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[PMID]: 29254296 [Au] Autor: Liu SY; Zhang L; Zhang Y; Zhen Y; Wu YF [Ad] Endereço: Department of Neurosurgery, Second Hospital, Jilin University, Changchun, China. [Ti] Título: Bioinformatic analysis of pivotal genes associated with septic shock. [So] Source: J Biol Regul Homeost Agents;31(4):935-941, 2017 Oct-Dec. [Is] ISSN: 0393-974X [Cp] País de publicação: Italy [La] Idioma: eng [Ab] Resumo: We aimed to identify important genes associated with septic shock and then explore the possibly significant mechanisms of this disease. We downloaded GSE26440 expression data of samples from 98 children with septic shock and 32 normal controls from the Gene Expression Omnibus (GEO) database. Differentially expressed genes (DEGs) in samples from patients with septic shock were analyzed in comparison with those in samples from normal controls using a limma package. Functional enrichment analysis for DEGs was performed using DAVID, and a protein–protein interaction (PPI) network was constructed. Upstream transcription factors for DEGs were predicted using the CHIPBase database, and a transcriptional regulation network was constructed. A total of 383 significantly DEGs, including 141 downregulated and 242 upregulated genes, were obtained in the sepsis shock group compared with the normal group. The top five nodes in the PPI network were lysine (K)-specific demethylase 6B (KDM6B), histone deacetylase 2 (HDAC2), V-Myc avian myelocytomatosis viral oncogene homolog (MYC), heat-shock protein 90 kDa alpha (cytosolic), class B member 1 (HSP90AB1), and poly (A)-binding protein, cytoplasmic 1 (PABPC1). Nuclear factor kappa-light-chain-enhancer of activated B cells (NFkB) was the transcription factor targeted by most genes, and it regulated the expression of KDM6B, HDAC2, MYC, HSP90AB1, and PABPC1. In conclusion, KDM6B, HDAC2, MYC, HSP90AB1, and PABPC1 may play important roles in the development of septic shock. Furthermore, NFκB may be involved in septic shock by regulating the expression of KDM6B, HDAC2, MYC, HSP90AB1, and PABPC1. [Mh] Termos MeSH primário: Biologia Computacional/métodos Redes Reguladoras de Genes NF-kappa B/genética Choque Séptico/genética Transcriptoma [Mh] Termos MeSH secundário: Estudos de Casos e Controles Criança Pré-Escolar Feminino Perfilação da Expressão Gênica Regulação da Expressão Gênica Proteínas de Choque Térmico HSP90/genética Proteínas de Choque Térmico HSP90/metabolismo Histona Desacetilase 2/genética Histona Desacetilase 2/metabolismo Seres Humanos Histona Desmetilases com o Domínio Jumonji/genética Histona Desmetilases com o Domínio Jumonji/metabolismo Masculino NF-kappa B/metabolismo Proteína I de Ligação a Poli(A)/genética Proteína I de Ligação a Poli(A)/metabolismo Mapeamento de Interação de Proteínas Proteínas Proto-Oncogênicas c-myc/genética Proteínas Proto-Oncogênicas c-myc/metabolismo Choque Séptico/metabolismo Choque Séptico/patologia [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (HSP90 Heat-Shock Proteins); 0 (HSP90AB1 protein, human); 0 (MYC protein, human); 0 (NF-kappa B); 0 (Poly(A)-Binding Protein I); 0 (Proto-Oncogene Proteins c-myc); EC 1.14.11.- (Jumonji Domain-Containing Histone Demethylases); EC 1.14.11.- (KDM6B protein, human); EC 3.5.1.98 (HDAC2 protein, human); EC 3.5.1.98 (Histone Deacetylase 2) [Em] Mês de entrada: 1802 [Cu] Atualização por classe: 180222 [Lr] Data última revisão: 180222 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 171220 [St] Status: MEDLINE

