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Pesquisa : A11.284.430.214.190.875.190 [Categoria DeCS]
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  1 / 1639 MEDLINE  
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[PMID]:28860114
[Au] Autor:Kopke DL; Lima SC; Alexandre C; Broadie K
[Ad] Endereço:Department of Biological Sciences, Kennedy Center for Research on Human Development, Vanderbilt University, Nashville, TN 37235, USA.
[Ti] Título:Notum coordinates synapse development via extracellular regulation of Wingless trans-synaptic signaling.
[So] Source:Development;144(19):3499-3510, 2017 10 01.
[Is] ISSN:1477-9129
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Synaptogenesis requires orchestrated communication between pre- and postsynaptic cells via coordinated trans-synaptic signaling across the extracellular synaptomatrix. The first Wnt signaling ligand discovered, Wingless (Wg; Wnt1 in mammals), plays crucial roles in synaptic development, regulating synapse architecture as well as functional differentiation. Here, we investigate synaptogenic functions of the secreted extracellular deacylase Notum, which restricts Wg signaling by cleaving an essential palmitoleate moiety. At the glutamatergic neuromuscular junction (NMJ) synapse, we find that Notum secreted from the postsynaptic muscle acts to strongly modulate synapse growth, structural architecture, ultrastructural development and functional differentiation. In null flies, we find upregulated extracellular Wg ligand and nuclear trans-synaptic signal transduction, as well as downstream misregulation of both pre- and postsynaptic molecular assembly. Structural, functional and molecular synaptogenic defects are all phenocopied by Wg overexpression, suggesting that Notum acts solely by inhibiting Wg trans-synaptic signaling. Moreover, these synaptic development phenotypes are suppressed by genetically correcting Wg levels in null mutants, indicating that Notum normally functions to coordinate synaptic structural and functional differentiation via negative regulation of Wg trans-synaptic signaling in the extracellular synaptomatrix.
[Mh] Termos MeSH primário: Proteínas de Drosophila/metabolismo
Drosophila melanogaster/metabolismo
Espaço Extracelular/metabolismo
Transdução de Sinais
Sinapses/metabolismo
Proteína Wnt1/metabolismo
[Mh] Termos MeSH secundário: Animais
Diferenciação Celular
Movimento Celular
Vesículas Citoplasmáticas/metabolismo
Vesículas Citoplasmáticas/ultraestrutura
Drosophila melanogaster/ultraestrutura
Ligantes
Músculos/metabolismo
Mutação/genética
Neuroglia/metabolismo
Junção Neuromuscular/metabolismo
Fenótipo
Sinapses/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (Ligands); 0 (Notum protein, Drosophila); 0 (Wnt1 Protein); 0 (wg protein, Drosophila)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171126
[Lr] Data última revisão:
171126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170902
[St] Status:MEDLINE
[do] DOI:10.1242/dev.148130


  2 / 1639 MEDLINE  
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[PMID]:28522593
[Au] Autor:Kakuta S; Yamaguchi J; Suzuki C; Sasaki M; Kazuno S; Uchiyama Y
[Ad] Endereço:Department of Cellular and Molecular Neuropathology, Juntendo University Graduate School of Medicine, Tokyo, Japan.
[Ti] Título:Small GTPase Rab1B is associated with ATG9A vesicles and regulates autophagosome formation.
[So] Source:FASEB J;31(9):3757-3773, 2017 Sep.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:ATG9 is a membrane protein that is essential for autophagy and is considered to be directly involved in the early steps of autophagosome formation. Yeast Atg9 is mainly localized to small vesicles (Atg9 vesicles), whereas mammalian ATG9A is reportedly localized to the -Golgi network, the endosomal compartment, and other unidentified membrane structures. To dissect the ATG9A-containing membranes, we examined the subcellular localization of ATG9A and performed immunoisolation of those membranes. ATG9A-green fluorescent protein in human culture cells was observed as numerous puncta that move rapidly throughout the cytoplasm. We isolated these cytoplasmic membranes and found that they were small vesicles that resemble the yeast Atg9 vesicle. One of the proteins obtained proteomic analyses of the mammalian ATG9A vesicle was Rab1, a small GTPase that is essential in endoplasmic reticulum-to-Golgi vesicle trafficking. Knockdown studies of Rab1B showed a suppression of autophagy. In these Rab1B-depleted cells, ATG9A accumulated in intermediate membrane structures at autophagosome formation sites. These results indicate that Rab1B is involved in regulating the proper development of autophagosomes.-Kakuta, S., Yamaguchi, J., Suzuki, C., Sasaki, M., Kazuno, S., Uchiyama, Y. Small GTPase Rab1B is associated with ATG9A vesicles and regulates autophagosome formation.
