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[PMID]:28878020
[Au] Autor:Cooney KA; Molden BM; Kowalczyk NS; Russell S; Baldini G
[Ad] Endereço:From the Department of Biochemistry and Molecular Biology University of Arkansas for Medical Sciences, Little Rock, Arkansas 72205-7199.
[Ti] Título:Lipid stress inhibits endocytosis of melanocortin-4 receptor from modified clathrin-enriched sites and impairs receptor desensitization.
[So] Source:J Biol Chem;292(43):17731-17745, 2017 Oct 27.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Melanocortin-4 receptor (MC4R) is a G-protein-coupled receptor expressed in the brain's hypothalamus where it regulates energy homeostasis. MC4R agonists function to lower food intake and weight. In this respect, although obesity promotes hyperlipidemia and hypothalamic injury, MC4R agonists are nevertheless more effective to reduce food intake within hours of administration in overweight, rather than lean, mice. MC4R undergoes constitutive internalization and recycling to the plasma membrane with agonist binding inducing receptor retention along the intracellular route and, under prolonged exposure, desensitization. Here, we found that, in neuronal cells, lipid stress by exposure to elevated palmitate leaves unchanged the rate by which MC4R and transferrin receptor are constitutively excluded from the cell surface. However, lipid stress disrupted later steps of MC4R and transferrin receptor internalization to endosomes as well as traffic of agonist-occupied MC4R to lysosomes and MC4R desensitization. In the lipid-stressed cells, MC4R and clathrin were redistributed to the plasma membrane where they colocalized to sites that appeared by super-resolution microscopy to be modified and to have higher clathrin content than those of cells not exposed to elevated palmitate. The data suggest that lipid stress disrupts steps of endocytosis following MC4R localization to clathrin-coated sites and exclusion of the receptor from the extracellular medium. We conclude that increased effectiveness of MC4R agonists in obesity may be an unexpected outcome of neuronal injury with disrupted clathrin-dependent endocytosis and impaired receptor desensitization.
[Mh] Termos MeSH primário: Membrana Celular/metabolismo
Clatrina/metabolismo
Endocitose
Hiperlipidemias/metabolismo
Obesidade/metabolismo
Receptor Tipo 4 de Melanocortina/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Membrana Celular/genética
Clatrina/genética
Hiperlipidemias/genética
Lisossomos/genética
Lisossomos/metabolismo
Masculino
Camundongos
Obesidade/genética
Receptor Tipo 4 de Melanocortina/genética
Receptores da Transferrina/genética
Receptores da Transferrina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Clathrin); 0 (Receptor, Melanocortin, Type 4); 0 (Receptors, Transferrin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170907
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.785758


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[PMID]:28215307
[Au] Autor:Vilar M
[Ad] Endereço:Molecular Basis of Neurodegeneration Unit, Institute of Biomedicine of Valencia (IBV-CSIC), València, Spain. Electronic address: mvilar@ibv.csic.es.
[Ti] Título:Structural Characterization of the p75 Neurotrophin Receptor: A Stranger in the TNFR Superfamily.
[So] Source:Vitam Horm;104:57-87, 2017.
[Is] ISSN:0083-6729
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Although p75 neurotrophin receptor (p75 ) was the founding member of the tumor necrosis factor (TNF) receptor superfamily (TNFRSF), it is an atypical TNFRSF protein. p75 like TNF-R1 and Fas-R contain an extracellular domain with four cysteine-rich domains (CRD) and a death domain (DD) in the intracellular region. While TNFRSF proteins are activated by trimeric TNFSF ligands, p75 forms dimers activated by dimeric neurotrophins that are structurally unrelated to TNFSF proteins. In addition, although p75 shares with other members the interaction with the TNF receptor-associated factors to activate the NF-κB and cell death pathways, p75 does not interact with the DD-containing proteins FADD, TRADD, or MyD88. By contrast, the DD of p75 is able to recruit several protein interactors via a full catalog of DD interactions not described before in the TNFRSF. p75-DD forms homotypic symmetrical DD-DD complexes with itself and with the related p45-DD; forms heterotypic DD-CARD interactions with the RIP2-CARD domain, and forms a new interaction between a DD and RhoGDI. All these features, in addition to its promiscuous interactions with several ligands and coreceptors, its processing by α- and γ-secretases, the dimeric nature of its transmembrane domain and its "special" juxtamembrane region, make p75 a truly stranger in the TNFR superfamily. In this chapter, I will summarize the known structural aspects of p75 and I will analyze from a structural point of view, the similitudes and differences between p75 and the other members of the TNFRSF.