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[PMID]: 28977530 [Au] Autor: Banerjee A; Vest KE; Pavlath GK; Corbett AH [Ad] Endereço: Department of Biology, Emory University, Atlanta, GA 30322, USA. [Ti] Título: Nuclear poly(A) binding protein 1 (PABPN1) and Matrin3 interact in muscle cells and regulate RNA processing. [So] Source: Nucleic Acids Res;45(18):10706-10725, 2017 Oct 13. [Is] ISSN: 1362-4962 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: The polyadenylate binding protein 1 (PABPN1) is a ubiquitously expressed RNA binding protein vital for multiple steps in RNA metabolism. Although PABPN1 plays a critical role in the regulation of RNA processing, mutation of the gene encoding this ubiquitously expressed RNA binding protein causes a specific form of muscular dystrophy termed oculopharyngeal muscular dystrophy (OPMD). Despite the tissue-specific pathology that occurs in this disease, only recently have studies of PABPN1 begun to explore the role of this protein in skeletal muscle. We have used co-immunoprecipitation and mass spectrometry to identify proteins that interact with PABPN1 in mouse skeletal muscles. Among the interacting proteins we identified Matrin 3 (MATR3) as a novel protein interactor of PABPN1. The MATR3 gene is mutated in a form of distal myopathy and amyotrophic lateral sclerosis (ALS). We demonstrate, that like PABPN1, MATR3 is critical for myogenesis. Furthermore, MATR3 controls critical aspects of RNA processing including alternative polyadenylation and intron retention. We provide evidence that MATR3 also binds and regulates the levels of long non-coding RNA (lncRNA) Neat1 and together with PABPN1 is required for normal paraspeckle function. We demonstrate that PABPN1 and MATR3 are required for paraspeckles, as well as for adenosine to inosine (A to I) RNA editing of Ctn RNA in muscle cells. We provide a functional link between PABPN1 and MATR3 through regulation of a common lncRNA target with downstream impact on paraspeckle morphology and function. We extend our analysis to a mouse model of OPMD and demonstrate altered paraspeckle morphology in the presence of endogenous levels of alanine-expanded PABPN1. In this study, we report protein-binding partners of PABPN1, which could provide insight into novel functions of PABPN1 in skeletal muscle and identify proteins that could be sequestered with alanine-expanded PABPN1 in the nuclear aggregates found in OPMD. [Mh] Termos MeSH primário: Músculo Esquelético/metabolismo Proteínas Associadas à Matriz Nuclear/metabolismo Proteína I de Ligação a Poli(A)/metabolismo Processamento Pós-Transcricional do RNA Proteínas de Ligação a RNA/metabolismo [Mh] Termos MeSH secundário: Animais Células Cultivadas Seres Humanos Camundongos Endogâmicos C57BL Desenvolvimento Muscular Proteína I de Ligação a Poli(A)/fisiologia [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Nuclear Matrix-Associated Proteins); 0 (PABPN1 protein, human); 0 (PABPN1 protein, mouse); 0 (Poly(A)-Binding Protein I); 0 (RNA-Binding Proteins); 0 (matrin-3 protein, mouse) [Em] Mês de entrada: 1711 [Cu] Atualização por classe: 171111 [Lr] Data última revisão: 171111 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 171005 [St] Status: MEDLINE [do] DOI: 10.1093/nar/gkx786

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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]: 28807897 [Au] Autor: Bansal D; Kulkarni J; Nadahalli K; Lakshmanan V; Krishna S; Sasidharan V; Geo J; Dilipkumar S; Pasricha R; Gulyani A; Raghavan S; Palakodeti D [Ad] Endereço: Institute for Stem Cell Biology and Regenerative Medicine, GKVK PO, Bellary Road, Bangalore 560065, India. [Ti] Título: Cytoplasmic poly (A)-binding protein critically regulates epidermal maintenance and turnover in the planarian . [So] Source: Development;144(17):3066-3079, 2017 09 01. [Is] ISSN: 1477-9129 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: Identifying key cellular events that facilitate stem cell function and tissue organization is crucial for understanding the process of regeneration. Planarians are powerful model system to study regeneration and stem cell (neoblast) function. Here, using planaria, we show that the initial events of regeneration, such as epithelialization and epidermal organization are critically regulated by a novel cytoplasmic poly A-binding protein, SMED-PABPC2. Knockdown leads to defects in epidermal lineage specification, disorganization of epidermis and ECM, and deregulated wound