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Pesquisa : D12.776.543.990.150.500.300 [Categoria DeCS]
Referências encontradas : 35 [refinar]
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[PMID]:26744459
[Au] Autor:Ammann S; Schulz A; Krägeloh-Mann I; Dieckmann NM; Niethammer K; Fuchs S; Eckl KM; Plank R; Werner R; Altmüller J; Thiele H; Nürnberg P; Bank J; Strauss A; von Bernuth H; Zur Stadt U; Grieve S; Griffiths GM; Lehmberg K; Hennies HC; Ehl S
[Ad] Endereço:Center for Chronic Immunodeficiency, University Medical Center Freiburg, Freiburg, Germany; Faculty of Biology, University Freiburg, Freiburg, Germany;
[Ti] Título:Mutations in AP3D1 associated with immunodeficiency and seizures define a new type of Hermansky-Pudlak syndrome.
[So] Source:Blood;127(8):997-1006, 2016 Feb 25.
[Is] ISSN:1528-0020
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Genetic disorders affecting biogenesis and transport of lysosome-related organelles are heterogeneous diseases frequently associated with albinism. We studied a patient with albinism, neutropenia, immunodeficiency, neurodevelopmental delay, generalized seizures, and impaired hearing but with no mutation in genes so far associated with albinism and immunodeficiency. Whole exome sequencing identified a homozygous mutation in AP3D1 that leads to destabilization of the adaptor protein 3 (AP3) complex. AP3 complex formation and the degranulation defect in patient T cells were restored by retroviral reconstitution. A previously described hypopigmented mouse mutant with an Ap3d1 null mutation (mocha strain) shares the neurologic phenotype with our patient and shows a platelet storage pool deficiency characteristic of Hermansky-Pudlak syndrome (HPS) that was not studied in our patient because of a lack of bleeding. HPS2 caused by mutations in AP3B1A leads to a highly overlapping phenotype without the neurologic symptoms. The AP3 complex exists in a ubiquitous and a neuronal form. AP3D1 codes for the AP3δ subunit of the complex, which is essential for both forms. In contrast, the AP3ß3A subunit, affected in HPS2 patients, is substituted by AP3ß3B in the neuron-specific heterotetramer. AP3δ deficiency thus causes a severe neurologic disorder with immunodeficiency and albinism that we propose to classify as HPS10.
[Mh] Termos MeSH primário: Complexo 3 de Proteínas Adaptadoras/genética
Subunidades delta do Complexo de Proteínas Adaptadoras/genética
Síndrome de Hermanski-Pudlak/classificação
Síndrome de Hermanski-Pudlak/genética
Síndromes de Imunodeficiência/genética
Convulsões/genética
[Mh] Termos MeSH secundário: Eletroforese em Gel de Poliacrilamida
Imunofluorescência
Seres Humanos
Mutação
Transfecção
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (AP3D1 protein, human); 0 (Adaptor Protein Complex 3); 0 (Adaptor Protein Complex delta Subunits)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:160226
[Lr] Data última revisão:
160226
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:160109
[St] Status:MEDLINE
[do] DOI:10.1182/blood-2015-09-671636


  2 / 35 MEDLINE  
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[PMID]:26564901
[Au] Autor:Gilliland WD
[Ad] Endereço:Department of Biological Sciences, DePaul University, Chicago, Illinois 60614.
[Ti] Título:A Comment on Fine-Scale Heterogeneity in Crossover Rate in the garnet-scalloped Region of the Drosophila melanogaster X Chromosome.
[So] Source:Genetics;201(3):1275-7, 2015 Nov.
[Is] ISSN:1943-2631
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Complexo 3 de Proteínas Adaptadoras/genética
Subunidades delta do Complexo de Proteínas Adaptadoras/genética
Cromossomos de Insetos/genética
Troca Genética
Proteínas de Drosophila/genética
Drosophila melanogaster/genética
Proteínas do Olho/genética
Heterogeneidade Genética
Fatores de Transcrição/genética
Cromossomo X/genética
[Mh] Termos MeSH secundário: Animais
[Pt] Tipo de publicação:COMMENT; LETTER; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Adaptor Protein Complex 3); 0 (Adaptor Protein Complex delta Subunits); 0 (Drosophila Proteins); 0 (Eye Proteins); 0 (Transcription Factors)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:161202
[Lr] Data última revisão:
161202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151114
[St] Status:MEDLINE
[do] DOI:10.1534/genetics.115.177808


