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  1 / 10450 MEDLINE  
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[PMID]:27777629
[Au] Autor:Lau AC; Zhu KP; Brouhard EA; Davis MB; Csankovszki G
[Ad] Endereço:Department of Molecular, Cellular and Developmental Biology, University of Michigan, 830 N. University Ave., Ann Arbor, MI 48109-1048 USA ; Genome Technologies, The Jackson Laboratory for Genomic Medicine, Farmington, CT 06032 USA.
[Ti] Título:An H4K16 histone acetyltransferase mediates decondensation of the X chromosome in males.
[So] Source:Epigenetics Chromatin;9:44, 2016.
[Is] ISSN:1756-8935
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: In , in order to equalize gene expression between the sexes and balance X and autosomal expression, two steps are believed to be required. First, an unknown mechanism is hypothesized to upregulate the X chromosome in both sexes. This mechanism balances the X to autosomal expression in males, but creates X overexpression in hermaphrodites. Therefore, to restore the balance, hermaphrodites downregulate gene expression twofold on both X chromosomes. While many studies have focused on X chromosome downregulation, the mechanism of X upregulation is not known. RESULTS: To gain more insight into X upregulation, we studied the effects of chromatin condensation and histone acetylation on gene expression levels in male . We have found that the H4K16 histone acetyltransferase MYS-1/Tip60 mediates dramatic decondensation of the male X chromosome as measured by FISH. However, RNA-seq analysis revealed that MYS-1 contributes only slightly to upregulation of gene expression on the X chromosome. These results suggest that the level of chromosome decondensation does not necessarily correlate with the degree of gene expression change in vivo. Furthermore, the X chromosome is more sensitive to MYS-1-mediated decondensation than the autosomes, despite similar levels of H4K16ac on all chromosomes, as measured by ChIP-seq. H4K16ac levels weakly correlate with gene expression levels on both the X and the autosomes, but highly expressed genes on the X chromosome do not contain exceptionally high levels of H4K16ac. CONCLUSION: These results indicate that H4K16ac and chromosome decondensation influence regulation of the male X chromosome; however, they do not fully account for the high levels of gene expression observed on the X chromosomes.
[Mh] Termos MeSH primário: Proteínas de Caenorhabditis elegans/metabolismo
Caenorhabditis elegans/metabolismo
Histona Acetiltransferases/metabolismo
Cromossomo X/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Animais
Caenorhabditis elegans/genética
Proteínas de Caenorhabditis elegans/genética
Cromatina/metabolismo
Montagem e Desmontagem da Cromatina
Imunoprecipitação da Cromatina
Compensação de Dosagem (Genética)
Expressão Gênica
Histona Acetiltransferases/genética
Histonas/metabolismo
Hibridização in Situ Fluorescente
Masculino
Análise de Sequência de DNA
Cromossomo X/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (Chromatin); 0 (Histones); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.48 (MYS-1 protein, C elegans)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180310
[Lr] Data última revisão:
180310
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161026
[St] Status:MEDLINE


  2 / 10450 MEDLINE  
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[PMID]:29281635
[Au] Autor:Takahashi M; Takagi S
[Ad] Endereço:Division of Biological Science, Nagoya University Graduate School of Science Chikusa-ku, Nagoya, Japan.
[Ti] Título:Optical silencing of body wall muscles induces pumping inhibition in Caenorhabditis elegans.
[So] Source:PLoS Genet;13(12):e1007134, 2017 12.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Feeding, a vital behavior in animals, is modulated depending on internal and external factors. In the nematode Caenorhabditis elegans, the feeding organ called the pharynx ingests food by pumping driven by the pharyngeal muscles. Here we report that optical silencing of the body wall muscles, which drive the locomotory movement of worms, affects pumping. In worms expressing the Arch proton pump or the ACR2 anion channel in the body wall muscle cells, the pumping rate decreases after activation of Arch or ACR2 with light illumination, and recovers gradually after terminating illumination. Pumping was similarly inhibited by illumination in locomotion-defective mutants carrying Arch, suggesting that perturbation of locomotory movement is not critical for pumping inhibition. Analysis of mutants and cell ablation experiments showed that the signals mediating the pumping inhibition response triggered by activation of Arch with weak light are transferred mainly through two pathways: one involving gap junction-dependent mechanisms through pharyngeal I1 neurons, which mediate fast signals, and the other involving dense-core vesicle-dependent mechanisms, which mediate slow signals. Activation of Arch with strong light inhibited pumping strongly in a manner that does not rely on either gap junction-dependent or dense-core vesicle-dependent mechanisms. Our study revealed a new aspect of the neural and neuroendocrine controls of pumping initiated from the body wall muscles.