healing, resulting in the selective failure of neoblast proliferation near the wound region. Polysome profiling suggests that epidermal lineage transcripts, including , are translationally regulated by SMED-PABPC2 Together, our results uncover a novel role for SMED-PABPC2 in the maintenance of epidermal and ECM integrity, critical for wound healing and subsequent processes for regeneration. [Mh] Termos MeSH primário: Citoplasma/metabolismo Epiderme/metabolismo Planárias/metabolismo Proteína I de Ligação a Poli(A)/metabolismo [Mh] Termos MeSH secundário: Animais Linhagem da Célula Proliferação Celular Epitélio/metabolismo Matriz Extracelular/metabolismo Técnicas de Silenciamento de Genes Homeostase Modelos Biológicos Planárias/genética RNA Mensageiro/genética RNA Mensageiro/metabolismo Regeneração Cicatrização [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Poly(A)-Binding Protein I); 0 (RNA, Messenger) [Em] Mês de entrada: 1710 [Cu] Atualização por classe: 171126 [Lr] Data última revisão: 171126 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170816 [St] Status: MEDLINE [do] DOI: 10.1242/dev.152942

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[PMID]: 28733330 [Au] Autor: Copsey AC; Cooper S; Parker R; Lineham E; Lapworth C; Jallad D; Sweet S; Morley SJ [Ad] Endereço: Department of Biochemistry, School of Life Sciences, University of Sussex, Brighton BN1 6SE, U.K. [Ti] Título: The helicase, DDX3X, interacts with poly(A)-binding protein 1 (PABP1) and caprin-1 at the leading edge of migrating fibroblasts and is required for efficient cell spreading. [So] Source: Biochem J;474(18):3109-3120, 2017 Aug 30. [Is] ISSN: 1470-8728 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: DDX3X, a helicase, can interact directly with mRNA and translation initiation factors, regulating the selective translation of mRNAs that contain a structured 5' untranslated region. This activity modulates the expression of mRNAs controlling cell cycle progression and mRNAs regulating actin dynamics, contributing to cell adhesion and motility. Previously, we have shown that ribosomes and translation initiation factors localise to the leading edge of migrating fibroblasts in loci enriched with actively translating ribosomes, thereby promoting steady-state levels of ArpC2 and Rac1 proteins at the leading edge of cells during spreading. As DDX3X can regulate Rac1 levels, cell motility and metastasis, we have examined DDX3X protein interactions and localisation using many complementary approaches. We now show that DDX3X can physically interact and co-localise with poly(A)-binding protein 1 and caprin-1 at the leading edge of spreading cells. Furthermore, as depletion of DDX3X leads to decreased cell motility, this provides a functional link between DDX3X, caprin-1 and initiation factors at the leading edge of migrating cells to promote cell migration and spreading. [Mh] Termos MeSH primário: Proteínas de Ciclo Celular/metabolismo RNA Helicases DEAD-box/metabolismo Pulmão/metabolismo Proteína I de Ligação a Poli(A)/metabolismo Pseudópodes/metabolismo RNA Mensageiro/metabolismo Mucosa Respiratória/metabolismo [Mh] Termos MeSH secundário: Western Blotting Sistemas CRISPR-Cas Linhagem Celular Movimento Celular Cromatografia de Afinidade RNA Helicases DEAD-box/genética Corantes Fluorescentes/química Seres Humanos Imunoprecipitação Pulmão/citologia Pulmão/enzimologia Microscopia Confocal Microscopia de Fluorescência Mapeamento de Peptídeos Transporte Proteico Proteômica/métodos Pseudópodes/enzimologia Mucosa Respiratória/citologia Mucosa Respiratória/enzimologia [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (CAPRIN1 protein, human); 0 (Cell Cycle Proteins); 0 (Fluorescent Dyes); 0 (Poly(A)-Binding Protein I); 0 (RNA, Messenger); EC 3.6.1.- (DDX3X protein, human); EC 3.6.4.13 (DEAD-box RNA Helicases) [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: 170723 [St] Status: MEDLINE [do] DOI: 10.1042/BCJ20170354