[Mh] Termos MeSH primário: Autofagossomos/fisiologia
Proteínas Relacionadas à Autofagia/metabolismo
Regulação Enzimológica da Expressão Gênica/fisiologia
Proteínas de Membrana/metabolismo
Proteínas de Transporte Vesicular/metabolismo
Proteínas rab1 de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Proteínas Relacionadas à Autofagia/genética
Membrana Celular/fisiologia
Vesículas Citoplasmáticas
Células HEK293
Células HeLa
Seres Humanos
Proteínas de Membrana/genética
Transporte Proteico
Proteínas de Transporte Vesicular/genética
Proteínas rab1 de Ligação ao GTP/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Atg9a protein, human); 0 (Autophagy-Related Proteins); 0 (Membrane Proteins); 0 (Vesicular Transport Proteins); EC 3.6.1.- (Rab1B protein, human); EC 3.6.5.2 (rab1 GTP-Binding Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170520
[St] Status:MEDLINE
[do] DOI:10.1096/fj.201601052R


  3 / 1639 MEDLINE  
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[PMID]:28433686
[Au] Autor:Eisenberg-Bord M; Schuldiner M
[Ad] Endereço:Department of Molecular Genetics, Weizmann Institute of Science, 7610001 Rehovot, Israel.
[Ti] Título:Mitochatting - If only we could be a fly on the cell wall.
[So] Source:Biochim Biophys Acta;1864(9):1469-1480, 2017 09.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Mitochondria, cellular metabolic hubs, perform many essential processes and are required for the production of metabolites such as ATP, iron-sulfur clusters, heme, amino acids and nucleotides. To fulfill their multiple roles, mitochondria must communicate with all other organelles to exchange small molecules, ions and lipids. Since mitochondria are largely excluded from vesicular trafficking routes, they heavily rely on membrane contact sites. Contact sites are areas of close proximity between organelles that allow efficient transfer of molecules, saving the need for slow and untargeted diffusion through the cytosol. More globally, multiple metabolic pathways require coordination between mitochondria and additional organelles and mitochondrial activity affects all other cellular entities and vice versa. Therefore, uncovering the different means of mitochondrial communication will allow us a better understanding of mitochondria and may illuminate disease processes that occur in the absence of proper cross-talk. In this review we focus on how mitochondria interact with all other organelles and emphasize how this communication is essential for mitochondrial and cellular homeostasis. This article is part of a Special Issue entitled: Membrane Contact Sites edited by Christian Ungermann and Benoit Kornmann.
[Mh] Termos MeSH primário: Compartimento Celular
Mitocôndrias/metabolismo
Transdução de Sinais
[Mh] Termos MeSH secundário: Animais
Vesículas Citoplasmáticas/metabolismo
Homeostase
Seres Humanos
Gotículas Lipídicas/metabolismo
Membranas Mitocondriais/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170424
[St] Status:MEDLINE


  4 / 1639 MEDLINE  
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[PMID]:28430903
[Au] Autor:Fothergill LJ; Callaghan B; Hunne B; Bravo DM; Furness JB
[Ad] Endereço:Department of Anatomy and Neuroscience, University of Melbourne, Parkville, Victoria 3010, Australia.
[Ti] Título:Costorage of Enteroendocrine Hormones Evaluated at the Cell and Subcellular Levels in Male Mice.
