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Pesquisa : D12.776.157.530.625.875 [Categoria DeCS]
Referências encontradas : 213 [refinar]
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  1 / 213 MEDLINE  
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[PMID]:28328131
[Au] Autor:Marini C; Hardies K; Pisano T; May P; Weckhuysen S; Cellini E; Suls A; Mei D; Balling R; Jonghe PD; Helbig I; Garozzo D; Guerrini R; EuroEPINOMICS consortium AR working group
[Ad] Endereço:Neurology Unit and Neurogenetics Laboratories, Meyer Children Hospital, Florence, Italy.
[Ti] Título:Recessive mutations in SLC35A3 cause early onset epileptic encephalopathy with skeletal defects.
[So] Source:Am J Med Genet A;173(4):1119-1123, 2017 Apr.
[Is] ISSN:1552-4833
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We describe the clinical and whole genome sequencing (WGS) study of a non-consanguineous Italian family in which two siblings, a boy and a girl, manifesting a severe epileptic encephalopathy (EE) with skeletal abnormalities, carried novel SLC35A3 compound heterozygous mutations. Both siblings exhibited infantile spasms, associated with focal, and tonic vibratory seizures from early infancy. EEG recordings showed a suppression-burst (SB) pattern and multifocal paroxysmal activity in both. In addition both had quadriplegia, acquired microcephaly, and severe intellectual disability. General examination showed distal arthrogryposis predominant in the hands in both siblings and severe left dorso-lumbar convex scoliosis in one. WGS of the siblings-parents quartet identified novel compound heterozygous mutations in SLC35A3 in both children. SLC35A3 encodes the major Golgi uridine diphosphate N-acetylglucosamine transporter. With this study, we add SLC35A3 to the gene list of epilepsies. Neurological symptoms and skeletal abnormalities might result from impaired glycosylation of proteins involved in normal development and function of the central nervous system and skeletal apparatus.
[Mh] Termos MeSH primário: Artrogripose/genética
Deficiência Intelectual/genética
Microcefalia/genética
Mutação
Proteínas de Transporte de Nucleotídeos/genética
Quadriplegia/genética
Espasmos Infantis/genética
[Mh] Termos MeSH secundário: Artrogripose/diagnóstico
Artrogripose/patologia
Osso e Ossos/anormalidades
Criança
Eletroencefalografia
Feminino
Expressão Gênica
Glicosilação
Heterozigoto
Seres Humanos
Deficiência Intelectual/diagnóstico
Deficiência Intelectual/patologia
Masculino
Microcefalia/diagnóstico
Microcefalia/patologia
Quadriplegia/diagnóstico
Quadriplegia/patologia
Irmãos
Espasmos Infantis/diagnóstico
Espasmos Infantis/patologia
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nucleotide Transport Proteins); 0 (SLC35A4 protein, human)
[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:170323
[St] Status:MEDLINE
[do] DOI:10.1002/ajmg.a.38112


  2 / 213 MEDLINE  
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[PMID]:28167211
[Au] Autor:Sosicka P; Maszczak-Seneczko D; Bazan B; Shauchuk Y; Kaczmarek B; Olczak M
[Ad] Endereço:Laboratory of Biochemistry, Faculty of Biotechnology, University of Wroclaw, 14A F. Joliot-Curie St., 50-383 Wroclaw, Poland.
[Ti] Título:An insight into the orphan nucleotide sugar transporter SLC35A4.
[So] Source:Biochim Biophys Acta;1864(5):825-838, 2017 05.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:SLC35A4 has been classified in the SLC35A subfamily based on amino acid sequence homology. Most of the proteins belonging to the SLC35 family act as transporters of nucleotide sugars. In this study, the subcellular localization of endogenous SLC35A4 was determined via immunofluorescence staining, and it was demonstrated that SLC35A4 localizes mainly to the Golgi apparatus. In silico topology prediction suggests that SLC35A4 has an uneven number of transmembrane domains and its N-terminus is directed towards the Golgi lumen. However, an experimental assay refuted this prediction: SLC35A4 has an even number of transmembrane regions with both termini facing the cytosol. In vivo interaction analysis using the FLIM-FRET approach revealed that SLC35A4 neither forms homomers nor associates with other members of the SLC35A subfamily except SLC35A5. Additional assays demonstrated that endogenous SLC35A4 is 10 to 40nm proximal to SLC35A2 and SLC35A3. To determine SLC35A4 function SLC35A4 knock-out cells were generated with the CRISPR-Cas9 approach. Although no significant changes in glycosylation were observed, the introduced mutation influenced the subcellular distribution of the SLC35A2/SLC35A3 complexes. Additional FLIM-FRET experiments revealed that overexpression of SLC35A4-BFP together with SLC35A3 and the SLC35A2-Golgi splice variant negatively affects the interaction between the two latter proteins. The results presented here strongly indicate a modulatory role for SLC35A4 in intracellular trafficking of SLC35A2/SLC35A3 complexes.
