Base de dados : MEDLINE
Pesquisa : D12.776.157.725.813.750 [Categoria DeCS]
Referências encontradas : 1591 [refinar]
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[PMID]:27771350
[Au] Autor:Tratnjek L; Zivin M; Glavan G
[Ad] Endereço:University of Ljubljana, Medical Faculty, Institute of Pathophysiology, Brain Research Laboratory, Zaloska 4, 1000, Ljubljana, Slovenia. Electronic address: larisa.tratnjek@mf.uni-lj.si.
[Ti] Título:Synaptotagmin 7 and SYNCRIP proteins are ubiquitously expressed in the rat brain and co-localize in Purkinje neurons.
[So] Source:J Chem Neuroanat;79:12-21, 2017 Jan.
[Is] ISSN:1873-6300
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Synaptotagmin 7 (SYT7) is ubiquitously expressed calcium sensor, involved in neuronal membrane trafficking. Immunoprecipitation experiments demonstrated that SYT7 interacts with Synaptotagmin-binding, cytoplasmic RNA-interacting protein (SYNCRIP). SYNCRIP is a component of mRNA granules, which are transported to dendrites and are prerequisite for synaptic plasticity. Given the potential significance of SYT7 regulation in processes of neurodegeneration, which are characterized by high level of synaptic vulnerability, we aimed to analyse and compare the distribution of SYT7 and SYNCRIP proteins in the adult rat striatum, hippocampus, cerebral and cerebellar cortex. We investigated the degree of SYT7-SYNCRIP co-localization in order to examine possible functional interaction of these two proteins. We found that SYT7 is abundantly distributed in neuropil of all examined anatomical areas of the brain, most prominently in axons. On the contrary, SYNCRIP had cytoplasmic somatodendritic pattern of expression, which was most prominent in the hippocampus and cerebellum. In the striatum, hippocampus and cerebral cortex SYT7 and SYNCRIP immunofluorescent signals were mutually excluded, thus diminishing the probability for their physiological interaction. In somata of Purkinje neurons in the cerebellar cortex, both SYT7 and SYNCRIP were expressed and partially co-localized suggesting possible functional connection between SYT7 and SYNCRIP proteins in Purkinje neurons.
[Mh] Termos MeSH primário: Química Encefálica
Encéfalo/metabolismo
Ribonucleoproteínas Nucleares Heterogêneas/biossíntese
Células de Purkinje/metabolismo
Sinaptotagminas/biossíntese
[Mh] Termos MeSH secundário: Animais
Expressão Gênica
Ribonucleoproteínas Nucleares Heterogêneas/análise
Ribonucleoproteínas Nucleares Heterogêneas/genética
Masculino
Células de Purkinje/química
Ratos
Ratos Wistar
Sinaptotagminas/análise
Sinaptotagminas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Heterogeneous-Nuclear Ribonucleoproteins); 0 (Syncrip protein, mouse); 0 (Syt7 protein, rat); 134193-27-4 (Synaptotagmins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180207
[Lr] Data última revisão:
180207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161030
[St] Status:MEDLINE


  2 / 1591 MEDLINE  
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[PMID]:27770549
[Au] Autor:Zhang L; Yang Z; Trottier J; Barbier O; Wang L
[Ad] Endereço:Department of Physiology and Neurobiology and Institute for Systems Genomics, University of Connecticut, Storrs, CT.
[Ti] Título:Long noncoding RNA MEG3 induces cholestatic liver injury by interaction with PTBP1 to facilitate shp mRNA decay.
[So] Source:Hepatology;65(2):604-615, 2017 Feb.