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[PMID]: 28611064 [Au] Autor: Peng Y; Yuan J; Zhang Z; Chang X [Ad] Endereço: From the Key Laboratory of Stem Cell Biology, Institute of Health Sciences, Shanghai Institutes for Biological Sciences and Shanghai Jiao Tong University School of Medicine, University of Chinese Academy of Sciences, Chinese Academy of Sciences, Shanghai 200031, China and. [Ti] Título: Cytoplasmic poly(A)-binding protein 1 (PABPC1) interacts with the RNA-binding protein hnRNPLL and thereby regulates immunoglobulin secretion in plasma cells. [So] Source: J Biol Chem;292(29):12285-12295, 2017 Jul 21. [Is] ISSN: 1083-351X [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Increasing evidence indicates that alternative processing of mRNA, including alternative splicing, 3' alternative polyadenylation, and regulation of mRNA stability/translation, represents a major mechanism contributing to protein diversification. For example, in alternative polyadenylation, the 3' end of the immunoglobulin heavy chain mRNA is processed during B cell differentiation, and this processing involves RNA-binding proteins. hnRNPLL (heterogeneous nuclear ribonucleoprotein L-like protein) is an RNA-binding protein expressed in terminally differentiated lymphocytes, such as memory T cells and plasma cells. hnRNPLL regulates various processes of RNA metabolism, including alternative pre-mRNA splicing and RNA stability. In plasma cells, hnRNPLL also regulates the transition from the membrane isoform of the immunoglobulin heavy-chain (mIgH) to the secreted isoform (sIgH), but the precise mechanism remains to be identified. In this study, we report that hnRNPLL specifically associates with cytoplasmic PABPC1 (poly(A)-binding protein 1) in both T cells and plasma cells. We found that although PABPC1 is not required for the alternative splicing of CD45, a primary target of hnRNPLL in lymphocytes, PABPC1 does promote the binding of hnRNPLL to the immunoglobulin mRNA and regulates switching from mIgH to sIgH in plasma cells. Given the recently identified role of PABPC1 in mRNA alternative polyadenylation, our findings suggest that PABPC1 recruits hnRNPLL to the 3'-end of RNA and regulates the transition from membrane Ig to secreted Ig through mRNA alternative polyadenylation. In conclusion, our study has revealed a mechanism that regulates immunoglobulin secretion in B cells via cooperation between a plasma cell-specific RBP (hnRNPLL) and a universally expressed RBP (PABPC1). [Mh] Termos MeSH primário: Citoplasma/metabolismo Ribonucleoproteínas Nucleares Heterogêneas/metabolismo Cadeias Pesadas de Imunoglobulinas/metabolismo Plasmócitos/metabolismo Proteína I de Ligação a Poli(A)/metabolismo Poliadenilação RNA Mensageiro/metabolismo [Mh] Termos MeSH secundário: Animais Células Cultivadas Ribonucleoproteínas Nucleares Heterogêneas/química Ribonucleoproteínas Nucleares Heterogêneas/genética Seres Humanos Switching de Imunoglobulina Cadeias Pesadas de Imunoglobulinas/genética Imunoprecipitação Células Jurkat Ativação Linfocitária Camundongos Camundongos Endogâmicos C57BL Plasmócitos/citologia Plasmócitos/imunologia Plasmócitos/secreção Proteína I de Ligação a Poli(A)/antagonistas & inibidores Proteína I de Ligação a Poli(A)/química Proteína I de Ligação a Poli(A)/genética Domínios e Motivos de Interação entre Proteínas Interferência de RNA Baço/citologia Baço/imunologia Linfócitos T/citologia Linfócitos T/imunologia Linfócitos T/metabolismo Linfócitos T/secreção [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Heterogeneous-Nuclear Ribonucleoproteins); 0 (Immunoglobulin Heavy Chains); 0 (Poly(A)-Binding Protein I); 0 (RNA, Messenger); 0 (hnRNPLL protein, mouse) [Em] Mês de entrada: 1708 [Cu] Atualização por classe: 170808 [Lr] Data última revisão: 170808 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170615 [St] Status: MEDLINE [do] DOI: 10.1074/jbc.M117.794834