[Mh] Termos MeSH primário: Proteínas de Transporte de Monossacarídeos/fisiologia
Proteínas de Transporte de Nucleotídeos/fisiologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Transporte Biológico/genética
Células COS
Metabolismo dos Carboidratos/genética
Linhagem Celular Tumoral
Cercopithecus aethiops
Cães
Células HEK293
Células Hep G2
Seres Humanos
Células Madin Darby de Rim Canino
Proteínas de Transporte de Monossacarídeos/química
Proteínas de Transporte de Monossacarídeos/genética
Proteínas de Transporte de Nucleotídeos/química
Proteínas de Transporte de Nucleotídeos/genética
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Monosaccharide Transport Proteins); 0 (Nucleotide Transport Proteins); 0 (SLC35A4 protein, human)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170208
[St] Status:MEDLINE


  3 / 213 MEDLINE  
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[PMID]:28060940
[Au] Autor:Ihara T; Mitsui T; Nakamura Y; Kira S; Nakagomi H; Sawada N; Hirayama Y; Shibata K; Shigetomi E; Shinozaki Y; Yoshiyama M; Andersson KE; Nakao A; Takeda M; Koizumi S
[Ad] Endereço:Department of Urology, Interdisciplinary Graduate School of Medicine, University of Yamanashi, Chuo, Yamanashi, Japan.
[Ti] Título:Clock Genes Regulate the Circadian Expression of Piezo1, TRPV4, Connexin26, and VNUT in an Ex Vivo Mouse Bladder Mucosa.
[So] Source:PLoS One;12(1):e0168234, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVES: ClockΔ19/Δ19 mice is an experimental model mouse for nocturia (NOC). Using the bladder mucosa obtained from ClockΔ19/Δ19 mice, we investigated the gene expression rhythms of mechanosensory cation channels such as transient receptor potential cation channel subfamily V member 4 (TRPV4) and Piezo1, and main ATP release pathways including vesicular nucleotide transporter (VNUT) and Connexin26(Cx26), in addition to clock genes. MATERIALS AND METHODS: Eight- to twelve-week-old male C57BL/6 mice (WT) and age- and sex-matched C57BL/6 ClockΔ19/Δ19 mice, which were bred under 12-h light/dark conditions for 2 weeks, were used. Gene expression rhythms and transcriptional regulation mechanisms in clock genes, mechanosensor, Cx26 and VNUT were measured in the mouse bladder mucosa, collected every 4 hours from WT and ClockΔ19/Δ19 mice using quantitative RT-PCR, a Western blot analysis, and ChIP assays. RESULTS: WT mice showed circadian rhythms in clock genes as well as mechanosensor, Cx26 and VNUT. Their expression was low during the sleep phase. The results of ChIP assays showed Clock protein binding to the promotor regions and the transcriptional regulation of mechanosensor, Cx26 and VNUT. In contrast, all of these circadian expressions were disrupted in ClockΔ19/Δ19 mice. The gene expression of mechanosensor, Cx26 and VNUT was maintained at a higher level in spite of the sleep phase. CONCLUSIONS: Mechanosensor, Cx26 and VNUT expressed with circadian rhythm in the mouse bladder mucosa. The disruption of circadian rhythms in these genes, induced by the abnormalities in clock genes, may be factors contributing to NOC because of hypersensitivity to bladder wall extension.