[Mh] Termos MeSH primário: Optogenética/métodos
Músculos Faríngeos/metabolismo
Bombas de Próton/metabolismo
[Mh] Termos MeSH secundário: Animais
Caenorhabditis elegans
Proteínas de Caenorhabditis elegans/metabolismo
Ingestão de Alimentos/fisiologia
Locomoção/fisiologia
Neurônios Motores/metabolismo
Músculo Esquelético/metabolismo
Faringe/metabolismo
Serotonina
Transdução de Sinais/fisiologia
Canais de Ânion Dependentes de Voltagem/genética
Canais de Ânion Dependentes de Voltagem/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (Proton Pumps); 0 (Voltage-Dependent Anion Channels); 333DO1RDJY (Serotonin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171228
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1007134


  3 / 10450 MEDLINE  
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[PMID]:29228003
[Au] Autor:Crawley O; Giles AC; Desbois M; Kashyap S; Birnbaum R; Grill B
[Ad] Endereço:Department of Neuroscience, The Scripps Research Institute, Scripps Florida, Jupiter, Florida, United States of America.
[Ti] Título:A MIG-15/JNK-1 MAP kinase cascade opposes RPM-1 signaling in synapse formation and learning.
[So] Source:PLoS Genet;13(12):e1007095, 2017 12.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Pam/Highwire/RPM-1 (PHR) proteins are conserved intracellular signaling hubs that regulate synapse formation and axon termination. The C. elegans PHR protein, called RPM-1, acts as a ubiquitin ligase to inhibit the DLK-1 and MLK-1 MAP kinase pathways. We have identified several kinases that are likely to form a new MAP kinase pathway that suppresses synapse formation defects, but not axon termination defects, in the mechanosensory neurons of rpm-1 mutants. This pathway includes: MIG-15 (MAP4K), NSY-1 (MAP3K), JKK-1 (MAP2K) and JNK-1 (MAPK). Transgenic overexpression of kinases in the MIG-15/JNK-1 pathway is sufficient to impair synapse formation in wild-type animals. The MIG-15/JNK-1 pathway functions cell autonomously in the mechanosensory neurons, and these kinases localize to presynaptic terminals providing further evidence of a role in synapse development. Loss of MIG-15/JNK-1 signaling also suppresses defects in habituation to repeated mechanical stimuli in rpm-1 mutants, a behavioral deficit that is likely to arise from impaired glutamatergic synapse formation. Interestingly, habituation results are consistent with the MIG-15/JNK-1 pathway functioning as a parallel opposing pathway to RPM-1. These findings indicate the MIG-15/JNK-1 pathway can restrict both glutamatergic synapse formation and short-term learning.
[Mh] Termos MeSH primário: Proteínas de Caenorhabditis elegans/metabolismo
Fatores de Troca do Nucleotídeo Guanina/metabolismo
Sistema de Sinalização das MAP Quinases
Proteínas Quinases Ativadas por Mitógeno/metabolismo
Proteínas Serina-Treonina Quinases/metabolismo
Sinapses/fisiologia
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Axônios/metabolismo
Caenorhabditis elegans/genética
Caenorhabditis elegans/crescimento & desenvolvimento
Proteínas de Caenorhabditis elegans/genética
Fatores de Troca do Nucleotídeo Guanina/genética
Proteínas Quinases Ativadas por Mitógeno/genética
Mutação
Neurogênese
Neurônios/metabolismo
Terminações Pré-Sinápticas/metabolismo
Proteínas Quinases/genética
Proteínas Quinases/metabolismo
Proteínas Serina-Treonina Quinases/genética
Transdução de Sinais
Sinapses/enzimologia
Ubiquitina-Proteína Ligases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (Guanine Nucleotide Exchange Factors); 0 (RPM-1 protein, C elegans); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 2.7.- (Protein Kinases); EC 2.7.1.- (jkk-1 protein, C elegans); EC 2.7.11.1 (Mig-15 protein, C elegans); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.24 (JNK-1 protein, C elegans); EC 2.7.11.24 (Mitogen-Activated Protein Kinases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171212
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1007095


  4 / 10450 MEDLINE  
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[PMID]:28451641
[Au] Autor:Yu J; Yang W; Liu H; Hao Y; Zhang Y
[Ad] Endereço:Department of Organismic and Evolutionary Biology, Center for Brain Science, Harvard University, Cambridge, MA 02138.
