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  1 / 1352 MEDLINE  
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[PMID]:29284612
[Au] Autor:Lowenstein CJ
[Ad] Endereço:UNIVERSITY OF ROCHESTER SCHOOL OF MEDICINE AND DENTISTRY.
[Ti] Título:VAMP-3 mediates platelet endocytosis.
[So] Source:Blood;130(26):2816-2818, 2017 12 28.
[Is] ISSN:1528-0020
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Plaquetas
Endocitose
[Mh] Termos MeSH secundário: Seres Humanos
Proteínas R-SNARE
[Pt] Tipo de publicação:JOURNAL ARTICLE; COMMENT
[Nm] Nome de substância:
0 (R-SNARE Proteins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180118
[Lr] Data última revisão:
180118
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:171230
[St] Status:MEDLINE
[do] DOI:10.1182/blood-2017-10-808576


  2 / 1352 MEDLINE  
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[PMID]:29065163
[Au] Autor:Gao H; He F; Lin X; Wu Y
[Ad] Endereço:School of Life Sciences, University of Science and Technology of China, Hefei, China.
[Ti] Título:Drosophila VAMP7 regulates Wingless intracellular trafficking.
[So] Source:PLoS One;12(10):e0186938, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Drosophila Wingless (Wg) is a morphogen that determines cell fate during development. Previous studies have shown that endocytic pathways regulate Wg trafficking and signaling. Here, we showed that loss of vamp7, a gene required for vesicle fusion, dramatically increased Wg levels and decreased Wg signaling. Interestingly, we found that levels of Dally-like (Dlp), a glypican that can interact with Wg to suppress Wg signaling at the dorsoventral boundary of the Drosophila wing, were also increased in vamp7 mutant cells. Moreover, Wg puncta in Rab4-dependent recycling endosomes were Dlp positive. We hypothesize that VAMP7 is required for Wg intracellular trafficking and the accumulation of Wg in Rab4-dependent recycling endosomes might affect Wg signaling.
[Mh] Termos MeSH primário: Proteínas de Drosophila/metabolismo
Proteínas de Drosophila/fisiologia
Drosophila/genética
Proteínas R-SNARE/fisiologia
Proteína Wnt1/metabolismo
[Mh] Termos MeSH secundário: Animais
Transporte Biológico
Proteínas de Drosophila/genética
Proteínas R-SNARE/genética
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (R-SNARE Proteins); 0 (VAMP7 protein, Drosophila); 0 (Wnt1 Protein); 0 (wg protein, Drosophila)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171025
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186938


  3 / 1352 MEDLINE  
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[PMID]:28827281
[Au] Autor:Arnold MG; Adhikari P; Kang B; Xu 徐昊 H
[Ad] Endereço:Department of Biological Sciences, University of Southern Mississippi, 118 College Drive, #5018, Hattiesburg, Mississippi 39406, U.S.A.
[Ti] Título:Munc18a clusters SNARE-bearing liposomes prior to -SNARE zippering.
[So] Source:Biochem J;474(19):3339-3354, 2017 Sep 24.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Sec1-Munc18 (SM) proteins co-operate with SNAREs {SNAP [soluble NSF ( -ethylmaleimide-sensitive factor) attachment protein] receptors} to mediate membrane fusion in eukaryotic cells. Studies of Munc18a/Munc18-1/Stxbp1 in neurotransmission suggest that SM proteins accelerate fusion kinetics primarily by activating the partially zippered -SNARE complex. However, accumulating evidence has argued for additional roles for SM proteins in earlier steps in the fusion cascade. Here, we investigate the function of Munc18a in reconstituted exocytic reactions mediated by neuronal and non-neuronal SNAREs. We show that Munc18a plays a direct role in promoting proteoliposome clustering, underlying vesicle docking during exocytosis. In the three different fusion reactions examined, Munc18a-dependent clustering requires an intact N-terminal peptide (N-peptide) motif in syntaxin that mediates the binary interaction between syntaxin and Munc18a. Importantly, clustering is preserved under inhibitory conditions that abolish both -SNARE complex formation and lipid mixing, indicating that Munc18a promotes membrane clustering in a step that is independent of -SNARE zippering and activation.
[Mh] Termos MeSH primário: Lipossomos/metabolismo
Proteínas Munc18/química
Proteínas Munc18/metabolismo
Proteínas SNARE/metabolismo
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Animais
Exocitose
Lipossomos/química
Fusão de Membrana
Proteínas Munc18/genética
Proteínas Qa-SNARE/química
Proteínas Qa-SNARE/metabolismo
Proteínas R-SNARE/genética
Proteínas R-SNARE/metabolismo
Ratos
Proteínas SNARE/genética
Proteína 25 Associada a Sinaptossoma/genética
Proteína 25 Associada a Sinaptossoma/metabolismo
Proteína 2 Associada à Membrana da Vesícula/genética
Proteína 2 Associada à Membrana da Vesícula/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Liposomes); 0 (Munc18 Proteins); 0 (Qa-SNARE Proteins); 0 (R-SNARE Proteins); 0 (SNARE Proteins); 0 (Snap25 protein, rat); 0 (Synaptosomal-Associated Protein 25); 0 (Vamp2 protein, rat); 0 (Vamp8 protein, rat); 0 (Vesicle-Associated Membrane Protein 2)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171025
[Lr] Data última revisão:
171025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170823
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20170494