[Mh] Termos MeSH primário: Modelos Moleculares
Receptor de Fator de Crescimento Neural/metabolismo
Receptores Tipo II do Fator de Necrose Tumoral/metabolismo
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transporte Vesicular/química
Proteínas Adaptadoras de Transporte Vesicular/metabolismo
Animais
Sítios de Ligação
Dimerização
Humanos
Ligantes
Fatores de Crescimento Neural/química
Fatores de Crescimento Neural/metabolismo
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
Precursores de Proteínas/química
Precursores de Proteínas/metabolismo
Receptor de Fator de Crescimento Neural/agonistas
Receptor de Fator de Crescimento Neural/química
Receptor de Fator de Crescimento Neural/genética
Receptores de Fator de Crescimento Neural/química
Receptores de Fator de Crescimento Neural/metabolismo
Receptores Tipo II do Fator de Necrose Tumoral/agonistas
Receptores Tipo II do Fator de Necrose Tumoral/química
Receptores Tipo II do Fator de Necrose Tumoral/genética
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Adaptor Proteins, Vesicular Transport); 0 (Ligands); 0 (Nerve Growth Factors); 0 (Protein Precursors); 0 (Receptor, Nerve Growth Factor); 0 (Receptors, Nerve Growth Factor); 0 (Receptors, Tumor Necrosis Factor, Type II); 0 (TNFRSF1B protein, human); 0 (sortilin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170220
[St] Status:MEDLINE


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[PMID]:29028839
[Au] Autor:Ward C; Maselko M; Lupfer C; Prescott M; Pastey MK
[Ad] Endereço:Department of Veterinary Biomedical Sciences, Oregon State University, Corvallis, Oregon, United States of America.
[Ti] Título:Interaction of the Human Respiratory Syncytial Virus matrix protein with cellular adaptor protein complex 3 plays a critical role in trafficking.
[So] Source:PLoS One;12(10):e0184629, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human Respiratory Syncytial Virus (HRSV) is a leading cause of bronchopneumonia in infants and the elderly. To date, knowledge of viral and host protein interactions within HRSV is limited and are critical areas of research. Here, we show that HRSV Matrix (M) protein interacts with the cellular adaptor protein complex 3 specifically via its medium subunit (AP-3Mu3A). This novel protein-protein interaction was first detected via yeast-two hybrid screen and was further confirmed in a mammalian system by immunofluorescence colocalization and co-immunoprecipitation. This novel interaction is further substantiated by the presence of a known tyrosine-based adaptor protein MU subunit sorting signal sequence, YXXФ: where Ф is a bulky hydrophobic residue, which is conserved across the related RSV M proteins. Analysis of point-mutated HRSV M derivatives indicated that AP-3Mu3A- mediated trafficking is contingent on the presence of the tyrosine residue within the YXXL sorting sequence at amino acids 197-200 of the M protein. AP-3Mu3A is up regulated at 24 hours post-infection in infected cells versus mock-infected HEp2 cells. Together, our data suggests that the AP-3 complex plays a critical role in the trafficking of HRSV proteins specifically matrix in epithelial cells. The results of this study add new insights and targets that may lead to the development of potential antivirals and attenuating mutations suitable for candidate vaccines in the future.
[Mh] Termos MeSH primário: Complexo 3 de Proteínas Adaptadoras/metabolismo
Vírus Sincicial Respiratório Humano/metabolismo
Proteínas da Matriz Viral/metabolismo
[Mh] Termos MeSH secundário: Complexo 3 de Proteínas Adaptadoras/química
Motivos de Aminoácidos
Sequência de Aminoácidos
Sequência Conservada
Células HeLa
Humanos
Ligação Proteica
Estabilidade Proteica
Subunidades Proteicas/química
Subunidades Proteicas/metabolismo
Transporte Proteico
Vírus Sincicial Respiratório Humano/fisiologia
Regulação para Cima
Proteínas da Matriz Viral/química
Montagem de Vírus
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Protein Complex 3); 0 (Protein Subunits); 0 (Viral Matrix Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171013
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184629


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[PMID]:28930658
[Au] Autor:Purbey PK; Scumpia PO; Kim PJ; Tong AJ; Iwamoto KS; McBride WH; Smale ST
[Ad] Endereço:Department of Microbiology, Immunology, and Molecular Genetics, and Molecular Biology Institute, University of California, Los Angeles, Los Angeles, CA 90095, USA.