[Ti] Título:An Aversive Response to Osmotic Upshift in .
[So] Source:eNeuro;4(2), 2017 Mar-Apr.
[Is] ISSN:2373-2822
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Environmental osmolarity presents a common type of sensory stimulus to animals. While behavioral responses to osmotic changes are important for maintaining a stable intracellular osmolarity, the underlying mechanisms are not fully understood. In the natural habitat of , changes in environmental osmolarity are commonplace. It is known that the nematode acutely avoids shocks of extremely high osmolarity. Here, we show that also generates gradually increased aversion of mild upshifts in environmental osmolarity. Different from an acute avoidance of osmotic shocks that depends on the function of a transient receptor potential vanilloid channel, the slow aversion to osmotic upshifts requires the cGMP-gated sensory channel subunit TAX-2. TAX-2 acts in several sensory neurons that are exposed to body fluid to generate the aversive response through a motor network that underlies navigation. Osmotic upshifts activate the body cavity sensory neuron URX, which is known to induce aversion upon activation. Together, our results characterize the molecular and cellular mechanisms underlying a novel sensorimotor response to osmotic stimuli and reveal that engages different behaviors and the underlying mechanisms to regulate responses to extracellular osmolarity.
[Mh] Termos MeSH primário: Proteínas de Caenorhabditis elegans/metabolismo
Canais Iônicos/metabolismo
Osmorregulação
Células Receptoras Sensoriais/metabolismo
[Mh] Termos MeSH secundário: Animais
Caenorhabditis elegans
Locomoção
Pressão Osmótica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (Ion Channels); 0 (tax-2 protein, C elegans)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180228
[Lr] Data última revisão:
180228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE


  5 / 10450 MEDLINE  
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[PMID]:29349444
[Au] Autor:Hayashi K; Hasegawa S; Sagawa T; Tasaki S; Niwa S
[Ad] Endereço:Department of Applied Physics, Graduate School of Engineering, Tohoku University, Sendai, Japan. kumiko@camp.apph.tohoku.ac.jp.
[Ti] Título:Non-invasive force measurement reveals the number of active kinesins on a synaptic vesicle precursor in axonal transport regulated by ARL-8.
[So] Source:Phys Chem Chem Phys;20(5):3403-3410, 2018 Jan 31.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Kinesin superfamily protein UNC-104, a member of the kinesin-3 family, transports synaptic vesicle precursors (SVPs). In this study, the number of active UNC-104 molecules hauling a single SVP in axons in the worm Caenorhabditis elegans was counted by applying a newly developed non-invasive force measurement technique. The distribution of the force acting on a SVP transported by UNC-104 was spread out over several clusters, implying the presence of several force-producing units (FPUs). We then compared the number of FPUs in the wild-type worms with that in arl-8 gene-deletion mutant worms. ARL-8 is a SVP-bound arf-like small guanosine triphosphatase, and is known to promote unlocking of the autoinhibition of the motor, which is critical for avoiding unnecessary consumption of adenosine triphosphate when the motor does not bind to a SVP. There were fewer FPUs in the arl-8 mutant worms. This finding indicates that a lack of ARL-8 decreased the number of active UNC-104 motors, which then led to a decrease in the number of motors responsible for SVP transport.
[Mh] Termos MeSH primário: Proteínas de Caenorhabditis elegans/metabolismo
GTP Fosfo-Hidrolases/metabolismo
Cinesina/metabolismo
Vesículas Sinápticas/metabolismo
[Mh] Termos MeSH secundário: Animais
Transporte Axonal
Axônios/metabolismo
Caenorhabditis elegans
Proteínas de Caenorhabditis elegans/química
Proteínas de Caenorhabditis elegans/genética
GTP Fosfo-Hidrolases/química
GTP Fosfo-Hidrolases/genética
Cinesina/química
Microscopia de Fluorescência
Mutagênese
Vesículas Sinápticas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); EC 3.6.1.- (Arl8 protein, C elegans); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.4.4 (Kinesin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180120
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp05890j


  6 / 10450 MEDLINE  
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[PMID]:27776915
[Au] Autor:Mendler M; Riedinger C; Schlotterer A; Volk N; Fleming T; Herzig S; Nawroth PP; Morcos M
[Ad] Endereço:Department of Medicine 1 and Clinical Chemistry, University of Heidelberg, Im Neuenheimer Feld 410, 69120 Heidelberg, Germany. Electronic address: michael.mendler@med.uni-heidelberg.de.