  4 / 1352 MEDLINE  
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[PMID]:28663435
[Au] Autor:Alloatti A; Rookhuizen DC; Joannas L; Carpier JM; Iborra S; Magalhaes JG; Yatim N; Kozik P; Sancho D; Albert ML; Amigorena S
[Ad] Endereço:INSERM U932, PSL Research University, Institut Curie, Paris, France.
[Ti] Título:Critical role for Sec22b-dependent antigen cross-presentation in antitumor immunity.
[So] Source:J Exp Med;214(8):2231-2241, 2017 Aug 07.
[Is] ISSN:1540-9538
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:CD8 T cells mediate antigen-specific immune responses that can induce rejection of solid tumors. In this process, dendritic cells (DCs) are thought to take up tumor antigens, which are processed into peptides and loaded onto MHC-I molecules, a process called "cross-presentation." Neither the actual contribution of cross-presentation to antitumor immune responses nor the intracellular pathways involved in vivo are clearly established because of the lack of experimental tools to manipulate this process. To develop such tools, we generated mice bearing a conditional DC-specific mutation in the gene, a critical regulator of endoplasmic reticulum-phagosome traffic required for cross-presentation. DCs from these mice show impaired cross-presentation ex vivo and defective cross-priming of CD8 T cell responses in vivo. These mice are also defective for antitumor immune responses and are resistant to treatment with anti-PD-1. We conclude that Sec22b-dependent cross-presentation in DCs is required to initiate CD8 T cell responses to dead cells and to induce effective antitumor immune responses during anti-PD-1 treatment in mice.
[Mh] Termos MeSH primário: Apresentação Cruzada/imunologia
Neoplasias/imunologia
Proteínas R-SNARE/fisiologia
[Mh] Termos MeSH secundário: Animais
Linfócitos T CD8-Positivos/imunologia
Linfócitos T CD8-Positivos/fisiologia
Morte Celular/imunologia
Células Dendríticas/imunologia
Feminino
Imunidade Celular/imunologia
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Camundongos Transgênicos
Proteínas R-SNARE/genética
Células RAW 264.7
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (R-SNARE Proteins); 0 (Sec22b protein, mouse)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170701
[St] Status:MEDLINE
[do] DOI:10.1084/jem.20170229


  5 / 1352 MEDLINE  
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[PMID]:28508576
[Au] Autor:Buaillon C; Guerrero NA; Cebrian I; Blanié S; Lopez J; Bassot E; Vasseur V; Santi-Rocca J; Blanchard N
[Ad] Endereço:Centre de Physiopathologie Toulouse Purpan (CPTP), INSERM, CNRS, Université de Toulouse, UPS, Toulouse, France.
[Ti] Título:MHC I presentation of Toxoplasma gondii immunodominant antigen does not require Sec22b and is regulated by antigen orientation at the vacuole membrane.
[So] Source:Eur J Immunol;47(7):1160-1170, 2017 Jul.
[Is] ISSN:1521-4141
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The intracellular Toxoplasma gondii parasite replicates within a parasitophorous vacuole (PV). T. gondii secretes proteins that remain soluble in the PV space, are inserted into PV membranes or are exported beyond the PV boundary. In addition to supporting T. gondii growth, these proteins can be processed and presented by MHC I for CD8 T-cell recognition. Yet it is unclear whether membrane binding influences the processing pathways employed and if topology of membrane antigens impacts their MHC I presentation. Here we report that the MHC I pathways of soluble and membrane-bound antigens differ in their requirement for host ER recruitment. In contrast to the soluble SAG1-OVA model antigen, we find that presentation of the membrane-bound GRA6 is independent from the SNARE Sec22b, a key molecule for transfer of host endoplasmic reticulum components onto the PV. Using parasites modified to secrete a transmembrane antigen with opposite orientations, we further show that MHC I presentation is highly favored when the C-terminal epitope is exposed to the host cell cytosol, which corresponds to GRA6 natural orientation. Our data suggest that the biochemical properties of antigens released by intracellular pathogens critically guide their processing pathway and are valuable parameters to consider for vaccination strategies.
[Mh] Termos MeSH primário: Apresentação do Antígeno
Antígenos de Protozoários/imunologia
Antígenos de Histocompatibilidade Classe I
Proteínas de Protozoários/imunologia
Proteínas R-SNARE/metabolismo
Toxoplasma/imunologia
[Mh] Termos MeSH secundário: Animais
Antígenos de Protozoários/química
Linfócitos T CD8-Positivos/imunologia
Citosol/imunologia
Citosol/parasitologia
Células Dendríticas/imunologia
Epitopos Imunodominantes
Camundongos
Proteínas de Protozoários/química
Toxoplasma/química
Vacúolos/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, Protozoan); 0 (GRA6 protein, Toxoplasma gondii); 0 (Histocompatibility Antigens Class I); 0 (Immunodominant Epitopes); 0 (Protozoan Proteins); 0 (R-SNARE Proteins); 0 (Sec22b protein, mouse)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170927
[Lr] Data última revisão:
170927
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170517
[St] Status:MEDLINE
[do] DOI:10.1002/eji.201646859