[Is] ISSN:1527-3350
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bile acids (BAs) play critical physiological functions in cholesterol homeostasis, and deregulation of BA metabolism causes cholestatic liver injury. The long noncoding RNA maternally expressed gene 3 (MEG3) was recently shown as a potential tumor suppressor; however, its basic hepatic function remains elusive. Using RNA pull-down with biotin-labeled sense or anti-sense MEG 3RNA followed by mass spectrometry, we identified RNA-binding protein polypyrimidine tract-binding protein 1 (PTBP1) as a MEG3 interacting protein and validated their interaction by RNA immunoprecipitation (RIP). Bioinformatics analysis revealed putative binding sites for PTBP1 within the coding region (CDS) of small heterodimer partner (SHP), a key repressor of BA biosynthesis. Forced expression of MEG3 in hepatocellular carcinoma cells guided and facilitated PTBP1 binding to the Shp CDS, resulting in Shp mRNA decay. Transient overexpression of MEG3 RNA in vivo in mouse liver caused rapid Shp mRNA degradation and cholestatic liver injury, which was accompanied by the disruption of BA homeostasis, elevation of liver enzymes, as well as dysregulation of BA synthetic enzymes and metabolic genes. Interestingly, RNA sequencing coupled with quantitative PCR (qPCR) revealed a drastic induction of MEG3 RNA in Shp liver. SHP inhibited MEG3 gene transcription by repressing cAMP response element-binding protein (CREB) transactivation of the MEG3 promoter. In addition, the expression of MEG3 and PTBP1 was activated in human fibrotic and cirrhotic livers. CONCLUSION: MEG3 causes cholestasis by serving as a guide RNA scaffold to recruit PTBP1 to destabilize Shp mRNA. SHP in turn represses CREB-mediated activation of MEG3 expression in a feedback-regulatory fashion. (Hepatology 2017;65:604-615).
[Mh] Termos MeSH primário: Colestase/metabolismo
Ribonucleoproteínas Nucleares Heterogêneas/genética
Fígado/lesões
Proteína de Ligação a Regiões Ricas em Polipirimidinas/genética
Estabilidade de RNA/genética
RNA Longo não Codificante/genética
[Mh] Termos MeSH secundário: Animais
Sítios de Ligação
Células Cultivadas
Colestase/patologia
Modelos Animais de Doenças
Regulação para Baixo
Células Hep G2
Hepatócitos/citologia
Hepatócitos/metabolismo
Seres Humanos
Fígado/patologia
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Regiões Promotoras Genéticas
Distribuição Aleatória
Sensibilidade e Especificidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Heterogeneous-Nuclear Ribonucleoproteins); 0 (MEG3 non-coding RNA, mouse); 0 (Ptbp1 protein, mouse); 0 (RNA, Long Noncoding); 139076-35-0 (Polypyrimidine Tract-Binding Protein)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:180201
[Lr] Data última revisão:
180201
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161023
[St] Status:MEDLINE
[do] DOI:10.1002/hep.28882


  3 / 1591 MEDLINE  
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[PMID]:28936921
[Au] Autor:Marques DS; Grativol J; Alves da Silva Peres R; da Rocha Matos A; Gimba ERP
[Ad] Endereço:1 Programa de Pós Graduação em Ciências Biomédicas (Fisiologia e Farmacologia), Universidade Federal Fluminense, Rio de Janeiro, Brazil.
[Ti] Título:Osteopontin-c isoform levels are associated with SR and hnRNP differential expression in ovarian cancer cell lines.
[So] Source:Tumour Biol;39(9):1010428317725442, 2017 Sep.