[Ti] Título:Reduction in ins-7 gene expression in non-neuronal cells of high glucose exposed Caenorhabditis elegans protects from reactive metabolites, preserves neuronal structure and head motility, and prolongs lifespan.
[So] Source:J Diabetes Complications;31(2):304-310, 2017 Feb.
[Is] ISSN:1873-460X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Glucose derived metabolism generates reactive metabolites affecting the neuronal system and lifespan in C. elegans. Here, the role of the insulin homologue ins-7 and its downstream effectors in the generation of high glucose induced neuronal damage and shortening of lifespan was studied. RESULTS: In C. elegans high glucose conditions induced the expression of the insulin homologue ins-7. Abrogating ins-7 under high glucose conditions in non-neuronal cells decreased reactive oxygen species (ROS)-formation and accumulation of methylglyoxal derived advanced glycation endproducts (AGEs), prevented structural neuronal damage and normalised head motility and lifespan. The restoration of lifespan by decreased ins-7 expression was dependent on the concerted action of sod-3 and glod-4 coding for the homologues of iron-manganese superoxide dismutase and glyoxalase 1, respectively. CONCLUSIONS: Under high glucose conditions mitochondria-mediated oxidative stress and glycation are downstream targets of ins-7. This impairs the neuronal system and longevity via a non-neuronal/neuronal crosstalk by affecting sod-3 and glod-4, thus giving further insight into the pathophysiology of diabetic complications.
[Mh] Termos MeSH primário: Proteínas de Caenorhabditis elegans/antagonistas & inibidores
Proteínas de Caenorhabditis elegans/metabolismo
Caenorhabditis elegans/metabolismo
Regulação da Expressão Gênica no Desenvolvimento
Glucose/envenenamento
Lactoilglutationa Liase/metabolismo
Estresse Oxidativo
Hormônios Peptídicos/antagonistas & inibidores
Superóxido Dismutase/metabolismo
[Mh] Termos MeSH secundário: Animais
Comportamento Animal
Caenorhabditis elegans/enzimologia
Caenorhabditis elegans/crescimento & desenvolvimento
Proteínas de Caenorhabditis elegans/agonistas
Proteínas de Caenorhabditis elegans/genética
Retroalimentação Fisiológica
Técnicas de Silenciamento de Genes
Técnicas de Inativação de Genes
Produtos Finais de Glicação Avançada/metabolismo
Lactoilglutationa Liase/antagonistas & inibidores
Lactoilglutationa Liase/genética
Longevidade
Mutação
Neuroproteção
Concentração Osmolar
Hormônios Peptídicos/agonistas
Hormônios Peptídicos/genética
Hormônios Peptídicos/metabolismo
Interferência de RNA
Espécies Reativas de Oxigênio/metabolismo
Superóxido Dismutase/antagonistas & inibidores
Superóxido Dismutase/genética
Análise de Sobrevida
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (Glycation End Products, Advanced); 0 (Ins-7 protein, C elegans); 0 (Peptide Hormones); 0 (Reactive Oxygen Species); EC 1.15.1.1 (Sod-3 protein, C elegans); EC 1.15.1.1 (Superoxide Dismutase); EC 4.4.1.5 (Lactoylglutathione Lyase); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161026
[St] Status:MEDLINE


  7 / 10450 MEDLINE  
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[PMID]:29293515
[Au] Autor:Buntschuh I; Raps DA; Joseph I; Reid C; Chait A; Totanes R; Sawh M; Li C
[Ad] Endereço:Department of Biology, City College of New York, City University of New York, New York, NY, United States of America.
[Ti] Título:FLP-1 neuropeptides modulate sensory and motor circuits in the nematode Caenorhabditis elegans.