  6 / 1352 MEDLINE  
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[PMID]:28483813
[Au] Autor:Jakhanwal S; Lee CT; Urlaub H; Jahn R
[Ad] Endereço:Department of Neurobiology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
[Ti] Título:An activated Q-SNARE/SM protein complex as a possible intermediate in SNARE assembly.
[So] Source:EMBO J;36(12):1788-1802, 2017 Jun 14.
[Is] ISSN:1460-2075
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Assembly of the SNARE proteins syntaxin1, SNAP25, and synaptobrevin into a SNARE complex is essential for exocytosis in neurons. For efficient assembly, SNAREs interact with additional proteins but neither the nature of the intermediates nor the sequence of protein assembly is known. Here, we have characterized a ternary complex between syntaxin1, SNAP25, and the SM protein Munc18-1 as a possible acceptor complex for the R-SNARE synaptobrevin. The ternary complex binds synaptobrevin with fast kinetics, resulting in the rapid formation of a fully zippered SNARE complex to which Munc18-1 remains tethered by the N-terminal domain of syntaxin1. Intriguingly, only one of the synaptobrevin truncation mutants (Syb1-65) was able to bind to the syntaxin1:SNAP25:Munc18-1 complex, suggesting either a cooperative zippering mechanism that proceeds bidirectionally or the progressive R-SNARE binding via an SM template. Moreover, the complex is resistant to disassembly by NSF Based on these findings, we consider the ternary complex as a strong candidate for a physiological intermediate in SNARE assembly.
[Mh] Termos MeSH primário: Proteínas Munc18/metabolismo
Multimerização Proteica
Proteínas R-SNARE/metabolismo
Proteína 25 Associada a Sinaptossoma/metabolismo
Sintaxina 1/metabolismo
[Mh] Termos MeSH secundário: Animais
Camundongos
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Munc18 Proteins); 0 (R-SNARE Proteins); 0 (Snap25 protein, mouse); 0 (Stxbp1 protein, mouse); 0 (Synaptosomal-Associated Protein 25); 0 (Syntaxin 1)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170717
[Lr] Data última revisão:
170717
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170510
[St] Status:MEDLINE
[do] DOI:10.15252/embj.201696270