[Mh] Termos MeSH primário: Ritmo Circadiano
Conexinas/genética
Regulação da Expressão Gênica
Canais Iônicos/genética
Proteínas de Transporte de Nucleotídeos/genética
Canais de Cátion TRPV/genética
Bexiga Urinária/metabolismo
[Mh] Termos MeSH secundário: Animais
Modelos Animais de Doenças
Masculino
Camundongos
Camundongos Endogâmicos BALB C
Noctúria/genética
Noctúria/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Connexins); 0 (Gjb2 protein, mouse); 0 (Ion Channels); 0 (Nucleotide Transport Proteins); 0 (Piezo1 protein, mouse); 0 (Slc17a9 protein, mouse); 0 (TRPV Cation Channels); 0 (Trpv4 protein, mouse)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170809
[Lr] Data última revisão:
170809
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170107
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0168234


  4 / 213 MEDLINE  
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[PMID]:27987306
[Au] Autor:Beck A; Fecher-Trost C; Wolske K; Philipp SE; Flockerzi V; Wissenbach U
[Ad] Endereço:Institut für Experimentelle und Klinische Pharmakologie und Toxikologie, Universität des Saarlandes, Homburg/Saar, Germany.
[Ti] Título:Identification of Sidt2 as a lysosomal cation-conducting protein.
[So] Source:FEBS Lett;591(1):76-87, 2017 Jan.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A screen to identify lysosomal-expressed ion channels led to the discovery of the human Sidt2 protein. Sidt2 is expressed within lysosomal organelles but as a result of heterologous overexpression the protein is also detectable within the plasma membrane of human embryonic kidney cells. The overexpressed protein leads to cell depolarization upon sodium addition. Accordingly in whole-cell patch clamp experiments a spontaneous noninactivating monovalent cation current can be detected in Sidt2-overexpressing cells. Strong overexpression of Sidt2 in HEK293 cells is attended by a significant reduction/loss of detectable lysosomes, indicating that the overexpressed protein leads to lysosomal dysfunction, a hallmark of Alzheimer's disease. Sidt2 is located on chromosome 11q23, a locus repeatedly found by chromosomal mapping of Alzheimer's disease-related genes.
[Mh] Termos MeSH primário: Lisossomos/metabolismo
Proteínas de Membrana/metabolismo
Proteínas de Transporte de Nucleotídeos/metabolismo
[Mh] Termos MeSH secundário: Doença de Alzheimer/patologia
Aminas
Animais
Cátions
Membrana Celular/metabolismo
Forma Celular
Tamanho Celular
Condutividade Elétrica
Evolução Molecular
Células HEK293
Seres Humanos
Glicoproteínas de Membrana Associadas ao Lisossomo/metabolismo
Potenciais da Membrana
Proteínas de Membrana/genética
Camundongos
Proteínas de Transporte de Nucleotídeos/genética
Sódio/metabolismo
Transfecção
[Pt] Tipo de publicação:LETTER
[Nm] Nome de substância:
0 (Amines); 0 (Cations); 0 (LAMP1 protein, human); 0 (Lysosome-Associated Membrane Glycoproteins); 0 (Membrane Proteins); 0 (Nucleotide Transport Proteins); 0 (Red DND-99); 0 (SIDT2 protein, human); 0 (Sidt2 protein, mouse); 9NEZ333N27 (Sodium)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170523
[Lr] Data última revisão:
170523
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161218
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12528


  5 / 213 MEDLINE  
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[PMID]:27477609
[Au] Autor:Zhong XZ; Cao Q; Sun X; Dong XP
[Ad] Endereço:Department of Physiology and Biophysics, Dalhousie University, Halifax, B3H 4R2, Nova Scotia, Canada.
[Ti] Título:Activation of lysosomal P2X4 by ATP transported into lysosomes via VNUT/SLC17A9 using V-ATPase generated voltage gradient as the driving force.
[So] Source:J Physiol;594(15):4253-66, 2016 Aug 01.