[Is] ISSN:1423-0380
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Osteopontin-c splicing isoform activates ovarian cancer progression features. Imbalanced expression of splicing factors from serine/arginine -rich and heterogeneous ribonucleoproteins families has been correlated with the generation of oncogenic splicing isoforms. Our goal was to investigate whether there is any association between the transcriptional patterns of these splicing factors in ovarian cells and osteopontin-c expression levels. We also aimed to investigate the occurrence of these splicing factors binding sites inside osteopontin exon 4 and adjacent introns. To test associations between osteopontin-c and splicing factors expression patterns, we used an in vitro model in which OVCAR-3 cells overexpressing osteopontin-c (OVCAR-3/OPNc ) presented higher transcriptional levels of osteopontin-c than two other ovarian carcinoma cells (TOV-112D, SKOV-3) and ovarian non-tumoral cell lines (IOSE 364 and IOSE 385). The transcriptional levels of osteopontin-c, serine/arginine-rich, and hnRNP factors were evaluated using real-time polymerase chain reaction. Human Splice Finder software was used to search for putative splicing factor binding sites in osteopontin genomic regions. OVCAR-3/OPNc cells presented higher transcriptional levels of hnRNP than serine/arginine-rich when compared to TOV-112D, SKOV-3, and IOSE cells. TOV-112D and SKOV-3 cells also overexpressed hnRNP in relation to serine/arginine-rich transcripts. Putative binding sites for these splicing factors have been predicted on osteopontin exon 4 and their upstream and downstream intronic regions. Our data showed that higher osteopontin-c expression levels are associated with a predominance of hnRNP in relation to serine/arginine-rich transcripts and that osteopontin exon 4 and adjacent intronic sequences contain predicted binding sites for some of these tested splicing factors. In conclusion, differential expression of these splicing factors in ovarian cancer cells could be one of the putative mechanisms leading to aberrant splicing of the osteopontin primary transcript. Future work, aiming to control ovarian cancer progression by downregulating osteopontin-c levels, could include strategies that also regulate heterogeneous ribonucleoproteins and serine/arginine-rich expression levels in order to modulate osteopontin splicing.
[Mh] Termos MeSH primário: Ribonucleoproteínas Nucleares Heterogêneas/genética
Osteopontina/metabolismo
Neoplasias Ovarianas/genética
Fatores de Processamento de Serina-Arginina/genética
[Mh] Termos MeSH secundário: Processamento Alternativo
Linhagem Celular Tumoral
Feminino
Perfilação da Expressão Gênica
Ribonucleoproteínas Nucleares Heterogêneas/metabolismo
Seres Humanos
Neoplasias Ovarianas/metabolismo
Isoformas de Proteínas
Reação em Cadeia da Polimerase em Tempo Real
Fatores de Processamento de Serina-Arginina/metabolismo
Transcriptoma
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Heterogeneous-Nuclear Ribonucleoproteins); 0 (Protein Isoforms); 0 (SPP1 protein, human); 106441-73-0 (Osteopontin); 170974-22-8 (Serine-Arginine Splicing Factors)
[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:170923
[St] Status:MEDLINE
[do] DOI:10.1177/1010428317725442


  4 / 1591 MEDLINE  
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[PMID]:28844665
[Au] Autor:Dong Z; Yang T; Yang Y; Dou H; Chen G
[Ad] Endereço:College of Life Science, Henan Normal University, Xinxiang, 453007, Henan, China.
[Ti] Título:DjhnRNPA2/B1-like gene is required for planarian regeneration and tissue homeostasis.
[So] Source:Gene;633:9-16, 2017 Oct 30.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The hnRNPs play important roles in physiological processes in eukaryotic organisms by regulation of pre-mRNA after transcription, including pre-mRNA splicing, mRNA stability, DNA replication and repair and telomere maintenance and so on. However, it remains unclear about the specific functions of these genes. In this study, the full-length cDNA sequence of hnRNPA2/B1-like was first cloned from Dugesia japonica, and its roles were investigated by WISH and RNAi. The results showed that: (1) DjhnRNPA2/B1-like was highly conserved during animal evolution; (2) DjhnRNPA2/B1-like mRNA was mainly distributed each side of the body in intact worms and regenerative blastemas, and its expression levels were up-regulated on days 0 and 5 after amputation; (3) the intact and regenerating worms gradually lysed or lost regeneration capacity after DjhnRNPA2/B1-like RNAi; and (4) DjhnRNPA2/B1-like expression is induced by temperature and heavy metal ion stress. The data suggests that DjhnRNPA2/B1-like is a multiple functional gene, it plays important roles in regeneration and homeostatic maintenance and it is also involved in stress responses in planarians. Our work provides basic data for the study of regenerative mechanism and stress responses in freshwater planarians.