  7 / 1352 MEDLINE  
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[PMID]:28414125
[Au] Autor:Yamamoto Y; Yurugi C; Sakisaka T
[Ad] Endereço:Division of Membrane Dynamics, Department of Physiology and Cell Biology, Kobe University Graduate School of Medicine, Kobe 650-0017, Japan.
[Ti] Título:The number of the C-terminal transmembrane domains has the potency to specify subcellular localization of Sec22c.
[So] Source:Biochem Biophys Res Commun;487(2):388-395, 2017 May 27.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sec22c has been characterized as an endoplasmic reticulum (ER)-localized transmembrane protein involved in regulation of the vesicle transport between the ER and the Golgi. Sec22c has several isoforms generated by alternative splicing that changes the number of the C-terminal transmembrane domains (TMDs). However, the physiological significance of the splicing remains unknown. Here we show that the splicing isoforms containing four TMDs unexpectedly localized at cis-Golgi, whereas the splicing isoforms containing less than four TMDs localized at the ER. The C-terminal fragment containing the four TMDs was sufficient for the cis-Golgi localization and bound to ADP-ribosylation factor 4 (ARF4). ARF4 knockdown and overexpression of a constitutively active mutant of ARF4 decreased the cis-Golgi localization of the C-terminal fragment and the full-length protein, respectively. These results indicate that the splicing-dependent changes in the number of TMDs allow Sec22c to regulate the subcellular localization in cooperation with ARF4, implying that Sec22c will function at the Golgi as well as the ER.
[Mh] Termos MeSH primário: Membrana Celular/metabolismo
Retículo Endoplasmático/metabolismo
Complexo de Golgi/metabolismo
Proteínas R-SNARE/química
Proteínas R-SNARE/metabolismo
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
Retículo Endoplasmático/química
Complexo de Golgi/química
Células HeLa
Seres Humanos
Ligação Proteica
Frações Subcelulares
Distribuição Tecidual
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (R-SNARE Proteins); 0 (Saccharomyces cerevisiae Proteins); 0 (Sec22 protein, S cerevisiae)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170619
[Lr] Data última revisão:
170619
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170418
[St] Status:MEDLINE


  8 / 1352 MEDLINE  
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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


  9 / 1352 MEDLINE  
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[PMID]:28242757
[Au] Autor:Messenger SW; Jones EK; Holthaus CL; Thomas DDH; Cooley MM; Byrne JA; Mareninova OA; Gukovskaya AS; Groblewski GE
[Ad] Endereço:From the Department of Nutritional Sciences, University of Wisconsin, Madison, Wisconsin 53706.
[Ti] Título:Acute acinar pancreatitis blocks vesicle-associated membrane protein 8 (VAMP8)-dependent secretion, resulting in intracellular trypsin accumulation.
[So] Source:J Biol Chem;292(19):7828-7839, 2017 May 12.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Zymogen secretory granules in pancreatic acinar cells express two vesicle-associated membrane proteins (VAMP), VAMP2 and -8, each controlling 50% of stimulated secretion. Analysis of secretion kinetics identified a first phase (0-2 min) mediated by VAMP2 and second (2-10 min) and third phases (10-30 min) mediated by VAMP8. Induction of acinar pancreatitis by supramaximal cholecystokinin (CCK-8) stimulation inhibits VAMP8-mediated mid- and late-phase but not VAMP2-mediated early-phase secretion. Elevation of cAMP during supramaximal CCK-8 mitigates third-phase secretory inhibition and acinar damage caused by the accumulation of prematurely activated trypsin. VAMP8 acini are resistant to secretory inhibition by supramaximal CCK-8, and despite a 4.5-fold increase in total cellular trypsinogen levels, are fully protected from intracellular trypsin accumulation and acinar damage. VAMP8-mediated secretion is dependent on expression of the early endosomal proteins Rab5, D52, and EEA1. Supramaximal CCK-8 (60 min) caused a 60% reduction in the expression of D52 followed by Rab5 and EEA1 in isolated acini and in The loss of D52 occurred as a consequence of its entry into autophagic vacuoles and was blocked by lysosomal cathepsin B and L inhibition. Accordingly, adenoviral overexpression of Rab5 or D52 enhanced secretion in response to supramaximal CCK-8 and prevented accumulation of activated trypsin. These data support that acute inhibition of VAMP8-mediated secretion during pancreatitis triggers intracellular trypsin accumulation and loss of the early endosomal compartment. Maintaining anterograde endosomal trafficking during pancreatitis maintains VAMP8-dependent secretion, thereby preventing accumulation of activated trypsin.
[Mh] Termos MeSH primário: Pancreatite/metabolismo
Proteínas R-SNARE/metabolismo
Tripsina/química
[Mh] Termos MeSH secundário: Animais
Endossomos/metabolismo
Feminino
Cinética
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Pâncreas/metabolismo
Ratos
Ratos Sprague-Dawley
Tripsinogênio/química
Proteínas de Transporte Vesicular/metabolismo
Proteínas rab5 de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (D52 protein, rat); 0 (R-SNARE Proteins); 0 (Vamp8 protein, mouse); 0 (Vamp8 protein, rat); 0 (Vesicular Transport Proteins); 0 (early endosome antigen 1); 9002-08-8 (Trypsinogen); EC 3.4.21.4 (Trypsin); EC 3.6.5.2 (rab5 GTP-Binding Proteins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170908
[Lr] Data última revisão:
170908
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170301
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.781815


  10 / 1352 MEDLINE  
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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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