[Is] ISSN:1469-7793
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:KEY POINTS: SLC17A9 proteins function as a lysosomal ATP transporter responsible for lysosomal ATP accumulation. P2X4 receptors act as lysosomal ion channels activated by luminal ATP. SLC17A9-mediated ATP transport across the lysosomal membrane is suppressed by Bafilomycin A1, the V-ATPase inhibitor. SLC17A9 mainly uses voltage gradient but not pH gradient generated by the V-ATPase as the driving force to transport ATP into the lysosome to activate P2X4. ABSTRACT: The lysosome contains abundant ATP which plays important roles in lysosome functions and in cell signalling. Recently, solute carrier family 17 member 9 (SLC17A9, also known as VNUT for vesicular nucleotide transporter) proteins were suggested to function as a lysosomal ATP transporter responsible for lysosomal ATP accumulation, and P2X4 receptors were suggested to be lysosomal ion channels that are activated by luminal ATP. However, the molecular mechanism of SLC17A9 transporting ATP and the regulatory mechanism of lysosomal P2X4 are largely unknown. In this study, we report that SLC17A9-mediated ATP transport across lysosomal membranes is suppressed by Bafilomycin A1, the V-ATPase inhibitor. By measuring P2X4 activity, which is indicative of ATP transport across lysosomal membranes, we further demonstrated that SLC17A9 mainly uses voltage gradient but not pH gradient as the driving force to transport ATP into lysosomes. This study provides a molecular mechanism for lysosomal ATP transport mediated by SLC17A9. It also suggests a regulatory mechanism of lysosomal P2X4 by SLC17A9.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/fisiologia
Trifosfato de Adenosina/fisiologia
Lisossomos/fisiologia
Proteínas de Transporte de Nucleotídeos/fisiologia
Receptores Purinérgicos P2X4/fisiologia
[Mh] Termos MeSH secundário: Animais
Células COS
Linhagem Celular
Cercopithecus aethiops
Técnicas de Silenciamento de Genes
Camundongos
Proteínas de Transporte de Nucleotídeos/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nucleotide Transport Proteins); 0 (Receptors, Purinergic P2X4); 0 (Slc17a9 protein, mouse); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.1.- (Adenosine Triphosphatases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170829
[Lr] Data última revisão:
170829
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160802
[St] Status:MEDLINE
[do] DOI:10.1113/JP271893


  6 / 213 MEDLINE  
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[PMID]:27046251
[Au] Autor:Aizawa S; Fujiwara Y; Contu VR; Hase K; Takahashi M; Kikuchi H; Kabuta C; Wada K; Kabuta T
[Ad] Endereço:a Department of Degenerative Neurological Diseases , National Institute of Neuroscience, National Center of Neurology and Psychiatry , Kodaira , Tokyo , Japan.
[Ti] Título:Lysosomal putative RNA transporter SIDT2 mediates direct uptake of RNA by lysosomes.
[So] Source:Autophagy;12(3):565-78, 2016.
[Is] ISSN:1554-8635
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lysosomes are thought to be the major intracellular compartment for the degradation of macromolecules. We recently identified a novel type of autophagy, RNautophagy, where RNA is directly taken up by lysosomes in an ATP-dependent manner and degraded. However, the mechanism of RNA translocation across the lysosomal membrane and the physiological role of RNautophagy remain unclear. In the present study, we performed gain- and loss-of-function studies with isolated lysosomes, and found that SIDT2 (SID1 transmembrane family, member 2), an ortholog of the Caenorhabditis elegans putative RNA transporter SID-1 (systemic RNA interference deficient-1), mediates RNA translocation during RNautophagy. We also observed that SIDT2 is a transmembrane protein, which predominantly localizes to lysosomes. Strikingly, knockdown of Sidt2 inhibited up to ˜50% of total RNA degradation at the cellular level, independently of macroautophagy. Moreover, we showed that this impairment is mainly due to inhibition of lysosomal RNA degradation, strongly suggesting that RNautophagy plays a significant role in constitutive cellular RNA degradation. Our results provide a novel insight into the mechanisms of RNA metabolism, intracellular RNA transport, and atypical types of autophagy.
[Mh] Termos MeSH primário: Lisossomos/metabolismo
Proteínas de Membrana/metabolismo
Proteínas de Transporte de Nucleotídeos/metabolismo
Transporte de RNA
RNA/metabolismo
[Mh] Termos MeSH secundário: Animais
Autofagia
Técnicas de Silenciamento de Genes
Células HeLa
Seres Humanos
Proteína 2 de Membrana Associada ao Lisossomo/metabolismo
Camundongos
Ligação Proteica
Estabilidade de RNA
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lysosomal-Associated Membrane Protein 2); 0 (Membrane Proteins); 0 (Nucleotide Transport Proteins); 0 (SIDT2 protein, human); 0 (Sidt2 protein, mouse); 63231-63-0 (RNA)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160406
[St] Status:MEDLINE
[do] DOI:10.1080/15548627.2016.1145325


  7 / 213 MEDLINE  
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[PMID]:26981769
[Au] Autor:Gehre L; Gorgette O; Perrinet S; Prevost MC; Ducatez M; Giebel AM; Nelson DE; Ball SG; Subtil A
[Ad] Endereço:Unité de Biologie cellulaire de l'infection microbienne, Institut Pasteur, Paris, France.