[So] Source:Endocrinology;158(7):2113-2123, 2017 Jul 01.
[Is] ISSN:1945-7170
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recent studies reveal complex patterns of hormone coexpression within enteroendocrine cells (EECs), contrary to the traditional view that gut hormones are expressed individually in EECs. Moreover, different hormones have been found in separate subcellular vesicles. However, detailed analysis of relative expression of multiple hormones has not been made. Subcellular studies have been confined to peptide hormones, and have not included the indolamine 5-hydroxytryptamine (5-HT) or the neuroendocrine protein chromogranin A (CgA). In the present work, coexpression of 5-HT, CgA, secretin, cholecystokinin (CCK), ghrelin, and glucagonlike peptide (GLP)-1 in mouse duodenum was quantified at a cellular and subcellular level by semiautomated cell counting and quantitative vesicle measurements. We investigated whether relative numbers of cells with colocalized hormones analyzed at a cell level matched the numbers revealed by examination of individual storage vesicles within cells. CgA and 5-HT were frequently expressed in EECs that contained combinations of GLP-1, ghrelin, secretin, and CCK. Separate subcellular stores of 5-HT, CgA, secretin, CCK, ghrelin, and GLP-1 were identified. In some cases, high-resolution analysis revealed small numbers of immunoreactive vesicles in cells dominated by a different hormone. Thus the observed incidence of cells with colocalized hormones is greater when analyzed at a subcellular, compared with a cellular, level. Subcellular analysis also showed that relative numbers of vesicles differ considerably between cells. Thus separate packaging of hormones that are colocalized is a general feature of EECs, and EECs exhibit substantial heterogeneity, including the colocalization of hormones that were formerly thought to be in cells of different lineages.
[Mh] Termos MeSH primário: Vesículas Citoplasmáticas/metabolismo
Células Enteroendócrinas/citologia
Células Enteroendócrinas/metabolismo
Hormônios Gastrointestinais/metabolismo
[Mh] Termos MeSH secundário: Animais
Colecistocinina/metabolismo
Grelina/metabolismo
Peptídeo 1 Semelhante ao Glucagon/metabolismo
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Peptídeo YY/metabolismo
Transporte Proteico
Serotonina/metabolismo
Frações Subcelulares
Distribuição Tecidual
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Gastrointestinal Hormones); 0 (Ghrelin); 106388-42-5 (Peptide YY); 333DO1RDJY (Serotonin); 89750-14-1 (Glucagon-Like Peptide 1); 9011-97-6 (Cholecystokinin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170422
[St] Status:MEDLINE
[do] DOI:10.1210/en.2017-00243


  5 / 1639 MEDLINE  
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[PMID]:28409545
[Au] Autor:Wacker MA; Teghanemt A; Weiss JP; Barker JH
[Ad] Endereço:1 Department of Biology, Central Michigan University, Mt. Pleasant, MI, USA.
[Ti] Título:High-affinity caspase-4 binding to LPS presented as high molecular mass aggregates or in outer membrane vesicles.
[So] Source:Innate Immun;23(4):336-344, 2017 May.
[Is] ISSN:1753-4267
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Caspases of the non-canonical inflammasome (caspases -4, -5, and -11) directly bind endotoxin (LOS/LPS) and can be activated in the absence of any co-factors. Models of LPS-induced caspase activation have postulated that 1:1 binding of endotoxin monomers to caspase trigger caspase oligomerization and activation, analogous to that established for endotoxin-induced activation of MD-2/TLR4. However, using metabolically radiolabeled LOS and LPS, we now show high affinity and selective binding of caspase-4 to high molecular mass aggregates of purified endotoxin and to endotoxin-rich outer membrane vesicles without formation of 1:1 endotoxin:caspase complexes. Thus, our findings demonstrate markedly different endotoxin recognition properties of caspase-4 from that of MD-2/TLR4 and strongly suggest that activation of caspase-4 (and presumably caspase-5 and caspase-11) are mediated by interactions with activating endotoxin-rich membrane interfaces rather than by endotoxin monomers.
