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Pesquisa : D12.776.543.990.812 [Categoria DeCS]
Referências encontradas : 352 [refinar]
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[PMID]:28403141
[Au] Autor:Gordon DE; Chia J; Jayawardena K; Antrobus R; Bard F; Peden AA
[Ad] Endereço:University of California San Francisco, Department of Cellular and Molecular Pharmacology, San Francisco, CA, United States of America.
[Ti] Título:VAMP3/Syb and YKT6 are required for the fusion of constitutive secretory carriers with the plasma membrane.
[So] Source:PLoS Genet;13(4):e1006698, 2017 Apr.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The cellular machinery required for the fusion of constitutive secretory vesicles with the plasma membrane in metazoans remains poorly defined. To address this problem we have developed a powerful, quantitative assay for measuring secretion and used it in combination with combinatorial gene depletion studies in Drosophila cells. This has allowed us to identify at least three SNARE complexes mediating Golgi to PM transport (STX1, SNAP24/29 and Syb; STX1, SNAP24/29 and YKT6; STX4, SNAP24 and Syb). RNAi mediated depletion of YKT6 and VAMP3 in mammalian cells also blocks constitutive secretion suggesting that YKT6 has an evolutionarily conserved role in this process. The unexpected role of YKT6 in plasma membrane fusion may in part explain why RNAi and gene disruption studies have failed to produce the expected phenotypes in higher eukaryotes.
[Mh] Termos MeSH primário: Membrana Celular/genética
Proteínas de Drosophila/genética
Proteínas R-SNARE/genética
Proteínas SNARE/genética
Proteína 3 Associada à Membrana da Vesícula/genética
[Mh] Termos MeSH secundário: Animais
Membrana Celular/metabolismo
Proteínas de Drosophila/metabolismo
Drosophila melanogaster/genética
Drosophila melanogaster/metabolismo
Complexo de Golgi/genética
Complexo de Golgi/metabolismo
Heterozigoto
Seres Humanos
Fusão de Membrana/genética
Transporte Proteico/genética
Proteínas R-SNARE/metabolismo
Interferência de RNA
Proteínas SNARE/metabolismo
Toxina Shiga I/genética
Toxina Shiga I/metabolismo
Proteínas de Ligação a Fator Solúvel Sensível a N-Etilmaleimida/genética
Proteínas de Ligação a Fator Solúvel Sensível a N-Etilmaleimida/metabolismo
Proteína 3 Associada à Membrana da Vesícula/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (R-SNARE Proteins); 0 (SNARE Proteins); 0 (Shiga Toxin 1); 0 (Snap24 protein, Drosophila); 0 (Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins); 0 (Vesicle-Associated Membrane Protein 3); 0 (synaptobrevin protein, Drosophila)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170530
[Lr] Data última revisão:
170530
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170414
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006698


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[PMID]:28359759
[Au] Autor:Lechuga S; Naydenov NG; Feygin A; Jimenez AJ; Ivanov AI
[Ad] Endereço:Department of Human and Molecular Genetics, Virginia Commonwealth University, Richmond, VA 23298, USA.
[Ti] Título:A vesicle trafficking protein αSNAP regulates Paneth cell differentiation in vivo.
[So] Source:Biochem Biophys Res Commun;486(4):951-957, 2017 May 13.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A soluble N-ethylmaleimide-sensitive factor-attachment protein alpha (αSNAP) is a multifunctional scaffolding protein that regulates intracellular vesicle trafficking and signaling. In cultured intestinal epithelial cells, αSNAP has been shown to be essential for cell survival, motility, and adhesion; however, its physiologic functions in the intestinal mucosa remain unknown. In the present study, we used a mouse with a spontaneous hydrocephalus with hop gait (hyh) mutation of αSNAP to examine the roles of this trafficking protein in regulating intestinal epithelial homeostasis in vivo. Homozygous hyh mice demonstrated decreased expression of αSNAP protein in the intestinal epithelium, but did not display gross abnormalities of epithelial architecture in the colon and ileum. Such αSNAP depletion attenuated differentiation of small intestinal epithelial enteroids ex vivo. Furthermore, αSNAP-deficient mutant animals displayed reduced formation of lysozyme granules in small intestinal crypts and decreased expression of lysozyme and defensins in the intestinal mucosa, which is indicative of defects in Paneth cell differentiation. By contrast, development of Goblet cells, enteroendocrine cells, and assembly of enterocyte apical junctions was not altered in hyh mutant mice. Our data revealed a novel role of αSNAP in the intestinal Paneth cell differentiation in vivo.