[Mh] Termos MeSH primário: Proteínas de Helminto/fisiologia
Ribonucleoproteínas Nucleares Heterogêneas/fisiologia
Homeostase/genética
Planárias/genética
Planárias/fisiologia
Regeneração/genética
[Mh] Termos MeSH secundário: Animais
DNA Complementar/genética
Proteínas de Helminto/classificação
Proteínas de Helminto/genética
Ribonucleoproteínas Nucleares Heterogêneas/classificação
Ribonucleoproteínas Nucleares Heterogêneas/genética
Hibridização In Situ
Metais Pesados/toxicidade
Interferência de RNA/fisiologia
Precursores de RNA/metabolismo
RNA Mensageiro/metabolismo
Homologia de Sequência de Aminoácidos
Estresse Fisiológico/genética
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Complementary); 0 (Helminth Proteins); 0 (Heterogeneous-Nuclear Ribonucleoproteins); 0 (Metals, Heavy); 0 (RNA Precursors); 0 (RNA, Messenger)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170829
[St] Status:MEDLINE


  5 / 1591 MEDLINE  
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[PMID]:28825698
[Au] Autor:Grelet S; Link LA; Howley B; Obellianne C; Palanisamy V; Gangaraju VK; Diehl JA; Howe PH
[Ad] Endereço:Department of Biochemistry, Medical University of South Carolina, Charleston, South Carolina 29425, USA.
[Ti] Título:A regulated PNUTS mRNA to lncRNA splice switch mediates EMT and tumour progression.
[So] Source:Nat Cell Biol;19(9):1105-1115, 2017 Sep.
[Is] ISSN:1476-4679
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The contribution of lncRNAs to tumour progression and the regulatory mechanisms driving their expression are areas of intense investigation. Here, we characterize the binding of heterogeneous nuclear ribonucleoprotein E1 (hnRNP E1) to a nucleic acid structural element located in exon 12 of PNUTS (also known as PPP1R10) pre-RNA that regulates its alternative splicing. HnRNP E1 release from this structural element, following its silencing, nucleocytoplasmic translocation or in response to TGFß, allows alternative splicing and generates a non-coding isoform of PNUTS. Functionally the lncRNA-PNUTS serves as a competitive sponge for miR-205 during epithelial-mesenchymal transition (EMT). In mesenchymal breast tumour cells and in breast tumour samples, the expression of lncRNA-PNUTS is elevated and correlates with levels of ZEB mRNAs. Thus, PNUTS is a bifunctional RNA encoding both PNUTS mRNA and lncRNA-PNUTS, each eliciting distinct biological functions. While PNUTS mRNA is ubiquitously expressed, lncRNA-PNUTS appears to be tightly regulated dependent on the status of hnRNP E1 and tumour context.