[Ti] Título:Defined Sensing Mechanisms and Signaling Pathways Contribute to the Global Inflammatory Gene Expression Output Elicited by Ionizing Radiation.
[So] Source:Immunity;47(3):421-434.e3, 2017 Sep 19.
[Is] ISSN:1097-4180
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Environmental insults are often detected by multiple sensors that activate diverse signaling pathways and transcriptional regulators, leading to a tailored transcriptional output. To understand how a tailored response is coordinated, we examined the inflammatory response elicited in mouse macrophages by ionizing radiation (IR). RNA-sequencing studies revealed that most radiation-induced genes were strongly dependent on only one of a small number of sensors and signaling pathways, notably the DNA damage-induced kinase ATM, which regulated many IR-response genes, including interferon response genes, via an atypical IRF1-dependent, STING-independent mechanism. Moreover, small, defined sets of genes activated by p53 and NRF2 accounted for the selective response to radiation in comparison to a microbial inducer of inflammation. Our findings reveal that genes comprising an environmental response are activated by defined sensing mechanisms with a high degree of selectivity, and they identify distinct components of the radiation response that might be susceptible to therapeutic perturbation.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica/efeitos de radiação
Inflamação/genética
Inflamação/metabolismo
Radiação Ionizante
Transdução de Sinal
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transporte Vesicular/metabolismo
Animais
Proteínas Mutadas de Ataxia Telangiectasia/genética
Proteínas Mutadas de Ataxia Telangiectasia/metabolismo
Análise por Conglomerados
Proteína Quinase Ativada por DNA/metabolismo
Relação Dose-Resposta à Radiação
MAP Quinases Reguladas por Sinal Extracelular/metabolismo
Perfilação da Expressão Gênica
Regulação da Expressão Gênica/efeitos de drogas
Técnicas de Inativação de Genes
Humanos
Interferons/metabolismo
Interferons/farmacologia
Macrófagos/metabolismo
Macrófagos/efeitos de radiação
Proteínas de Membrana/metabolismo
Camundongos
Fator 88 de Diferenciação Mieloide/metabolismo
Fator 2 Relacionado a NF-E2/metabolismo
Espécies de Oxigênio Reativas/metabolismo
Receptor de Interferon alfa e beta/genética
Receptor de Interferon alfa e beta/metabolismo
Transcrição Genética/efeitos de radiação
Ativação Transcricional
Regulador Transcricional ERG/genética
Proteína Supressora de Tumor p53/genética
Proteína Supressora de Tumor p53/metabolismo
Proteínas Quinases p38 Ativadas por Mitógeno/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Vesicular Transport); 0 (MPYS protein, human); 0 (Membrane Proteins); 0 (Myeloid Differentiation Factor 88); 0 (NF-E2-Related Factor 2); 0 (Reactive Oxygen Species); 0 (TICAM1 protein, human); 0 (Transcriptional Regulator ERG); 0 (Tumor Suppressor Protein p53); 156986-95-7 (Receptor, Interferon alpha-beta); 9008-11-1 (Interferons); EC 2.7.11.1 (Ataxia Telangiectasia Mutated Proteins); EC 2.7.11.1 (DNA-Activated Protein Kinase); EC 2.7.11.24 (Extracellular Signal-Regulated MAP Kinases); EC 2.7.11.24 (p38 Mitogen-Activated Protein Kinases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170920
[St] Status:MEDLINE


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[PMID]:28450454
[Au] Autor:Pan X; Zaarur N; Singh M; Morin P; Kandror KV
[Ad] Endereço:Department of Biochemistry, Boston University School of Medicine, Boston, MA 02118.
[Ti] Título:Sortilin and retromer mediate retrograde transport of Glut4 in 3T3-L1 adipocytes.