[Mh] Termos MeSH primário: Diferenciação Celular/fisiologia
Celulas de Paneth/citologia
Celulas de Paneth/metabolismo
Proteínas de Ligação a Fator Solúvel Sensível a N-Etilmaleimida/metabolismo
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Feminino
Masculino
Camundongos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170621
[Lr] Data última revisão:
170621
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170401
[St] Status:MEDLINE


  3 / 352 MEDLINE  
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[PMID]:28292915
[Au] Autor:Wickner W; Rizo J
[Ad] Endereço:Department of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Hanover, NH 03755 Bill.Wickner@Dartmouth.edu) Jose.Rizo-Rey@UTSouthwestern.edu.
[Ti] Título:A cascade of multiple proteins and lipids catalyzes membrane fusion.
[So] Source:Mol Biol Cell;28(6):707-711, 2017 Mar 15.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recent studies suggest revisions to the SNARE paradigm of membrane fusion. Membrane tethers and/or SNAREs recruit proteins of the Sec 1/Munc18 family to catalyze SNARE assembly into -complexes. SNARE-domain zippering draws the bilayers into immediate apposition and provides a platform to position fusion triggers such as Sec 17/α-SNAP and/or synaptotagmin, which insert their apolar "wedge" domains into the bilayers, initiating the lipid rearrangements of fusion.
[Mh] Termos MeSH primário: Proteínas SNARE/metabolismo
Proteínas SNARE/fisiologia
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Lipídeos
Fusão de Membrana/fisiologia
Proteínas de Membrana/metabolismo
Proteínas Munc18/metabolismo
Proteínas Munc18/fisiologia
Ligação Proteica
Proteínas de Ligação a Fator Solúvel Sensível a N-Etilmaleimida
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Lipids); 0 (Membrane Proteins); 0 (Munc18 Proteins); 0 (SNARE Proteins); 0 (Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170316
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E16-07-0517


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[PMID]:28202687
[Au] Autor:Dingjan I; Linders PT; van den Bekerom L; Baranov MV; Halder P; Ter Beest M; van den Bogaart G
[Ad] Endereço:Department of Tumor Immunology, Radboud Institute for Molecular Life Sciences, Radboud University Medical Center, Nijmegen 6525 GA, The Netherlands.
[Ti] Título:Oxidized phagosomal NOX2 complex is replenished from lysosomes.
[So] Source:J Cell Sci;130(7):1285-1298, 2017 Apr 01.
[Is] ISSN:1477-9137
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In dendritic cells, the NADPH oxidase 2 complex (NOX2) is recruited to the phagosomal membrane during antigen uptake. NOX2 produces reactive oxygen species (ROS) in the lumen of the phagosome that kill ingested pathogens, delay antigen breakdown and alter the peptide repertoire for presentation to T cells. How the integral membrane component of NOX2, cytochrome (which comprises CYBB and CYBA), traffics to phagosomes is incompletely understood. In this study, we show in dendritic cells derived from human blood-isolated monocytes that cytochrome is initially recruited to the phagosome from the plasma membrane during phagosome formation. Cytochrome also traffics from a lysosomal pool to phagosomes and this is required to replenish oxidatively damaged NOX2. We identified syntaxin-7, SNAP23 and VAMP8 as the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins mediating this process. Our data describe a key mechanism of how dendritic cells sustain ROS production after antigen uptake that is required to initiate T cell responses.