[Mh] Termos MeSH primário: Caspases Iniciadoras/metabolismo
Vesículas Citoplasmáticas/metabolismo
Lipopolissacarídeos/metabolismo
Membranas Mitocondriais/metabolismo
Neisseria meningitidis/imunologia
Protoplastos/metabolismo
Staphylococcus aureus/imunologia
[Mh] Termos MeSH secundário: Caspases Iniciadoras/genética
Parede Celular/metabolismo
Seres Humanos
Ligação Proteica
Multimerização Proteica
Proteínas Recombinantes/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lipopolysaccharides); 0 (Recombinant Proteins); EC 3.4.22.- (CASP4 protein, human); EC 3.4.22.- (Caspases, Initiator)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170804
[Lr] Data última revisão:
170804
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170415
[St] Status:MEDLINE
[do] DOI:10.1177/1753425917695446


  6 / 1639 MEDLINE  
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[PMID]:28404749
[Au] Autor:Schneider F; Waithe D; Clausen MP; Galiani S; Koller T; Ozhan G; Eggeling C; Sezgin E
[Ad] Endereço:MRC Human Immunology Unit, University of Oxford, Oxford OX39DS, United Kingdom.
[Ti] Título:Diffusion of lipids and GPI-anchored proteins in actin-free plasma membrane vesicles measured by STED-FCS.
[So] Source:Mol Biol Cell;28(11):1507-1518, 2017 Jun 01.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Diffusion and interaction dynamics of molecules at the plasma membrane play an important role in cellular signaling and are suggested to be strongly associated with the actin cytoskeleton. Here we use superresolution STED microscopy combined with fluorescence correlation spectroscopy (STED-FCS) to access and compare the diffusion characteristics of fluorescent lipid analogues and GPI-anchored proteins (GPI-APs) in the live-cell plasma membrane and in actin cytoskeleton-free, cell-derived giant plasma membrane vesicles (GPMVs). Hindered diffusion of phospholipids and sphingolipids is abolished in the GPMVs, whereas transient nanodomain incorporation of ganglioside lipid GM1 is apparent in both the live-cell membrane and GPMVs. For GPI-APs, we detect two molecular pools in living cells; one pool shows high mobility with transient incorporation into nanodomains, and the other pool forms immobile clusters, both of which disappear in GPMVs. Our data underline the crucial role of the actin cortex in maintaining hindered diffusion modes of many but not all of the membrane molecules and highlight a powerful experimental approach to decipher specific influences on molecular plasma membrane dynamics.
[Mh] Termos MeSH primário: Bicamadas Lipídicas/metabolismo
Espectrometria de Fluorescência/métodos
[Mh] Termos MeSH secundário: Citoesqueleto de Actina/metabolismo
Actinas/metabolismo
Animais
Células CHO
Membrana Celular/metabolismo
Cricetulus
Vesículas Citoplasmáticas/metabolismo
Difusão
Corantes Fluorescentes/química
Seres Humanos
Lipídeos de Membrana/metabolismo
Microdomínios da Membrana/metabolismo
Proteínas de Membrana/metabolismo
Microscopia
Modelos Biológicos
Simulação de Dinâmica Molecular
Fosfolipídeos/metabolismo
Ligação Proteica
Transdução de Sinais
Técnicas de Cultura de Tecidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Fluorescent Dyes); 0 (Lipid Bilayers); 0 (Membrane Lipids); 0 (Membrane Proteins); 0 (Phospholipids)
[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:170414
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E16-07-0536


  7 / 1639 MEDLINE  
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[PMID]:28388487
[Au] Autor:Yu L; Takeda K; Gao Y
[Ad] Endereço:Division of Viral Products, Office of Vaccines Research and Review, USA. Electronic address: li.yu@fda.hhs.gov.
[Ti] Título:Characterization of virus-specific vesicles assembled by West Nile virus non-structural proteins.