[So] Source:Mol Biol Cell;28(12):1667-1675, 2017 Jun 15.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sortilin is a multiligand sorting receptor responsible for the anterograde transport of lysosomal enzymes and substrates. Here we demonstrate that sortilin is also involved in retrograde protein traffic. In cultured 3T3-L1 adipocytes, sortilin together with retromer rescues Glut4 from degradation in lysosomes and retrieves it to the TGN, where insulin--responsive vesicles are formed. Mechanistically, the luminal Vps10p domain of sortilin interacts with the first luminal loop of Glut4, and the cytoplasmic tail of sortilin binds to retromer. Ablation of the retromer does not affect insulin signaling but decreases the stability of sortilin and Glut4 and blocks their entry into the small vesicular carriers. As a result, Glut4 cannot reach the insulin-responsive compartment, and insulin-stimulated glucose uptake in adipocytes is suppressed. We suggest that sortilin- and retromer-mediated Glut4 retrieval from endosomes may represent a step in the Glut4 pathway vulnerable to the development of insulin resistance and diabetes.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transporte Vesicular/metabolismo
Transportador de Glucose Tipo 4/metabolismo
Nexinas de Classificação/metabolismo
[Mh] Termos MeSH secundário: Células 3T3-L1
Proteínas Adaptadoras de Transporte Vesicular/genética
Adipócitos/metabolismo
Animais
Transporte Biológico
Membrana Celular/metabolismo
Endossomos/metabolismo
Insulina/metabolismo
Resistência à Insulina
Lisossomos
Camundongos
Proteínas Musculares/metabolismo
Domínios Proteicos
Transporte Proteico/fisiologia
Rede trans-Golgi/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Vesicular Transport); 0 (Glucose Transporter Type 4); 0 (Insulin); 0 (Muscle Proteins); 0 (Slc2a4 protein, mouse); 0 (Sorting Nexins); 0 (sortilin)
[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:170428
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E16-11-0777


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[PMID]:28428254
[Au] Autor:Bottanelli F; Kilian N; Ernst AM; Rivera-Molina F; Schroeder LK; Kromann EB; Lessard MD; Erdmann RS; Schepartz A; Baddeley D; Bewersdorf J; Toomre D; Rothman JE
[Ad] Endereço:Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06520.
[Ti] Título:A novel physiological role for ARF1 in the formation of bidirectional tubules from the Golgi.
[So] Source:Mol Biol Cell;28(12):1676-1687, 2017 Jun 15.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Capitalizing on CRISPR/Cas9 gene-editing techniques and super-resolution nanoscopy, we explore the role of the small GTPase ARF1 in mediating transport steps at the Golgi. Besides its well-established role in generating COPI vesicles, we find that ARF1 is also involved in the formation of long (∼3 µm), thin (∼110 nm diameter) tubular carriers. The anterograde and retrograde tubular carriers are both largely free of the classical Golgi coat proteins coatomer (COPI) and clathrin. Instead, they contain ARF1 along their entire length at a density estimated to be in the range of close packing. Experiments using a mutant form of ARF1 affecting GTP hydrolysis suggest that ARF1[GTP] is functionally required for the tubules to form. Dynamic confocal and stimulated emission depletion imaging shows that ARF1-rich tubular compartments fall into two distinct classes containing 1) anterograde cargoes and clathrin clusters or 2) retrograde cargoes and coatomer clusters.
[Mh] Termos MeSH primário: Fator 1 de Ribosilação do ADP/fisiologia
Complexo de Golgi/fisiologia
[Mh] Termos MeSH secundário: Fator 1 de Ribosilação do ADP/genética
Fator 1 de Ribosilação do ADP/metabolismo
Vesículas Revestidas pelo Complexo de Proteína do Envoltório/metabolismo
Clatrina/metabolismo
Complexo I de Proteína do Envoltório/metabolismo
GTP Fosfo-Hidrolases/metabolismo
Complexo de Golgi/metabolismo
Guanosina Trifosfato/metabolismo
Células HeLa
Humanos
Hidrólise
Membranas Intracelulares/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Clathrin); 0 (Coat Protein Complex I); 86-01-1 (Guanosine Triphosphate); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.5.2 (ADP-Ribosylation Factor 1)
[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:170421
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E16-12-0863


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[PMID]:28316001
[Au] Autor:Vacínová G; Vejrazková D; Lukásová P; Lischková O; Dvoráková K; Rusina R; Holmerová I; Vanková H; Vcelák J; Bendlová B; Vanková M
[Ad] Endereço:Department of Molecular Endocrinology, Institute of Endocrinology, Národní 8, Prague, 116 94, Czech Republic. gvacinova@endo.cz.
[Ti] Título:Associations of polymorphisms in the candidate genes for Alzheimer's disease BIN1, CLU, CR1 and PICALM with gestational diabetes and impaired glucose tolerance.