[So] Source:PLoS One;13(1):e0189320, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Parasitic nematodes infect over one quarter of the population worldwide, causing morbidity in over one billion people. Current anthelmintic drugs are beginning to lose effectiveness due to the presence of resistant strains. We are interested in the role of neuropeptides, which regulate behaviors in all organisms, as another possible target for anthelmintic drugs. FMRFamide-related peptides (FaRPs) are a family of neuropeptides that are conserved throughout the animal kingdom. In particular, nematodes contain the largest family of FaRPs identified thus far and many of these FaRPs are identical among different nematode species; FaRPs in nematodes are collectively referred to as FLPs (FMRFamide-like peptides). However, little is known about the function of these FLPs. We are using the non-parasitic nematode Caenorhabditis elegans as a model for examining FLPs in nematodes. C. elegans contains at least 31 flp genes that encode 72 potential FLPs. Among the flp genes, flp-1 is one of the few that is universally found in nematodes. FLP-1 neuropeptides were previously reported to be involved in sensory and motor functions. However, previous alleles of flp-1 also disrupted a neighboring gene, daf-10. To understand the phenotypes of flp-1, new alleles that specifically disrupt flp-1 were characterized. The previously reported locomotory and egg-laying defects were found to be due to loss of flp-1, while the osmolarity defect is due to loss of daf-10. In addition, loss of flp-1 and daf-10 both cause several phenotypes that increase in severity in the double mutants by disrupting different neurons in the neural circuits.
[Mh] Termos MeSH primário: Proteínas de Caenorhabditis elegans/fisiologia
Caenorhabditis elegans/fisiologia
Neuropeptídeos/fisiologia
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Caenorhabditis elegans/metabolismo
Proteínas de Caenorhabditis elegans/química
Locomoção
Neuropeptídeos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (Flp-1 protein, C elegans); 0 (Neuropeptides)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180103
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189320


  8 / 10450 MEDLINE  
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[PMID]:28463115
[Au] Autor:O'Hern PJ; do Carmo G Gonçalves I; Brecht J; López Soto EJ; Simon J; Chapkis N; Lipscombe D; Kye MJ; Hart AC
[Ad] Endereço:Department of Neuroscience, Brown University, Providence, United States.
[Ti] Título:Decreased microRNA levels lead to deleterious increases in neuronal M2 muscarinic receptors in Spinal Muscular Atrophy models.
[So] Source:Elife;6, 2017 05 02.
[Is] ISSN:2050-084X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Spinal Muscular Atrophy (SMA) is caused by diminished Survival of Motor Neuron (SMN) protein, leading to neuromuscular junction (NMJ) dysfunction and spinal motor neuron (MN) loss. Here, we report that reduced SMN function impacts the action of a pertinent microRNA and its mRNA target in MNs. Loss of the SMN ortholog, SMN-1, causes NMJ defects. We found that increased levels of the Gemin3 ortholog, MEL-46, ameliorates these defects. Increased MEL-46 levels also restored perturbed microRNA (miR-2) function in animals. We determined that miR-2 regulates expression of the M2 muscarinic receptor (m2R) ortholog, GAR-2. GAR-2 loss ameliorated and synaptic defects. In an SMA mouse model, m2R levels were increased and pharmacological inhibition of m2R rescued MN process defects. Collectively, these results suggest decreased SMN leads to defective microRNA function MEL-46 misregulation, followed by increased m2R expression, and neuronal dysfunction in SMA.
[Mh] Termos MeSH primário: Proteínas de Caenorhabditis elegans/metabolismo
Caenorhabditis elegans
MicroRNAs/metabolismo
Atrofia Muscular Espinal/fisiopatologia
Receptor Muscarínico M2/análise
Proteína 1 de Sobrevivência do Neurônio Motor/metabolismo
[Mh] Termos MeSH secundário: Animais
RNA Helicases DEAD-box/metabolismo
Modelos Animais de Doenças
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (MEL-46 protein, C elegans); 0 (MicroRNAs); 0 (Receptor, Muscarinic M2); 0 (SMN1 protein, C elegans); 0 (Survival of Motor Neuron 1 Protein); EC 3.6.4.13 (DEAD-box RNA Helicases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180211
[Lr] Data última revisão:
180211
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE


  9 / 10450 MEDLINE  
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[PMID]:29324872
[Au] Autor:Jiao AL; Foster DJ; Dixon J; Slack FJ
[Ad] Endereço:Institute for RNA Medicine, Department of Pathology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, United States of America.
[Ti] Título:lin-4 and the NRDE pathway are required to activate a transgenic lin-4 reporter but not the endogenous lin-4 locus in C. elegans.