[So] Source:Virology;506:130-140, 2017 Jun.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Flavivirus genome encodes seven non-structural proteins (NSPs) and these NSPs are believed to be involved in their genomic RNA replication, of which the mechanism is unclear. We find that West Nile virus (WNV) NSPs were capable of self-assembling membranous vesicles in cells, which are composed of the host endoplasmic reticulum membrane integrated with viral NS1 and NS4A, and possibly NS2A. The vesicles can further organize into replication complex (RC)-associated vesicles which combine both the vesicle and predicted RC components. The authentic RC-associated vesicles were observed in cells transfected with infectious WNV cDNA as well as WNV replicon. Further mutational analysis showed that WNV/DENV heterologous NS polyproteins derived from lethal chimeric recombinants produced abnormal vesicles. Site-directed mutation of either NS2A or NS4A, which resulted in failure of viral RNA replication, caused immature vesicles too. These findings reveal molecular composition and assembly of the virus-specific nanomachine and confirm that these structures are used for the viral RNA replication.
[Mh] Termos MeSH primário: Vesículas Citoplasmáticas/virologia
Proteínas não Estruturais Virais/metabolismo
Montagem de Vírus
Febre do Nilo Ocidental/virologia
Vírus do Nilo Ocidental/fisiologia
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Retículo Endoplasmático/virologia
Proteínas não Estruturais Virais/genética
Replicação Viral
Vírus do Nilo Ocidental/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Viral Nonstructural Proteins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170705
[Lr] Data última revisão:
170705
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170408
[St] Status:MEDLINE


  8 / 1639 MEDLINE  
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[PMID]:28381426
[Au] Autor:Semenova I; Gupta D; Usui T; Hayakawa I; Cowan A; Rodionov V
[Ad] Endereço:R. D. Berlin Center for Cell Analysis and Modeling and Department of Cell Biology, UConn Health, Farmington, CT 06030.
[Ti] Título:Stimulation of microtubule-based transport by nucleation of microtubules on pigment granules.
[So] Source:Mol Biol Cell;28(11):1418-1425, 2017 Jun 01.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Microtubule (MT)-based transport can be regulated through changes in organization of MT transport tracks, but the mechanisms that regulate these changes are poorly understood. In melanophores, aggregation of pigment granules in the cell center involves their capture by the tips of MTs growing toward the cell periphery, and granule aggregation signals facilitate capture by increasing the number of growing MT tips. This increase could be explained by stimulation of MT nucleation either on the centrosome or on the aggregate of pigment granules that gradually forms in the cell center. We blocked movement of pigment granules to the cell center and compared the MT-nucleation activity of the centrosome in the same cells in two signaling states. We found that granule aggregation signals did not stimulate MT nucleation on the centrosome but did increase MT nucleation activity of pigment granules. Elevation of MT-nucleation activity correlated with the recruitment to pigment granules of a major component of MT-nucleation templates, γ-tubulin, and was suppressed by γ-tubulin inhibitors. We conclude that generation of new MT transport tracks by concentration of the leading pigment granules provides a positive feedback loop that enhances delivery of trailing granules to the cell center.
[Mh] Termos MeSH primário: Melanóforos/metabolismo
Microtúbulos/metabolismo
[Mh] Termos MeSH secundário: Animais
Transporte Biológico
Técnicas de Cultura de Células
Centrossomo/metabolismo
Grânulos Citoplasmáticos/metabolismo
Vesículas Citoplasmáticas/metabolismo
Dineínas/metabolismo
Modelos Biológicos
Movimento/fisiologia
Transdução de Sinais/fisiologia
Tubulina (Proteína)/metabolismo
Xenopus/metabolismo
Xenopus laevis/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Tubulin); EC 3.6.4.2 (Dyneins)
[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:170407
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E16-08-0571


  9 / 1639 MEDLINE  
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[PMID]:28323853
[Au] Autor:Harris MC; Cislo D; Lenz JS; Umbach C; Lindau M
[Ad] Endereço:School of Applied and Engineering Physics, Engineering, Cornell University, Ithaca, NY, United States of America.
[Ti] Título:AFM/TIRF force clamp measurements of neurosecretory vesicle tethers reveal characteristic unfolding steps.