[Mh] Termos MeSH primário: Lisossomos/metabolismo
Glicoproteínas de Membrana/metabolismo
NADPH Oxidases/metabolismo
Fagossomos/metabolismo
[Mh] Termos MeSH secundário: Compartimento Celular
Membrana Celular/metabolismo
Grupo dos Citocromos b/metabolismo
Endossomos/metabolismo
Técnicas de Silenciamento de Genes
Seres Humanos
Membranas Intracelulares/metabolismo
Proteína 1 de Membrana Associada ao Lisossomo/metabolismo
Modelos Biológicos
NADPH Oxidase 2
Oxirredução
Fosfatidilinositóis/metabolismo
Proteínas Qa-SNARE
Proteínas Qb-SNARE/metabolismo
Proteínas Qc-SNARE/metabolismo
Proteínas R-SNARE/metabolismo
RNA Interferente Pequeno/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Proteínas de Ligação a Fator Solúvel Sensível a N-Etilmaleimida/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytochrome b Group); 0 (Lysosomal-Associated Membrane Protein 1); 0 (Membrane Glycoproteins); 0 (Phosphatidylinositols); 0 (Qa-SNARE Proteins); 0 (Qb-SNARE Proteins); 0 (Qc-SNARE Proteins); 0 (R-SNARE Proteins); 0 (RNA, Small Interfering); 0 (Reactive Oxygen Species); 0 (SNAP23 protein, human); 0 (Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins); 0 (VAMP8 protein, human); 9064-78-2 (cytochrome b558); EC 1.6.3.- (CYBB protein, human); EC 1.6.3.- (NADPH Oxidase 2); EC 1.6.3.- (NADPH Oxidases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170217
[St] Status:MEDLINE
[do] DOI:10.1242/jcs.196931


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[PMID]:28100639
[Au] Autor:Woo SS; James DJ; Martin TF
[Ad] Endereço:Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706.
[Ti] Título:Munc13-4 functions as a Ca sensor for homotypic secretory granule fusion to generate endosomal exocytic vacuoles.
[So] Source:Mol Biol Cell;28(6):792-808, 2017 Mar 15.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Munc13-4 is a Ca -dependent SNARE (soluble -ethylmaleimide-sensitive factor attachment protein receptor)- and phospholipid-binding protein that localizes to and primes secretory granules (SGs) for Ca -evoked secretion in various secretory cells. Studies in mast cell-like RBL-2H3 cells provide direct evidence that Munc13-4 with its two Ca -binding C2 domains functions as a Ca sensor for SG exocytosis. Unexpectedly, Ca stimulation also generated large (>2.4 µm in diameter) Munc13-4 /Rab7 /Rab11 endosomal vacuoles. Vacuole generation involved the homotypic fusion of Munc13-4 /Rab7 SGs, followed by a merge with Rab11 endosomes, and depended on Ca binding to Munc13-4. Munc13-4 promoted the Ca -stimulated fusion of VAMP8-containing liposomes with liposomes containing exocytic or endosomal Q-SNAREs and directly interacted with late endosomal SNARE complexes. Thus Munc13-4 is a tethering/priming factor and Ca sensor for both heterotypic SG-plasma membrane and homotypic SG-SG fusion. Total internal reflection fluorescence microscopy imaging revealed that vacuoles were exocytic and mediated secretion of ß-hexosaminidase and cytokines accompanied by Munc13-4 diffusion onto the plasma membrane. The results provide new molecular insights into the mechanism of multigranular compound exocytosis commonly observed in various secretory cells.
[Mh] Termos MeSH primário: Proteínas/metabolismo
Proteínas/fisiologia
[Mh] Termos MeSH secundário: Animais
Cálcio/metabolismo
Proteínas de Transporte/metabolismo
Linhagem Celular
Endossomos/metabolismo
Endossomos/fisiologia
Exocitose/fisiologia
Fusão de Membrana/fisiologia
Transporte Proteico
Proteínas/genética
Ratos
Proteínas SNARE/metabolismo
Vesículas Secretórias/fisiologia
Proteínas de Ligação a Fator Solúvel Sensível a N-Etilmaleimida/metabolismo
Vacúolos/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Proteins); 0 (SNARE Proteins); 0 (Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins); 0 (Unc13h4 protein, rat); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170120
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E16-08-0617


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[PMID]:27816473
[Au] Autor:Li X; Shi S; Li FF; Cheng R; Han Y; Diao LW; Zhang Q; Zhi JX; Liu SL
[Ad] Endereço:Systemomics Center, College of Pharmacy, and Genomics Research Center (State-Province Key Laboratories of Biomedicine-Pharmaceutics of China), Harbin Medical University, Harbin, China; Translational Medicine Research and Cooperation Center of Northern China, Heilongjiang Academy of Medical Sciences,
[Ti] Título:Characterization of soluble N-ethylmaleimide-sensitive factor attachment protein receptor gene STX18 variations for possible roles in congenital heart diseases.
