the utilization of upUUG initiation codons at the 5' regulatory region present between uORF1 and the main GCN4 ORF.
[Mh] Termos MeSH primário: Fatores de Transcrição de Zíper de Leucina Básica/genética
Repressão Epigenética/genética
Proteínas Ativadoras de GTPase/genética
Regulação da Expressão Gênica/genética
Fatores de Iniciação de Peptídeos/genética
Biossíntese de Proteínas/genética
Proteínas de Ligação a RNA/genética
Proteínas de Saccharomyces cerevisiae/genética
[Mh] Termos MeSH secundário: Códon/genética
Mutação/genética
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Basic-Leucine Zipper Transcription Factors); 0 (Codon); 0 (GCN4 protein, S cerevisiae); 0 (GTPase-Activating Proteins); 0 (Peptide Initiation Factors); 0 (RNA-Binding Proteins); 0 (Saccharomyces cerevisiae Proteins); 0 (eukaryotic translation initiation factor 5A)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170612
[Lr] Data última revisão:
170612
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170408
[St] Status:MEDLINE


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[PMID]:28381547
[Au] Autor:Strnadel J; Choi S; Fujimura K; Wang H; Zhang W; Wyse M; Wright T; Gross E; Peinado C; Park HW; Bui J; Kelber J; Bouvet M; Guan KL; Klemke RL
[Ad] Endereço:Department of Pathology, University of California, San Diego, La Jolla, California.
[Ti] Título:eIF5A-PEAK1 Signaling Regulates YAP1/TAZ Protein Expression and Pancreatic Cancer Cell Growth.
[So] Source:Cancer Res;77(8):1997-2007, 2017 Apr 15.
[Is] ISSN:1538-7445
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In pancreatic ductal adenocarcinoma (PDAC), mutant KRAS stimulates the translation initiation factor eIF5A and upregulates the focal adhesion kinase PEAK1, which transmits integrin and growth factor signals mediated by the tumor microenvironment. Although eIF5A-PEAK1 signaling contributes to multiple aggressive cancer cell phenotypes, the downstream signaling processes that mediate these responses are uncharacterized. Through proteomics and informatic analyses of PEAK1-depleted PDAC cells, we defined protein translation, cytoskeleton organization, and cell-cycle regulatory pathways as major pathways controlled by PEAK1. Biochemical and functional studies revealed that the transcription factors YAP1 and TAZ are key targets of eIF5A-PEAK1 signaling. YAP1/TAZ coimmunoprecipitated with PEAK1. Interfering with eIF5A-PEAK1 signaling in PDAC cells inhibited YAP/TAZ protein expression, decreasing expression of stem cell-associated transcription factors (STF) including Oct4, Nanog, c-Myc, and TEAD, thereby decreasing three-dimensional (3D) tumor sphere growth. Conversely, amplified eIF5A-PEAK1 signaling increased YAP1/TAZ expression, increasing expression of STF and enhancing 3D tumor sphere growth. Informatic interrogation of mRNA sequence databases revealed upregulation of the eIF5A-PEAK1-YAP1-TEAD signaling module in PDAC patients. Taken together, our findings indicate that eIF5A-PEAK1-YAP signaling contributes to PDAC development by regulating an STF program associated with increased tumorigenicity. .
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Carcinoma Ductal Pancreático/metabolismo
Neoplasias Pancreáticas/metabolismo
Fatores de Iniciação de Peptídeos/metabolismo
Fosfoproteínas/metabolismo
Proteínas Tirosina Quinases/metabolismo
Proteínas de Ligação a RNA/metabolismo
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/biossíntese
Proteínas Adaptadoras de Transdução de Sinal/genética
Carcinoma Ductal Pancreático/genética
Carcinoma Ductal Pancreático/patologia
Ciclo Celular/fisiologia
Linhagem Celular Tumoral
Citoesqueleto/metabolismo
Seres Humanos
Células-Tronco Neoplásicas/metabolismo
Células-Tronco Neoplásicas/patologia
Fator 3 de Transcrição de Octâmero/biossíntese
Fator 3 de Transcrição de Octâmero/genética
Neoplasias Pancreáticas/genética
Neoplasias Pancreáticas/patologia
Fatores de Iniciação de Peptídeos/biossíntese
Fatores de Iniciação de Peptídeos/genética
Fosfoproteínas/biossíntese
Fosfoproteínas/genética
Proteínas Tirosina Quinases/biossíntese
Proteínas Tirosina Quinases/genética
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Proteínas de Ligação a RNA/biossíntese
Proteínas de Ligação a RNA/genética
Transdução de Sinais
Fatores de Transcrição/biossíntese
Fatores de Transcrição/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Octamer Transcription Factor-3); 0 (POU5F1 protein, human); 0 (Peptide Initiation Factors); 0 (Phosphoproteins); 0 (RNA, Messenger); 0 (RNA-Binding Proteins); 0 (TAZ protein, human); 0 (Transcription Factors); 0 (YAP1 (Yes-associated) protein, human); 0 (eukaryotic translation initiation factor 5A); EC 2.7.10.1 (PEAK1 protein, human); EC 2.7.10.1 (Protein-Tyrosine Kinases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170510
[Lr] Data última revisão:
170510
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170407
[St] Status:MEDLINE
[do] DOI:10.1158/0008-5472.CAN-16-2594



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