[Mh] Termos MeSH primário: Processamento Alternativo
Neoplasias da Mama/metabolismo
Proteínas de Ligação a DNA/metabolismo
Transição Epitelial-Mesenquimal
Neoplasias Pulmonares/metabolismo
Proteínas Nucleares/metabolismo
Precursores de RNA/metabolismo
RNA Longo não Codificante/metabolismo
RNA Mensageiro/metabolismo
Proteínas de Ligação a RNA/metabolismo
[Mh] Termos MeSH secundário: Células A549
Animais
Sítios de Ligação
Neoplasias da Mama/genética
Neoplasias da Mama/patologia
Células CACO-2
Movimento Celular
Proteínas de Ligação a DNA/genética
Éxons
Feminino
Regulação Neoplásica da Expressão Gênica
Ribonucleoproteínas Nucleares Heterogêneas/genética
Ribonucleoproteínas Nucleares Heterogêneas/metabolismo
Seres Humanos
Neoplasias Pulmonares/genética
Neoplasias Pulmonares/secundário
Células MCF-7
Camundongos
MicroRNAs/genética
MicroRNAs/metabolismo
Invasividade Neoplásica
Proteínas Nucleares/genética
Conformação de Ácido Nucleico
Ligação Proteica
Interferência de RNA
Precursores de RNA/química
Precursores de RNA/genética
Sítios de Splice de RNA
RNA Longo não Codificante/química
RNA Longo não Codificante/genética
RNA Mensageiro/química
RNA Mensageiro/genética
Proteínas de Ligação a RNA/genética
Transdução de Sinais
Relação Estrutura-Atividade
Transcrição Genética
Transfecção
Homeobox 1 de Ligação a E-box em Dedo de Zinco/genética
Homeobox 1 de Ligação a E-box em Dedo de Zinco/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (Heterogeneous-Nuclear Ribonucleoproteins); 0 (MIRN205 microRNA, human); 0 (MicroRNAs); 0 (Nuclear Proteins); 0 (PCBP1 protein, human); 0 (PPP1R10 protein, human); 0 (RNA Precursors); 0 (RNA Splice Sites); 0 (RNA, Long Noncoding); 0 (RNA, Messenger); 0 (RNA-Binding Proteins); 0 (ZEB1 protein, human); 0 (Zinc Finger E-box-Binding Homeobox 1)
[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:170822
[St] Status:MEDLINE
[do] DOI:10.1038/ncb3595


  6 / 1591 MEDLINE  
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[PMID]:28805284
[Au] Autor:Lannes L; Young P; Richter C; Morgner N; Schwalbe H
[Ad] Endereço:Institute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe University Frankfurt, Max-von-Laue-Strasse 7, 60438, Frankfurt/Main, Germany.
[Ti] Título:Interaction of the N-Terminal Tandem Domains of hnRNP LL with the BCL2 Promoter i-Motif DNA Sequence.
[So] Source:Chembiochem;18(20):2033-2044, 2017 Oct 18.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The human genome contains GC-rich sequences able to form tetraplex secondary structures known as the G-quadruplex and i-motif. Such sequences are notably present in the promoter region of oncogenes and are proposed to function as regulatory elements of gene expression. The P1 promoter of BCL2 contains a 39-mer C-rich sequence (Py39wt) that can fold into a hairpin or an i-motif in a pH-dependent manner in vitro. The protein hnRNP LL was identified to recognise the i-motif over the hairpin conformation and act as an activating transcription factor. Thus, the Py39wt sequence would act as an ON/OFF switch, according to the secondary structure adopted. Herein, a structural study of the interaction between hnRNP LL and Py39wt is reported. Both N-terminal RNA recognition motifs (RRM12) cooperatively recognise one Py39wt DNA sequence and engage their ß-sheet to form a large binding platform. In contrast, the C-terminal RRMs show no binding capacity. It is observed that RRM12 binds to Py39wt regardless of the DNA conformation. We propose that RRM12 recognises a single-stranded CTCCC element present in loop 1 of the i-motif and in the apical loop of the hairpin conformation.
[Mh] Termos MeSH primário: Ribonucleoproteínas Nucleares Heterogêneas/química
Ribonucleoproteínas Nucleares Heterogêneas/metabolismo
Motivos de Nucleotídeos
Regiões Promotoras Genéticas/genética
Proteínas Proto-Oncogênicas c-bcl-2/genética
[Mh] Termos MeSH secundário: Sítios de Ligação
Seres Humanos
Concentração de Íons de Hidrogênio
Modelos Moleculares
Ligação Proteica
Domínios Proteicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (BCL2 protein, human); 0 (Heterogeneous-Nuclear Ribonucleoproteins); 0 (Proto-Oncogene Proteins c-bcl-2)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170815
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201700390


  7 / 1591 MEDLINE  
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[PMID]:28801479
[Au] Autor:Sun X; Haider Ali MSS; Moran M
[Ad] Endereço:Department of Biochemistry, University of Nebraska - Lincoln, Lincoln, Nebraska 68588, U.S.A. xsun17@unl.edu.