[So] Source:Mol Biol Rep;44(2):227-231, 2017 Apr.
[Is] ISSN:1573-4978
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Alzheimer's disease (AD) is the most common type of dementia, with a prevalence that is rising every year. AD is associated with type 2 diabetes mellitus (T2DM) and insulin resistance, and is therefore sometimes called "type 3 diabetes mellitus". The aim of this study was to examine whether the variants of some candidate genes involved in the development of AD, namely BIN1 (rs744373), CLU (rs11136000), CR1 (rs3818361), and PICALM (rs3851179), are related to several disorders of glucose metabolism-gestational diabetes (GDM), T2DM and impaired glucose tolerance (IGT). Our study included 550 women with former GDM and 717 control women, 392 patients with T2DM and 180 non-diabetic controls, and 117 patients with IGT and 630 controls with normal glucose tolerance. Genotyping analysis was performed using specially-designed TaqMan assays. No significant associations of the genetic variants rs744373 in BIN1, rs11136000 in CLU, or rs3818361 in CR1 were found with GDM, T2DM or IGT, but rs3851179 in PICALM was associated with an increased risk of GDM. The frequency of the AD risk-associated C allele was significantly higher in the GDM group compared to controls: OR 1.21; 95% CI (1.03-1.44). This finding was not apparent in T2DM and IGT; conversely, the C allele of the PICALM SNP was protective for IGT: OR 0.67; 95% CI (0.51-0.89). This study demonstrates an association between PICALM rs3851179 and GDM as well as IGT. However, elucidation of the possible role of this gene in the pathogenesis of GDM requires further independent studies.
[Mh] Termos MeSH primário: Doença de Alzheimer/genética
Diabetes Gestacional/genética
Intolerância à Glucose/genética
Proteínas Monoméricas de Montagem de Clatrina/genética
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/sangue
Proteínas Adaptadoras de Transdução de Sinal/genética
Adulto
Idoso
Alelos
Doença de Alzheimer/complicações
Clusterina/sangue
Clusterina/genética
Diabetes Mellitus Tipo 2/genética
Diabetes Gestacional/metabolismo
Grupo com Ancestrais do Continente Europeu/genética
Feminino
Frequência do Gene
Estudos de Associação Genética/métodos
Predisposição Genética para Doença
Variação Genética
Intolerância à Glucose/metabolismo
Humanos
Meia-Idade
Proteínas Monoméricas de Montagem de Clatrina/sangue
Proteínas Nucleares/sangue
Proteínas Nucleares/genética
Razão de Chances
Polimorfismo de Nucleotídeo Único/genética
Gravidez
Receptores de Complemento 3b/sangue
Receptores de Complemento 3b/genética
Fatores de Risco
Proteínas Supressoras de Tumor/sangue
Proteínas Supressoras de Tumor/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (BIN1 protein, human); 0 (CLU protein, human); 0 (CR1 protein, human); 0 (Clusterin); 0 (Monomeric Clathrin Assembly Proteins); 0 (Nuclear Proteins); 0 (PICALM protein, human); 0 (Receptors, Complement 3b); 0 (Tumor Suppressor Proteins)
[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:170319
[St] Status:MEDLINE
[do] DOI:10.1007/s11033-017-4100-9


  8 / 8698 MEDLINE  
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[PMID]:28670876
[Au] Autor:Nowikovsky K; Bergmann M
[Ad] Endereço:Department of Internal Medicine I, Medical University Vienna, Austria.
[Ti] Título:Autophagy regulates apoptosis on the level of the death-inducing signalling complex.
[So] Source:FEBS J;284(13):1967-1969, 2017 07.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The interactions between apoptotic and autophagic proteins via the proteolytic systems are known mechanisms through which autophagy and apoptosis regulate each other. In this issue of The FEBS Journal, Gentle and colleagues propose a mechanism through which autophagy regulates the induction of apoptosis at the level of the TIR-domain-containing adaptor-inducing interferon-ß (TRIF) in TLR signaling.