[Ti] Título:Sequestration of host metabolism by an intracellular pathogen.
[So] Source:Elife;5:e12552, 2016 Mar 16.
[Is] ISSN:2050-084X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:For intracellular pathogens, residence in a vacuole provides a shelter against cytosolic host defense to the cost of limited access to nutrients. The human pathogen Chlamydia trachomatis grows in a glycogen-rich vacuole. How this large polymer accumulates there is unknown. We reveal that host glycogen stores shift to the vacuole through two pathways: bulk uptake from the cytoplasmic pool, and de novo synthesis. We provide evidence that bacterial glycogen metabolism enzymes are secreted into the vacuole lumen through type 3 secretion. Our data bring strong support to the following scenario: bacteria co-opt the host transporter SLC35D2 to import UDP-glucose into the vacuole, where it serves as substrate for de novo glycogen synthesis, through a remarkable adaptation of the bacterial glycogen synthase. Based on these findings we propose that parasitophorous vacuoles not only offer protection but also provide a microorganism-controlled metabolically active compartment essential for redirecting host resources to the pathogens.
[Mh] Termos MeSH primário: Chlamydia trachomatis/crescimento & desenvolvimento
Chlamydia trachomatis/metabolismo
Glicogênio Sintase/metabolismo
Glicogênio/metabolismo
Interações Hospedeiro-Patógeno
Vacúolos/química
Vacúolos/microbiologia
[Mh] Termos MeSH secundário: Animais
Proteínas de Bactérias/metabolismo
Proteínas de Bactérias/secreção
Transporte Biológico
Linhagem Celular
Glicogênio Sintase/secreção
Seres Humanos
Proteínas de Transporte de Nucleotídeos/metabolismo
Uridina Difosfato Glucose/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Nucleotide Transport Proteins); 0 (SLC35D2 protein, human); 9005-79-2 (Glycogen); EC 2.4.1.11 (Glycogen Synthase); V50K1D7P4Y (Uridine Diphosphate Glucose)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160317
[St] Status:MEDLINE


  8 / 213 MEDLINE  
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[PMID]:26601946
[Au] Autor:Fenyk S; Dixon CH; Gittens WH; Townsend PD; Sharples GJ; Pålsson LO; Takken FL; Cann MJ
[Ad] Endereço:From the School of Biological and Biomedical Sciences, the Biophysical Sciences Institute, and.
[Ti] Título:The Tomato Nucleotide-binding Leucine-rich Repeat Immune Receptor I-2 Couples DNA-binding to Nucleotide-binding Domain Nucleotide Exchange.
[So] Source:J Biol Chem;291(3):1137-47, 2016 Jan 15.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Plant nucleotide-binding leucine-rich repeat (NLR) proteins enable plants to recognize and respond to pathogen attack. Previously, we demonstrated that the Rx1 NLR of potato is able to bind and bend DNA in vitro. DNA binding in situ requires its genuine activation following pathogen perception. However, it is unknown whether other NLR proteins are also able to bind DNA. Nor is it known how DNA binding relates to the ATPase activity intrinsic to NLR switch function required to immune activation. Here we investigate these issues using a recombinant protein corresponding to the N-terminal coiled-coil and nucleotide-binding domain regions of the I-2 NLR of tomato. Wild type I-2 protein bound nucleic acids with a preference of ssDNA ≈ dsDNA > ssRNA, which is distinct from Rx1. I-2 induced bending and melting of DNA. Notably, ATP enhanced DNA binding relative to ADP in the wild type protein, the null P-loop mutant K207R, and the autoactive mutant S233F. DNA binding was found to activate the intrinsic ATPase activity of I-2. Because DNA binding by I-2 was decreased in the presence of ADP when compared with ATP, a cyclic mechanism emerges; activated ATP-associated I-2 binds to DNA, which enhances ATP hydrolysis, releasing ADP-bound I-2 from the DNA. Thus DNA binding is a general property of at least a subset of NLR proteins, and NLR activation is directly linked to its activity at DNA.