[So] Source:Gene;598:79-83, 2017 Jan 20.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Congenital heart disease (CHD) is among the most prevalent and complex congenital anatomic malformations in newborns. Interactions of cardiac progenitor with a broad range of cellular regulatory factors play key roles in the formation of mammalian heart and pathogenesis of CHD. STX18 is a soluble N-ethylmaleimide-sensitive factor attachment protein receptor, which is involved in numeral cellular activities such as organelle assembly and the cell cycle. The aim of this work was to find evidence on whether STX18 variations might be associated with CHD in Chinese Han populations. We evaluated SNPs rs2044, rs33952588, rs61740788, rs12504020 and rs12644497, which are located within the exon or intron sequences of the STX18 gene, for 310 Chinese Han CHD patients and 400 non-CHD controls. Using SPSS software (version 19.0) and the online software OEGE, we conducted statistical analyses and Hardy-Weinberg equilibrium test, respectively. Among the five SNPs identified in the STX18 gene, rs33952588 and rs61740788 had very low genetic heterozygosity. In contrast, the genetic heterozygosity of the remaining three variations rs12504020 and rs12644497 near the 5'UTR and rs2044 within 3'UTR of the STX18 gene was considerably high. Analysis of associations of these genetic variations with the risk of CHD showed that rs12644497 (P value=0.017<0.05) was associated with the risk of CHD, specifically VSD and ASD, whereas rs12504020 (P value=0.560>0.05) and rs2044 (P value=0.972>0.05) were not. The SNP rs12644497 in the STX18 gene was associated with CHD in Chinese Han populations.
[Mh] Termos MeSH primário: Cardiopatias Congênitas/genética
Proteínas Qa-SNARE/genética
Proteínas de Ligação a Fator Solúvel Sensível a N-Etilmaleimida/genética
[Mh] Termos MeSH secundário: Adolescente
Adulto
Grupo com Ancestrais do Continente Asiático/genética
Estudos de Casos e Controles
Criança
Pré-Escolar
China
Grupos Étnicos/genética
Feminino
Predisposição Genética para Doença
Seres Humanos
Lactente
Masculino
Meia-Idade
Polimorfismo de Nucleotídeo Único
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Qa-SNARE Proteins); 0 (Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170201
[Lr] Data última revisão:
170201
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161107
[St] Status:MEDLINE


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[PMID]:27335124
[Au] Autor:Li P; Miao Y; Dani A; Vig M
[Ad] Endereço:Department of Pathology and Immunology, School of Medicine, Washington University in St. Louis, St. Louis, MO 63110.
[Ti] Título:α-SNAP regulates dynamic, on-site assembly and calcium selectivity of Orai1 channels.
[So] Source:Mol Biol Cell;27(16):2542-53, 2016 Aug 15.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Orai1 forms a highly calcium-selective pore of the calcium release activated channel, and α-SNAP is necessary for its function. Here we show that α-SNAP regulates on-site assembly of Orai1 dimers into calcium-selective multimers. We find that Orai1 is a dimer in resting primary mouse embryonic fibroblasts but displays variable stoichiometry in the plasma membrane of store-depleted cells. Remarkably, α-SNAP depletion induces formation of higher-order Orai1 oligomers, which permeate significant levels of sodium via Orai1 channels. Sodium permeation in α-SNAP-deficient cells cannot be corrected by tethering multiple Stim1 domains to Orai1 C-terminal tail, demonstrating that α-SNAP regulates functional assembly and calcium selectivity of Orai1 multimers independently of Stim1 levels. Fluorescence nanoscopy reveals sustained coassociation of α-SNAP with Stim1 and Orai1, and α-SNAP-depleted cells show faster and less constrained mobility of Orai1 within ER-PM junctions, suggesting Orai1 and Stim1 coentrapment without stable contacts. Furthermore, α-SNAP depletion significantly reduces fluorescence resonance energy transfer between Stim1 and Orai1 N-terminus but not C-terminus. Taken together, these data reveal a unique role of α-SNAP in the on-site functional assembly of Orai1 subunits and suggest that this process may, in part, involve enabling crucial low-affinity interactions between Orai1 N-terminus and Stim1.