[Mh] Termos MeSH primário: Apoptose
Autofagia
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transporte Vesicular
Humanos
Transdução de Sinal
[Pt] Tipo de publicação:JOURNAL ARTICLE; COMMENT
[Nm] Nome de substância:
0 (Adaptor Proteins, Vesicular Transport)
[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:170703
[St] Status:MEDLINE
[do] DOI:10.1111/febs.14119


  9 / 8698 MEDLINE  
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[PMID]:28453927
[Au] Autor:Gentle IE; McHenry KT; Weber A; Metz A; Kretz O; Porter D; Häcker G
[Ad] Endereço:Faculty of Medicine, Institute for Medical Microbiology and Hygiene, Medical Center - University of Freiburg, University of Freiburg, Germany.
[Ti] Título:TIR-domain-containing adapter-inducing interferon-ß (TRIF) forms filamentous structures, whose pro-apoptotic signalling is terminated by autophagy.
[So] Source:FEBS J;284(13):1987-2003, 2017 Jul.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The formation of amyloid-like protein structures has recently emerged as a feature in signal transduction, particularly in innate immunity. These structures appear to depend on defined domains for their formation but likely also require dedicated ways to terminate signalling. We, here, define the innate immunity protein/Toll-like receptor adaptor TIR-domain-containing adapter-inducing interferon-ß (TRIF) as a novel platform of fibril formation and probe signal initiation through TRIF as well as its termination in Toll-like receptor 3 (TLR3)-stimulated melanoma cells. A main signalling pathway triggered by TLR3 caused apoptosis, which was controlled by inhibitor of apoptosis proteins and was dependent on RIPK1 and independent of TNF. Using correlative electron/fluorescence microscopy, we visualised fibrillar structures formed through both Toll/interleukin-1 receptor and RIP homotypic interacting motif regions of TRIF. We provide evidence that these fibrillary structures are active signalling platforms whose activity is terminated by autophagy. TRIF-signalling enhanced autophagy, and fibrillary structures were partly contained within autophagosomes. Inhibition of autophagy increased levels of pro-apoptotic TRIF complexes, leading to the accumulation of active caspase-8 and enhanced apoptosis while stimulation of autophagy reduced TRIF-dependent death. We conclude that pro-death signals through TRIF are regulated by autophagy and propose that pro-apoptotic signalling through TRIF/RIPK1/caspase-8 occurs in fibrillary platforms.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transporte Vesicular/metabolismo
Apoptose/fisiologia
Autofagia/fisiologia
Transdução de Sinal
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transporte Vesicular/química
Proteínas Adaptadoras de Transporte Vesicular/genética
Animais
Apoptose/efeitos de drogas
Autofagia/efeitos de drogas
Western Blotting
Caspase 8/genética
Caspase 8/metabolismo
Linhagem Celular Tumoral
Células Cultivadas
Células HEK293
Células HeLa
Humanos
Camundongos Knockout
Microscopia Eletrônica de Transmissão
Microscopia de Fluorescência
Oligopeptídeos/farmacologia
Poli I-C/farmacologia
Proteína Serina-Treonina Quinases de Interação com Receptores/metabolismo
Receptor 3 Toll-Like/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Vesicular Transport); 0 (LBW242); 0 (Oligopeptides); 0 (TICAM1 protein, human); 0 (Toll-Like Receptor 3); 24939-03-5 (Poly I-C); EC 2.7.11.1 (RIPK1 protein, human); EC 2.7.11.1 (Receptor-Interacting Protein Serine-Threonine Kinases); EC 3.4.22.- (Caspase 8)
[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:170428
[St] Status:MEDLINE
[do] DOI:10.1111/febs.14091


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[PMID]:28007916
[Au] Autor:Frazier MN; Jackson LP
[Ad] Endereço:Department of Biological Sciences, Center for Structural Biology, Vanderbilt University, Nashville, TN 37232.
[Ti] Título:Watching real-time endocytosis in living cells.
[So] Source:J Cell Biol;216(1):9-11, 2017 01 02.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The precise sequence of events promoting clathrin-coated vesicle assembly is still debated. In this issue, Kadlecova et al. (2017. J. Cell Biol. https://doi.org/10.1083/jcb.201608071) test structural models using quantitative microscopy in living cells to investigate the hierarchy and temporal importance of molecular events required for clathrin-coated pit initiation.
[Mh] Termos MeSH primário: Invaginações Revestidas da Membrana Celular
Endocitose
[Mh] Termos MeSH secundário: Transporte Biológico
Clatrina/química
Vesículas Revestidas por Clatrina
Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; COMMENT
[Nm] Nome de substância:
0 (Clathrin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161223
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201611115



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