[Mh] Termos MeSH primário: DNA de Cadeia Simples/metabolismo
Proteínas de Ligação a DNA/agonistas
Lycopersicon esculentum/metabolismo
Modelos Moleculares
Proteínas de Transporte de Nucleotídeos/agonistas
Proteínas de Plantas/agonistas
Proteínas/agonistas
[Mh] Termos MeSH secundário: Difosfato de Adenosina/metabolismo
Adenosina Trifosfatases/química
Adenosina Trifosfatases/genética
Adenosina Trifosfatases/metabolismo
Trifosfato de Adenosina/metabolismo
Substituição de Aminoácidos
Sítios de Ligação
Proteínas de Ligação a DNA/química
Proteínas de Ligação a DNA/genética
Proteínas de Ligação a DNA/metabolismo
Ensaio de Desvio de Mobilidade Eletroforética
Hidrólise
Lycopersicon esculentum/enzimologia
Lycopersicon esculentum/imunologia
Mutação
Proteínas de Transporte de Nucleotídeos/química
Proteínas de Transporte de Nucleotídeos/genética
Proteínas de Transporte de Nucleotídeos/metabolismo
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Imunidade Vegetal
Proteínas de Plantas/química
Proteínas de Plantas/genética
Proteínas de Plantas/metabolismo
Domínios e Motivos de Interação entre Proteínas
Proteínas/química
Proteínas/genética
Proteínas/metabolismo
RNA/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA, Single-Stranded); 0 (DNA-Binding Proteins); 0 (Nucleotide Transport Proteins); 0 (Peptide Fragments); 0 (Plant Proteins); 0 (Proteins); 0 (Recombinant Proteins); 0 (leucine-rich repeat proteins); 61D2G4IYVH (Adenosine Diphosphate); 63231-63-0 (RNA); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.1.- (Adenosine Triphosphatases)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151126
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.698589


  9 / 213 MEDLINE  
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[PMID]:26601776
[Au] Autor:Jung J; Uesugi N; Jeong NY; Park BS; Konishi H; Kiyama H
[Ad] Endereço:Department of Anatomy and Neurobiology, School of Medicine, Kyung Hee University, Heogi-Dong 1, Dongdaemun-Gu, Seoul 130-701, Republic of Korea; Core Research for Evolutional Science and Technology (CREST) of the Japan Science and Technology Agency (JST), Saitama, Japan.
[Ti] Título:Increase of transcription factor EB (TFEB) and lysosomes in rat DRG neurons and their transportation to the central nerve terminal in dorsal horn after nerve injury.
[So] Source:Neuroscience;313:10-22, 2016 Jan 28.
[Is] ISSN:1873-7544
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In the spinal dorsal horn (DH), nerve injury activates microglia and induces neuropathic pain. Several studies clarified an involvement of adenosine triphosphate (ATP) in the microglial activation. However, the origin of ATP together with the release mechanism is unclear. Recent in vitro study revealed that an ATP marker, quinacrine, in lysosomes was released from neurite terminal of dorsal root ganglion (DRG) neurons to extracellular space via lysosomal exocytosis. Here, we demonstrate a possibility that the lysosomal ingredient including ATP released from DRG neurons by lysosomal-exocytosis is an additional source of the glial activation in DH after nerve injury. After rat L5 spinal nerve ligation (SNL), mRNA for transcription factor EB (TFEB), a transcription factor controlling lysosomal activation and exocytosis, was induced in the DRG. Simultaneously both lysosomal protein, LAMP1- and vesicular nuclear transporter (VNUT)-positive vesicles were increased in L5 DRG neurons and ipsilateral DH. The quinacrine staining in DH was increased and co-localized with LAMP1 immunoreactivity after nerve injury. In DH, LAMP1-positive vesicles were also co-localized with a peripheral nerve marker, Isolectin B4 (IB4) lectin. Injection of the adenovirus encoding mCherry-LAMP1 into DRG showed that mCherry-positive lysosomes are transported to the central nerve terminal in DH. These findings suggest that activation of lysosome synthesis including ATP packaging in DRG, the central transportation of the lysosome, and subsequent its exocytosis from the central nerve terminal of DRG neurons in response to nerve injury could be a partial mechanism for activation of microglia in DH. This lysosome-mediated microglia activation mechanism may provide another clue to control nociception and pain.