[So] Source:PLoS One;12(3):e0173993, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Although several proteins have been implicated in secretory vesicle tethering, the identity and mechanical properties of the components forming the physical vesicle-plasma membrane link remain unknown. Here we present the first experimental measurements of nanomechanical properties of secretory vesicle-plasma membrane tethers using combined AFM force clamp and TIRF microscopy on membrane sheets from PC12 cells expressing the vesicle marker ANF-eGFP. Application of pulling forces generated tether extensions composed of multiple steps with variable length. The frequency of short (<10 nm) tether extension events was markedly higher when a fluorescent vesicle was present at the cantilever tip and increased in the presence of GTPγS, indicating that these events reflect specifically the properties of vesicle-plasma membrane tethers. The magnitude of the short tether extension events is consistent with extension lengths expected from progressive unfolding of individual helices of the exocyst complex, supporting its direct role in forming the physical vesicle-plasma membrane link.
[Mh] Termos MeSH primário: Fator Natriurético Atrial/metabolismo
Membrana Celular/metabolismo
Vesículas Citoplasmáticas/metabolismo
Microscopia de Força Atômica/métodos
Microscopia de Interferência/métodos
Vesículas Secretórias/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Corantes Fluorescentes/metabolismo
Proteínas de Fluorescência Verde/metabolismo
Fenômenos Mecânicos
Células PC12
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fluorescent Dyes); 0 (enhanced green fluorescent protein); 147336-22-9 (Green Fluorescent Proteins); 85637-73-6 (Atrial Natriuretic Factor)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170322
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0173993


  10 / 1639 MEDLINE  
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[PMID]:28273099
[Au] Autor:Eppler FJ; Quast T; Kolanus W
[Ad] Endereço:Division of Molecular Immunology and Cell Biology, Life and Medical Sciences Institute (LIMES), University of Bonn, Bonn, Germany.
[Ti] Título:Dynamin2 controls Rap1 activation and integrin clustering in human T lymphocyte adhesion.
[So] Source:PLoS One;12(3):e0172443, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Leukocyte trafficking is crucial to facilitate efficient immune responses. Here, we report that the large GTPase dynamin2, which is generally considered to have a key role in endocytosis and membrane remodeling, is an essential regulator of integrin-dependent human T lymphocyte adhesion and migration. Chemical inhibition or knockdown of dynamin2 expression significantly reduced integrin-dependent T cell adhesion in vitro. This phenotype was not observed when T cells were treated with various chemical inhibitors which abrogate endocytosis or actin polymerization. We furthermore detected dynamin2 in signaling complexes and propose that it controls T cell adhesion via FAK/Pyk2- and RapGEF1-mediated Rap1 activation. In addition, the dynamin2 inhibitor-induced reduction of lymphocyte adhesion can be rescued by Rap1a overexpression. We demonstrate that the dynamin2 effect on T cell adhesion does not involve integrin affinity regulation but instead relies on its ability to modulate integrin valency. Taken together, we suggest a previously unidentified role of dynamin2 in the regulation of integrin-mediated lymphocyte adhesion via a Rap1 signaling pathway.
[Mh] Termos MeSH primário: Adesão Celular
Dinamina II/metabolismo
Integrinas/metabolismo
Linfócitos T/imunologia
Linfócitos T/metabolismo
Proteínas rap1 de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Transporte Biológico
Movimento Celular
Vesículas Citoplasmáticas/metabolismo
Quinase 2 de Adesão Focal/metabolismo
Proteína-Tirosina Quinases de Adesão Focal/metabolismo
Expressão Gênica
Genes Reporter
Seres Humanos
Ligação Proteica
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Integrins); EC 2.7.10.2 (Focal Adhesion Kinase 2); EC 2.7.10.2 (Focal Adhesion Protein-Tyrosine Kinases); EC 3.6.5.2 (rap1 GTP-Binding Proteins); EC 3.6.5.5 (Dynamin II)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170901
[Lr] Data última revisão:
170901
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170309
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0172443



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