  3 / 35 MEDLINE  
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[PMID]:24916648
[Au] Autor:Hirokawa M; Morita H; Tajima T; Takahashi A; Ashikawa K; Miya F; Shigemizu D; Ozaki K; Sakata Y; Nakatani D; Suna S; Imai Y; Tanaka T; Tsunoda T; Matsuda K; Kadowaki T; Nakamura Y; Nagai R; Komuro I; Kubo M
[Ad] Endereço:1] Laboratory for Genotyping Development, Center for Genomic Medicine, RIKEN Yokohama Institute, Yokohama, Japan [2] Department of Cardiovascular Medicine, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.
[Ti] Título:A genome-wide association study identifies PLCL2 and AP3D1-DOT1L-SF3A2 as new susceptibility loci for myocardial infarction in Japanese.
[So] Source:Eur J Hum Genet;23(3):374-80, 2015 Mar.
[Is] ISSN:1476-5438
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Despite considerable progress in preventive and therapeutic strategies, myocardial infarction (MI) is one of the leading causes of death throughout the world. A total of 55 susceptibility genes have been identified mostly in European genome-wide association studies (GWAS). Nevertheless, large-scale GWAS from other population could possibly find additional susceptibility loci. To identify as many MI susceptibility loci as possible, we performed a large-scale genomic analysis in Japanese population. To identify MI susceptibility loci in Japanese, we conducted a GWAS using 1666 cases and 3198 controls using the Illumina Human610-Quad BeadChip and HumanHap550v3 Genotyping BeadChip. We performed replication studies using a total of 11,412 cases and 28,397 controls in the Japanese population. Our study identified two novel susceptibility loci for MI: PLCL2 on chromosome 3p24.3 (rs4618210:A>G, P = 2.60 × 10(-9), odds ratio (OR) = 0.91) and AP3D1-DOT1L-SF3A2 on chromosome 19p13.3 (rs3803915:A>C, P = 3.84 × 10(-9), OR = 0.89). Besides, a total of 14 previously reported MI susceptibility loci were replicated in our study. In particular, we validated a strong association on chromosome 12q24 (rs3782886:A>G: P = 1.14 × 10(-14), OR = 1.46). Following pathway analysis using 265 genes related to MI or coronary artery disease, we found that these loci might be involved in the pathogenesis of MI via the promotion of atherosclerosis. In the present large-scale genomic analysis, we identified PLCL2 and AP3D1-DOT1L-SF3A2 as new susceptibility loci for MI in the Japanese population. Our findings will add novel findings for MI susceptibility loci.
[Mh] Termos MeSH primário: Complexo 3 de Proteínas Adaptadoras/genética
Subunidades delta do Complexo de Proteínas Adaptadoras/genética
Grupo com Ancestrais do Continente Asiático/genética
Predisposição Genética para Doença
Estudo de Associação Genômica Ampla
Peptídeos e Proteínas de Sinalização Intracelular/genética
Metiltransferases/genética
Infarto do Miocárdio/genética
Proteínas de Ligação a RNA/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
Alelos
Estudos de Casos e Controles
Cromossomos Humanos Par 12
Feminino
Redes Reguladoras de Genes
Genótipo
Seres Humanos
Japão
Desequilíbrio de Ligação
Masculino
Meia-Idade
Razão de Chances
Polimorfismo de Nucleotídeo Único
Fatores de Processamento de RNA
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (AP3D1 protein, human); 0 (Adaptor Protein Complex 3); 0 (Adaptor Protein Complex delta Subunits); 0 (Intracellular Signaling Peptides and Proteins); 0 (PLCL2 protein, human); 0 (RNA Splicing Factors); 0 (RNA-Binding Proteins); 0 (SF3A2 protein, human); EC 2.1.1.- (DOT1L protein, human); EC 2.1.1.- (Methyltransferases)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140612
[St] Status:MEDLINE
[do] DOI:10.1038/ejhg.2014.110


  4 / 35 MEDLINE  
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[PMID]:23733850
[Au] Autor:Heil CS; Noor MA
[Ad] Endereço:Biology Department, Duke University, Durham, NC 27708, USA.
[Ti] Título:Studying recombination with high-throughput sequencing: an educational primer for use with "fine-scale heterogeneity in crossover rate in the garnet-scalloped region of the Drosophila melanogaster X chromosome".
[So] Source:Genetics;194(2):335-9, 2013 Jun.
[Is] ISSN:1943-2631
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:An article by Singh and colleagues in this issue of GENETICS quantifies variation in recombination rate across a small region of the Drosophila melanogaster genome, providing an opportunity for instructors of genetics to introduce or reinforce important concepts such as recombination and recombination rate variation, genome sequencing, and sequence features of the genome. Additional background information, a detailed explanation of the methods used in this study, and discussion questions are provided.
[Mh] Termos MeSH primário: Complexo 3 de Proteínas Adaptadoras/genética
Subunidades delta do Complexo de Proteínas Adaptadoras/genética
Cromossomos de Insetos/genética
Troca Genética
Proteínas de Drosophila/genética
Drosophila melanogaster/genética
Proteínas do Olho/genética
Heterogeneidade Genética
Fatores de Transcrição/genética
Cromossomo X/genética
[Mh] Termos MeSH secundário: Animais
[Pt] Tipo de publicação:COMMENT; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Protein Complex 3); 0 (Adaptor Protein Complex delta Subunits); 0 (Drosophila Proteins); 0 (Eye Proteins); 0 (Transcription Factors); 0 (garnet protein, Drosophila); 0 (scalloped protein, Drosophila)
[Em] Mês de entrada:1312
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130605
[St] Status:MEDLINE
[do] DOI:10.1534/genetics.113.150771