[Mh] Termos MeSH primário: Fatores de Transcrição de Zíper de Leucina e Hélice-Alça-Hélix Básicos/metabolismo
Gânglios Espinais/metabolismo
Lisossomos/metabolismo
Neurônios/metabolismo
Nervos Espinhais/lesões
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Adenoviridae/genética
Animais
Modelos Animais de Doenças
Exocitose/fisiologia
Gânglios Espinais/patologia
Vetores Genéticos
Glicoproteínas/metabolismo
Lectinas/metabolismo
Vértebras Lombares
Proteínas Luminescentes/genética
Proteínas Luminescentes/metabolismo
Glicoproteínas de Membrana Associadas ao Lisossomo/genética
Glicoproteínas de Membrana Associadas ao Lisossomo/metabolismo
Masculino
Microglia/metabolismo
Neurônios/patologia
Proteínas de Transporte de Nucleotídeos/genética
Proteínas de Transporte de Nucleotídeos/metabolismo
RNA Mensageiro/metabolismo
Ratos Wistar
Nervos Espinhais/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Basic Helix-Loop-Helix Leucine Zipper Transcription Factors); 0 (Glycoproteins); 0 (Lamp1 protein, rat); 0 (Lectins); 0 (Luminescent Proteins); 0 (Lysosome-Associated Membrane Glycoproteins); 0 (Nucleotide Transport Proteins); 0 (RNA, Messenger); 0 (TFEB protein, rat); 0 (VNUT protein, rat); 0 (isolectin B4-binding glycoprotein, rat); 0 (red fluorescent protein); 8L70Q75FXE (Adenosine Triphosphate)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:151228
[Lr] Data última revisão:
151228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151126
[St] Status:MEDLINE


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[PMID]:26418963
[Au] Autor:Niemann MC; Werner T
[Ad] Endereço:a Institute of Biology/Applied Genetics; Dahlem Center of Plant Sciences (DCPS); Freie Universität Berlin ; Berlin , Germany.
[Ti] Título:Endoplasmic reticulum: Where nucleotide sugar transport meets cytokinin control mechanisms.
[So] Source:Plant Signal Behav;10(10):e1072668, 2015.
[Is] ISSN:1559-2324
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The endoplasmic reticulum (ER) is a multifunctional eukaryotic organelle where the vast majority of secretory proteins are folded and assembled to achieve their correct tertiary structures. The lumen of the ER and Golgi apparatus also provides an environment for numerous glycosylation reactions essential for modifications of proteins and lipids, and for cell wall biosynthesis. These glycosylation reactions require a constant supply of cytosolically synthesized substrate precursors, nucleotide sugars, which are transported by a group of dedicated nucleotide sugar transporters (NST). Recently, we have reported on the identification of a novel ER-localized NST protein, ROCK1, which mediates the transport of UDP-linked acetylated hexosamines across the ER membrane in Arabidopsis. Interestingly, it has been demonstrated that the activity of ROCK1 is important for the regulation of cytokinin-degrading enzymes, cytokinin oxidases/dehydrogenases (CKX), in the ER and, thus, for cytokinin responses. In this addendum we will address the biochemical and cellular activity of the ROCK1 transporter and its phylogenetic relation to other NST proteins.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/metabolismo
Proteínas de Transporte/metabolismo
Citocininas/metabolismo
Retículo Endoplasmático/metabolismo
Hexosaminas/metabolismo
Proteínas de Membrana Transportadoras/metabolismo
Nucleotídeos/metabolismo
[Mh] Termos MeSH secundário: Arabidopsis/genética
Proteínas de Arabidopsis/genética
Transporte Biológico
Proteínas de Transporte/genética
Citosol/metabolismo
Glicosilação
Complexo de Golgi/metabolismo
Proteínas de Membrana Transportadoras/genética
Proteínas de Transporte de Monossacarídeos/genética
Proteínas de Transporte de Monossacarídeos/metabolismo
Proteínas de Transporte de Nucleotídeos/genética
Proteínas de Transporte de Nucleotídeos/metabolismo
Filogenia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Carrier Proteins); 0 (Cytokinins); 0 (Hexosamines); 0 (Membrane Transport Proteins); 0 (Monosaccharide Transport Proteins); 0 (Nucleotide Transport Proteins); 0 (Nucleotides); 0 (ROCK1 protein, Arabidopsis)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150930
[St] Status:MEDLINE
[do] DOI:10.1080/15592324.2015.1072668



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