[Mh] Termos MeSH primário: Proteína ORAI1/metabolismo
Proteínas de Ligação a Fator Solúvel Sensível a N-Etilmaleimida/metabolismo
[Mh] Termos MeSH secundário: Animais
Cálcio/metabolismo
Canais de Cálcio/metabolismo
Membrana Celular/metabolismo
Transferência Ressonante de Energia de Fluorescência
Células HEK293
Seres Humanos
Transporte de Íons
Proteínas de Membrana/metabolismo
Camundongos
Camundongos Endogâmicos C57BL
Ligação Proteica
Transporte Proteico
Canais de Sódio/genética
Canais de Sódio/metabolismo
Molécula 1 de Interação Estromal/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Calcium Channels); 0 (Membrane Proteins); 0 (ORAI1 Protein); 0 (Sodium Channels); 0 (Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins); 0 (Stromal Interaction Molecule 1); SY7Q814VUP (Calcium)
[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:160624
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E16-03-0163


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[PMID]:27068468
[Au] Autor:Ma L; Kang Y; Jiao J; Rebane AA; Cha HK; Xi Z; Qu H; Zhang Y
[Ad] Endereço:Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06520, USA.
[Ti] Título:α-SNAP Enhances SNARE Zippering by Stabilizing the SNARE Four-Helix Bundle.
[So] Source:Cell Rep;15(3):531-539, 2016 Apr 19.
[Is] ISSN:2211-1247
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Intracellular membrane fusion is mediated by dynamic assembly and disassembly of soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptors (SNAREs). α-SNAP guides NSF to disassemble SNARE complexes after membrane fusion. Recent experiments showed that α-SNAP also dramatically enhances SNARE assembly and membrane fusion. How α-SNAP is involved in these opposing activities is not known. Here, we examine the effect of α-SNAP on the stepwise assembly of the synaptic SNARE complex using optical tweezers. We found that α-SNAP destabilized the linker domain (LD) of the SNARE complex but stabilized its C-terminal domain (CTD) through a conformational selection mechanism. In contrast, α-SNAP minimally affected assembly of the SNARE N-terminal domain (NTD), indicating that α-SNAP barely bound the partially assembled trans-SNARE complex. Thus, α-SNAP recognizes the folded CTD for SNARE disassembly with NSF and subtly modulates membrane fusion by altering the stabilities of the SNARE CTD and LD.
[Mh] Termos MeSH primário: Proteínas SNARE/química
Proteínas SNARE/metabolismo
Proteínas de Ligação a Fator Solúvel Sensível a N-Etilmaleimida/metabolismo
[Mh] Termos MeSH secundário: Animais
Fenômenos Biomecânicos
Bovinos
Cinética
Ligação Proteica
Domínios Proteicos
Dobramento de Proteína
Estabilidade Proteica
Estrutura Secundária de Proteína
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (SNARE Proteins); 0 (Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170831
[Lr] Data última revisão:
170831
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160413
[St] Status:MEDLINE


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[PMID]:26984393
[Au] Autor:Shih YT; Hsueh YP
[Ad] Endereço:Molecular Cell Biology, Taiwan International Graduate Program, Institute of Molecular Biology, Academia Sinica, and Graduate Institute of Life Sciences, National Defense Medical Center, Taipei 115, Taiwan.
[Ti] Título:VCP and ATL1 regulate endoplasmic reticulum and protein synthesis for dendritic spine formation.