[Ti] Título:The role of interactions of long non-coding RNAs and heterogeneous nuclear ribonucleoproteins in regulating cellular functions.
[So] Source:Biochem J;474(17):2925-2935, 2017 Aug 11.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Long non-coding RNAs (lncRNAs) are emerging as critical regulators of various biological processes and human diseases. The mechanisms of action involve their interactions with proteins, RNA and genomic DNA. Most lncRNAs display strong nuclear localization. Heterogeneous nuclear ribonucleoproteins (hnRNPs) are a large family of RNA-binding proteins that are important for multiple aspects of nucleic acid metabolism. hnRNPs are also predominantly expressed in the nucleus. This review discusses the interactions of lncRNAs and hnRNPs in regulating gene expression at transcriptional and post-transcriptional levels or by changing genomic structure, highlighting their involvements in glucose and lipid metabolism, immune response, DNA damage response, and other cellular functions. Toward the end, several techniques that are used to identify lncRNA binding partners are summarized. There are still many questions that need to be answered in this relatively new research area, which might provide novel targets to control the biological outputs of cells in response to different stimuli.
[Mh] Termos MeSH primário: Núcleo Celular/metabolismo
Regulação da Expressão Gênica/fisiologia
Ribonucleoproteínas Nucleares Heterogêneas/metabolismo
RNA Longo não Codificante/metabolismo
[Mh] Termos MeSH secundário: Animais
Núcleo Celular/genética
Dano ao DNA
Glucose/genética
Glucose/metabolismo
Ribonucleoproteínas Nucleares Heterogêneas/genética
Seres Humanos
Metabolismo dos Lipídeos/fisiologia
RNA Longo não Codificante/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Heterogeneous-Nuclear Ribonucleoproteins); 0 (RNA, Long Noncoding); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170827
[Lr] Data última revisão:
170827
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170813
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20170280


  8 / 1591 MEDLINE  
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[PMID]:28709000
[Au] Autor:Gueroussov S; Weatheritt RJ; O'Hanlon D; Lin ZY; Narula A; Gingras AC; Blencowe BJ
[Ad] Endereço:Donnelly Centre, University of Toronto, Toronto, ON, Canada; Department of Molecular Genetics, University of Toronto, Toronto, ON, Canada. Electronic address: serge.gueroussov@utoronto.ca.
[Ti] Título:Regulatory Expansion in Mammals of Multivalent hnRNP Assemblies that Globally Control Alternative Splicing.
[So] Source:Cell;170(2):324-339.e23, 2017 Jul 13.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Alternative splicing (AS) patterns have diverged rapidly during vertebrate evolution, yet the functions of most species- and lineage-specific splicing events are not known. We observe that mammalian-specific AS events are enriched in transcript sequences encoding intrinsically disordered regions (IDRs) of proteins, in particular those containing glycine/tyrosine repeats that mediate formation of higher-order protein assemblies implicated in gene regulation and human disease. These evolutionary changes impact nearly all members of the hnRNP A and D families of RNA binding proteins. Regulation of these events requires formation of unusual, long-range mammalian-specific RNA duplexes. Differential inclusion of the alternative exons controls the formation of tyrosine-dependent multivalent hnRNP assemblies that, in turn, function to globally regulate splicing. Together, our results demonstrate that AS control of IDR-mediated interactions between hnRNPs represents an important and recurring mechanism underlying splicing regulation. Furthermore, this mechanism has expanded the regulatory capacity of mammalian cells.