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[PMID]: 28590779 [Au] Autor: Braverman I; Blumen SC; Newman H; Rizel L; Khayat M; Hanna R; St Guily JL; Tiosano B; Ben-Yosef T [Ad] Endereço: 1 Otolaryngology, Head and Neck Surgery Unit, Hillel Yaffe Medical Center , Hadera, Israel . [Ti] Título: Oculopharyngeal Muscular Dystrophy and Inherited Retinal Dystrophy in Bukhara Jews Due to Linked Mutations in the PABPN1 and NRL Genes. [So] Source: Genet Test Mol Biomarkers;21(7):450-453, 2017 Jul. [Is] ISSN: 1945-0257 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: AIM: We have previously described two unrelated Bukhara Jews (BJs) with a combination of oculopharyngeal muscular dystrophy (OPMD) and inherited retinal dystrophy (IRD), because of mutations in two linked genes: PABPN1 and NRL. Here we investigated the prevalence of the NRL mutation among BJs with OPMD. MATERIALS AND METHODS: PABPN1 and NRL mutation testing were performed by polymerase chain reaction amplification and direct sequencing on two cohorts of Bukhara Jewish patients: OPMD patients (with or without IRD) and IRD patients (without OPMD). RESULTS: Of 24 unrelated chromosomes from Bukhara Jewish OPMD patients, 19 (79%) harbored the NRL mutation. In contrast, the NRL mutation was not detected in Bukhara Jewish patients diagnosed with IRD but without OPMD. CONCLUSIONS: Our findings provide an explanation for the reoccurrence of IRD in Bukhara Jewish OPMD homozygotes. Moreover, they indicate that Bukhara Jewish OPMD patients are at high risk for carrying the NRL mutation, and should be offered appropriate genetic counseling and testing. [Mh] Termos MeSH primário: Fatores de Transcrição de Zíper de Leucina Básica/genética Proteínas do Olho/genética Proteína I de Ligação a Poli(A)/genética [Mh] Termos MeSH secundário: Adulto Idoso Fatores de Transcrição de Zíper de Leucina Básica/metabolismo Estudos de Coortes Grupos Étnicos/genética Proteínas do Olho/metabolismo Feminino Homozigoto Seres Humanos Judeus/genética Masculino Meia-Idade Distrofia Muscular Oculofaríngea/genética Mutação Linhagem Proteína I de Ligação a Poli(A)/metabolismo Distrofias Retinianas/genética [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Basic-Leucine Zipper Transcription Factors); 0 (Eye Proteins); 0 (NRL protein, human); 0 (PABPN1 protein, human); 0 (Poly(A)-Binding Protein I) [Em] Mês de entrada: 1709 [Cu] Atualização por classe: 171106 [Lr] Data última revisão: 171106 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170608 [St] Status: MEDLINE [do] DOI: 10.1089/gtmb.2016.0429

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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]: 28096519 [Au] Autor: Kühn U; Buschmann J; Wahle E [Ad] Endereço: Institute of Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, 06099 Halle, Germany. [Ti] Título: The nuclear poly(A) binding protein of mammals, but not of fission yeast, participates in mRNA polyadenylation. [So] Source: RNA;23(4):473-482, 2017 Apr. [Is] ISSN: 1469-9001 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: The nuclear poly(A) binding protein (PABPN1) has been suggested, on the basis of biochemical evidence, to play a role in mRNA polyadenylation by strongly increasing the processivity of poly(A) polymerase. While experiments in metazoans have tended to support such a role, the results were not unequivocal, and genetic data show that the ortholog of PABPN1, Pab2, is not involved in mRNA polyadenylation. The specific model in which PABPN1 increases the rate of poly(A) tail elongation has never been examined in vivo. Here, we have used 4-thiouridine pulse-labeling to examine the lengths of newly synthesized poly(A) tails in human cells. Knockdown of PABPN1 strongly reduced the synthesis of full-length tails of ∼250 nucleotides, as predicted from biochemical data. We have also purified Pab2 and the poly(A) polymerase, Pla1, and examined their in vitro activities. Whereas PABPN1 strongly increases the activity of its cognate poly(A) polymerase in vitro, Pab2 was unable to stimulate Pla1 to any significant extent. Thus, in vitro and in vivo data are consistent in supporting