[So] Source:Nat Commun;7:11020, 2016 Mar 17.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Imbalanced protein homeostasis, such as excessive protein synthesis and protein aggregation, is a pathogenic hallmark of a range of neurological disorders. Here, using expression of mutant proteins, a knockdown approach and disease mutation knockin mice, we show that VCP (valosin-containing protein), together with its cofactor P47 and the endoplasmic reticulum (ER) morphology regulator ATL1 (Atlastin-1), regulates tubular ER formation and influences the efficiency of protein synthesis to control dendritic spine formation in neurons. Strengthening the significance of protein synthesis in dendritic spinogenesis, the translation blocker cyclohexamide and the mTOR inhibitor rapamycin reduce dendritic spine density, while a leucine supplement that increases protein synthesis ameliorates the dendritic spine defects caused by Vcp and Atl1 deficiencies. Because VCP and ATL1 are the causative genes of several neurodegenerative and neurodevelopmental disorders, we suggest that impaired ER formation and inefficient protein synthesis are significant in the pathogenesis of multiple neurological disorders.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/metabolismo
Proteínas de Ciclo Celular/metabolismo
Espinhas Dendríticas/metabolismo
Retículo Endoplasmático/metabolismo
Proteínas de Membrana/metabolismo
Biossíntese de Proteínas
[Mh] Termos MeSH secundário: Animais
Cicloeximida/farmacologia
Espinhas Dendríticas/efeitos dos fármacos
Retículo Endoplasmático/efeitos dos fármacos
Técnicas de Introdução de Genes
Técnicas de Silenciamento de Genes
Canais Iônicos/metabolismo
Leucina/farmacologia
Camundongos
Mutação/genética
Neurônios/efeitos dos fármacos
Neurônios/metabolismo
Neurônios/ultraestrutura
Biossíntese de Proteínas/efeitos dos fármacos
Proteínas/metabolismo
Proteólise/efeitos dos fármacos
Ratos
Sirolimo/farmacologia
Proteínas de Ligação a Fator Solúvel Sensível a N-Etilmaleimida/metabolismo
Sinapses/efeitos dos fármacos
Sinapses/metabolismo
Proteína com Valosina
Proteínas rab de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cell Cycle Proteins); 0 (Ion Channels); 0 (Membrane Proteins); 0 (Nsfl1c protein, rat); 0 (Proteins); 0 (Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins); 0 (Ufd1l protein, mouse); 0 (atlastin-1 protein, mouse); 98600C0908 (Cycloheximide); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.1.- (Rab10 protein, mouse); EC 3.6.4.6 (Valosin Containing Protein); EC 3.6.4.6 (Vcp protein, mouse); EC 3.6.4.6 (Vcp protein, rat); EC 3.6.5.2 (rab GTP-Binding Proteins); GMW67QNF9C (Leucine); W36ZG6FT64 (Sirolimus)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160318
[St] Status:MEDLINE
[do] DOI:10.1038/ncomms11020


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[PMID]:26566590
[Au] Autor:Stewart RJ; Ferguson DJ; Whitehead L; Bradin CH; Wu HJ; Tonkin CJ
[Ad] Endereço:The Walter and Eliza Hall Institute of Medical Research, Melbourne, 3052, Australia.
[Ti] Título:Phosphorylation of αSNAP is Required for Secretory Organelle Biogenesis in Toxoplasma gondii.
[So] Source:Traffic;17(2):102-16, 2016 Feb.
[Is] ISSN:1600-0854
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Upon infection, apicomplexan parasites quickly invade host cells and begin a replicative cycle rapidly increasing in number over a short period of time, leading to tissue lysis and disease. The secretory pathway of these highly polarized protozoan parasites tightly controls, in time and space, the biogenesis of specialized structures and organelles required for invasion and intracellular survival. In other systems, regulation of protein trafficking can occur by phosphorylation of vesicle fusion machinery. Previously, we have shown that Toxoplasma gondii αSNAP - a protein that controls the disassembly of cis-SNARE complexes--is phosphorylated. Here, we show that this post-translational modification is required for the correct function of αSNAP in controlling secretory traffic. We demonstrate that during intracellular development conditional expression of a non-phosphorylatable form of αSNAP results in Golgi fragmentation and vesiculation of all downstream secretory organelles. In addition, we show that the vestigial plastid (termed apicoplast), although reported not to be reliant on Golgi trafficking for biogenesis, is also affected upon overexpression of αSNAP and is much more sensitive to the levels of this protein than targeting to other organelles. This work highlights the importance of αSNAP and its phosphorylation in Toxoplasma organelle biogenesis and exposes a hereto fore-unexplored mechanism of regulation of vesicle fusion during secretory pathway trafficking in apicomplexan parasites.
[Mh] Termos MeSH primário: Organelas/metabolismo
Fosforilação/fisiologia
Processamento de Proteína Pós-Traducional/fisiologia
Via Secretória/fisiologia
Proteínas de Ligação a Fator Solúvel Sensível a N-Etilmaleimida/metabolismo
Toxoplasma/metabolismo
[Mh] Termos MeSH secundário: Complexo de Golgi/fisiologia
Biogênese de Organelas
Organelas/fisiologia
Transporte Proteico/fisiologia
Proteínas de Protozoários/metabolismo
Toxoplasma/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protozoan Proteins); 0 (Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151115
[St] Status:MEDLINE
[do] DOI:10.1111/tra.12348



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