[Mh] Termos MeSH primário: Processamento Alternativo
Ribonucleoproteínas Nucleares Heterogêneas/metabolismo
Mamíferos/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Regulação da Expressão Gênica
Seres Humanos
Mamíferos/metabolismo
Isoformas de Proteínas/metabolismo
Precursores de RNA/metabolismo
Alinhamento de Sequência
Vertebrados/genética
Vertebrados/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Heterogeneous-Nuclear Ribonucleoproteins); 0 (Protein Isoforms); 0 (RNA Precursors)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170801
[Lr] Data última revisão:
170801
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170715
[St] Status:MEDLINE


  9 / 1591 MEDLINE  
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[PMID]:28615454
[Au] Autor:Philpott CC; Ryu MS; Frey A; Patel S
[Ad] Endereço:From the Genetics and Metabolism Section, Liver Diseases Branch, NIDDK, National Institutes of Health, Bethesda, Maryland 20892, Carolinep@mail.nih.gov.
[Ti] Título:Cytosolic iron chaperones: Proteins delivering iron cofactors in the cytosol of mammalian cells.
[So] Source:J Biol Chem;292(31):12764-12771, 2017 Aug 04.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Eukaryotic cells contain hundreds of metalloproteins that are supported by intracellular systems coordinating the uptake and distribution of metal cofactors. Iron cofactors include heme, iron-sulfur clusters, and simple iron ions. Poly(rC)-binding proteins are multifunctional adaptors that serve as iron ion chaperones in the cytosolic/nuclear compartment, binding iron at import and delivering it to enzymes, for storage (ferritin) and export (ferroportin). Ferritin iron is mobilized by autophagy through the cargo receptor, nuclear co-activator 4. The monothiol glutaredoxin Glrx3 and BolA2 function as a [2Fe-2S] chaperone complex. These proteins form a core system of cytosolic iron cofactor chaperones in mammalian cells.
[Mh] Termos MeSH primário: Citosol/metabolismo
Ferritinas/metabolismo
Proteínas com Ferro-Enxofre/metabolismo
Ferro/metabolismo
Modelos Biológicos
Modelos Moleculares
Chaperonas Moleculares/metabolismo
[Mh] Termos MeSH secundário: Animais
Apoenzimas/química
Apoenzimas/metabolismo
Apoferritinas/química
Apoferritinas/metabolismo
Autofagia
Proteínas de Transporte/química
Proteínas de Transporte/metabolismo
Proteínas de Transporte de Cátions/química
Proteínas de Transporte de Cátions/metabolismo
Dimerização
Células Precursoras Eritroides/citologia
Células Precursoras Eritroides/metabolismo
Ferritinas/química
Ribonucleoproteínas Nucleares Heterogêneas/química
Ribonucleoproteínas Nucleares Heterogêneas/metabolismo
Seres Humanos
Proteínas com Ferro-Enxofre/química
Chaperonas Moleculares/química
Coativadores de Receptor Nuclear/química
Coativadores de Receptor Nuclear/metabolismo
Multimerização Proteica
Transporte Proteico
Proteínas/química
Proteínas/metabolismo
Proteínas de Ligação a RNA/química
Proteínas de Ligação a RNA/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Apoenzymes); 0 (BOLA2 protein, human); 0 (Carrier Proteins); 0 (Cation Transport Proteins); 0 (GLRX3 protein, human); 0 (Heterogeneous-Nuclear Ribonucleoproteins); 0 (Iron-Sulfur Proteins); 0 (Molecular Chaperones); 0 (NCOA4 protein, human); 0 (Nuclear Receptor Coactivators); 0 (PCBP1 protein, human); 0 (PCBP2 protein, human); 0 (Proteins); 0 (RNA-Binding Proteins); 0 (metal transporting protein 1); 9007-73-2 (Ferritins); 9013-31-4 (Apoferritins); E1UOL152H7 (Iron)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170825
[Lr] Data última revisão:
170825
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170616
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.R117.791962


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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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