a role of PABPN1 but not Pab2 in the polyadenylation of mRNA precursors. [Mh] Termos MeSH primário: Poli A/genética Proteína I de Ligação a Poli(A)/genética Proteínas de Ligação a Poli(A)/genética Polinucleotídeo Adenililtransferase/genética Precursores de RNA/genética Proteínas de Schizosaccharomyces pombe/genética Schizosaccharomyces/genética [Mh] Termos MeSH secundário: Clonagem Molecular Escherichia coli/genética Escherichia coli/metabolismo Expressão Gênica Regulação da Expressão Gênica Células HEK293 Seres Humanos Isoenzimas/genética Isoenzimas/metabolismo Poli A/biossíntese Proteína I de Ligação a Poli(A)/metabolismo Proteínas de Ligação a Poli(A)/metabolismo Poliadenilação Polinucleotídeo Adenililtransferase/metabolismo Precursores de RNA/metabolismo RNA Mensageiro/genética RNA Mensageiro/metabolismo Proteínas Recombinantes/genética Proteínas Recombinantes/metabolismo Schizosaccharomyces/metabolismo Proteínas de Schizosaccharomyces pombe/metabolismo Especificidade da Espécie Especificidade por Substrato [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Isoenzymes); 0 (PABPN1 protein, human); 0 (Pab2 protein, S pombe); 0 (Poly(A)-Binding Protein I); 0 (Poly(A)-Binding Proteins); 0 (RNA Precursors); 0 (RNA, Messenger); 0 (Recombinant Proteins); 0 (Schizosaccharomyces pombe Proteins); 24937-83-5 (Poly A); EC 2.7.7.19 (Polynucleotide Adenylyltransferase) [Em] Mês de entrada: 1709 [Cu] Atualização por classe: 170906 [Lr] Data última revisão: 170906 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170119 [St] Status: MEDLINE [do] DOI: 10.1261/rna.057026.116

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[PMID]: 28080204 [Au] Autor: Abdelmohsen K; Panda AC; Munk R; Grammatikakis I; Dudekula DB; De S; Kim J; Noh JH; Kim KM; Martindale JL; Gorospe M [Ad] Endereço: a Laboratory of Genetics and Genomics, National Institute on Aging, National Institutes of Health , Baltimore , MD , USA. [Ti] Título: Identification of HuR target circular RNAs uncovers suppression of PABPN1 translation by CircPABPN1. [So] Source: RNA Biol;14(3):361-369, 2017 Mar 04. [Is] ISSN: 1555-8584 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: HuR influences gene expression programs and hence cellular phenotypes by binding to hundreds of coding and noncoding linear RNAs. However, whether HuR binds to circular RNAs (circRNAs) and impacts on their function is unknown. Here, we have identified en masse circRNAs binding HuR in human cervical carcinoma HeLa cells. One of the most prominent HuR target circRNAs was hsa_circ_0031288, renamed CircPABPN1 as it arises from the PABPN1 pre-mRNA. Further analysis revealed that HuR did not influence CircPABPN1 abundance; interestingly, however, high levels of CircPABPN1 suppressed HuR binding to PABPN1 mRNA. Evaluation of PABPN1 mRNA polysomes indicated that PABPN1 translation was modulated positively by HuR and hence negatively by CircPABPN1. We propose that the extensive binding of CircPABPN1 to HuR prevents HuR binding to PABPN1 mRNA and lowers PABPN1 translation, providing the first example of competition between a circRNA and its cognate mRNA for an RBP that affects translation. [Mh] Termos MeSH primário: Proteína Semelhante a ELAV 1/metabolismo Regulação da Expressão Gênica Proteína I de Ligação a Poli(A)/genética Biossíntese de Proteínas RNA/genética RNA/metabolismo [Mh] Termos MeSH secundário: Sequência de Bases Sítios de Ligação Linhagem Celular Tumoral Seres Humanos Modelos Biológicos Ligação Proteica RNA Mensageiro/química RNA Mensageiro/genética RNA Mensageiro/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (ELAV-Like Protein 1); 0 (PABPN1 protein, human); 0 (Poly(A)-Binding Protein I); 0 (RNA, Messenger); 0 (RNA, circular); 63231-63-0 (RNA) [Em] Mês de entrada: 1710 [Cu] Atualização por classe: 171019 [Lr] Data última revisão: 171019 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170113 [St] Status: MEDLINE [do] DOI: 10.1080/15476286.2017.1279788

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