[So] Source:PLoS One;13(1):e0190766, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:As the founding member of the microRNA (miRNA) gene family, insights into lin-4 regulation and function have laid a conceptual foundation for countless miRNA-related studies that followed. We previously showed that a transcriptional lin-4 reporter in C. elegans was positively regulated by a lin-4-complementary element (LCE), and by lin-4 itself. In this study, we sought to (1) identify additional factors required for lin-4 reporter expression, and (2) validate the endogenous relevance of a potential positive autoregulatory mechanism of lin-4 expression. We report that all four core nuclear RNAi factors (nrde-1, nrde-2, nrde-3 and nrde-4), positively regulate lin-4 reporter expression. In contrast, endogenous lin-4 levels were largely unaffected in nrde-2;nrde-3 mutants. Further, an endogenous LCE deletion generated by CRISPR-Cas9 revealed that the LCE was also not necessary for the activity of the endogenous lin-4 promoter. Finally, mutations in mature lin-4 did not reduce primary lin-4 transcript levels. Taken together, these data indicate that under growth conditions that reveal effects at the transgenic locus, a direct, positive autoregulatory mechanism of lin-4 expression does not occur in the context of the endogenous lin-4 locus.
[Mh] Termos MeSH primário: Proteínas de Caenorhabditis elegans/metabolismo
Caenorhabditis elegans/genética
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Proteínas de Caenorhabditis elegans/genética
Regiões Promotoras Genéticas
Interferência de RNA
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180206
[Lr] Data última revisão:
180206
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180112
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190766


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[PMID]:29232700
[Au] Autor:Shin H; Haupt KA; Kershner AM; Kroll-Conner P; Wickens M; Kimble J
[Ad] Endereço:Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin, United States of America.
[Ti] Título:SYGL-1 and LST-1 link niche signaling to PUF RNA repression for stem cell maintenance in Caenorhabditis elegans.
[So] Source:PLoS Genet;13(12):e1007121, 2017 12.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Central questions in regenerative biology include how stem cells are maintained and how they transition from self-renewal to differentiation. Germline stem cells (GSCs) in Caeno-rhabditis elegans provide a tractable in vivo model to address these questions. In this system, Notch signaling and PUF RNA binding proteins, FBF-1 and FBF-2 (collectively FBF), maintain a pool of GSCs in a naïve state. An open question has been how Notch signaling modulates FBF activity to promote stem cell self-renewal. Here we report that two Notch targets, SYGL-1 and LST-1, link niche signaling to FBF. We find that SYGL-1 and LST-1 proteins are cytoplasmic and normally restricted to the GSC pool region. Increasing the distribution of SYGL-1 expands the pool correspondingly, and vast overexpression of either SYGL-1 or LST-1 generates a germline tumor. Thus, SYGL-1 and LST-1 are each sufficient to drive "stemness" and their spatial restriction prevents tumor formation. Importantly, SYGL-1 and LST-1 can only drive tumor formation when FBF is present. Moreover, both proteins interact physically with FBF, and both are required to repress a signature FBF mRNA target. Together, our results support a model in which SYGL-1 and LST-1 form a repressive complex with FBF that is crucial for stem cell maintenance. We further propose that progression from a naïve stem cell state to a state primed for differentiation relies on loss of SYGL-1 and LST-1, which in turn relieves FBF target RNAs from repression. Broadly, our results provide new insights into the link between niche signaling and a downstream RNA regulatory network and how this circuitry governs the balance between self-renewal and differentiation.
[Mh] Termos MeSH primário: Proteínas de Caenorhabditis elegans/genética
Diferenciação Celular/genética
Autorrenovação Celular/genética
Peptídeo 1 Semelhante ao Glucagon/genética
[Mh] Termos MeSH secundário: Animais
Caenorhabditis elegans/genética
Caenorhabditis elegans/crescimento & desenvolvimento
Meiose/genética
RNA/genética
RNA Mensageiro/genética
Proteínas de Ligação a RNA/genética
Transdução de Sinais/genética
Células-Tronco/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (LST-1 protein, C elegans); 0 (RNA, Messenger); 0 (RNA-Binding Proteins); 0 (SYGL-1 protein, C elegans); 63231-63-0 (RNA); 89750-14-1 (Glucagon-Like Peptide 1)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180113
[Lr] Data última revisão:
180113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171213
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1007121



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