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[PMID]:23410829
[Au] Autor:Singh ND; Stone EA; Aquadro CF; Clark AG
[Ad] Endereço:Department of Genetics, North Carolina State University, Raleigh, NC 27695, USA. ndsingh@ncsu.edu
[Ti] Título:Fine-scale heterogeneity in crossover rate in the garnet-scalloped region of the Drosophila melanogaster X chromosome.
[So] Source:Genetics;194(2):375-87, 2013 Jun.
[Is] ISSN:1943-2631
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Homologous recombination affects myriad aspects of genome evolution, from standing levels of nucleotide diversity to the efficacy of natural selection. Rates of crossing over show marked variability at all scales surveyed, including species-, population-, and individual-level differences. Even within genomes, crossovers are nonrandomly distributed in a wide diversity of taxa. Although intra- and intergenomic heterogeneities in crossover distribution have been documented in Drosophila, the scale and degree of crossover rate heterogeneity remain unclear. In addition, the genetic features mediating this heterogeneity are unknown. Here we quantify fine-scale heterogeneity in crossover distribution in a 2.1-Mb region of the Drosophila melanogaster X chromosome by localizing crossover breakpoints in 2500 individuals, each containing a single crossover in this specific X chromosome region. We show 90-fold variation in rates of crossing over at a 5-kb scale, place this variation in the context of several aspects of genome evolution, and identify several genetic features associated with crossover rates. Our results shed new light on the scale and magnitude of crossover rate heterogeneity in D. melanogaster and highlight potential features mediating this heterogeneity.
[Mh] Termos MeSH primário: Complexo 3 de Proteínas Adaptadoras/genética
Subunidades delta do Complexo de Proteínas Adaptadoras/genética
Cromossomos de Insetos/genética
Troca Genética
Proteínas de Drosophila/genética
Drosophila melanogaster/genética
Proteínas do Olho/genética
Heterogeneidade Genética
Fatores de Transcrição/genética
Cromossomo X/genética
[Mh] Termos MeSH secundário: Animais
Pontos de Quebra do Cromossomo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adaptor Protein Complex 3); 0 (Adaptor Protein Complex delta Subunits); 0 (Drosophila Proteins); 0 (Eye Proteins); 0 (Transcription Factors); 0 (garnet protein, Drosophila); 0 (scalloped protein, Drosophila)
[Em] Mês de entrada:1312
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130216
[St] Status:MEDLINE
[do] DOI:10.1534/genetics.112.146746


  6 / 35 MEDLINE  
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[PMID]:22875976
[Au] Autor:Liu L; Sutton J; Woodruff E; Villalta F; Spearman P; Dong X
[Ad] Endereço:Department of Microbiology and Immunology and Center for AIDS Health Disparities Research, Meharry Medical College, Nashville, Tennessee, USA.
[Ti] Título:Defective HIV-1 particle assembly in AP-3-deficient cells derived from patients with Hermansky-Pudlak syndrome type 2.
[So] Source:J Virol;86(20):11242-53, 2012 Oct.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Adaptor protein complex 3 (AP-3) is a heterotetramer that is involved in signal-mediated protein sorting to endosomal-lysosomal organelles. AP-3 deficiency in humans, induced by mutations in the AP3B1 gene, which encodes the ß3A subunit of the AP-3 complex, results in Hermansky-Pudlak syndrome 2 (HPS2), which is a rare genetic disorder with defective lysosome-related organelles. In a previous study, we identified the AP-3 complex as an important contributor to HIV-1 assembly and release. We hypothesized that cells from patients affected by HPS2 should demonstrate abnormalities of HIV-1 assembly. Here we report that HIV-1 particle assembly and release are indeed diminished in HPS2 fibroblast cultures. Transient or stable expression of the full-length wild-type ß3A subunit in HPS2 fibroblasts restored the impaired virus assembly and release. In contrast, virus-like particle release mediated by MA-deficient Gag mutants lacking the AP-3 binding site was not altered in HPS2 cells, indicating that the MA domain serves as the major viral determinant required for the recruitment of the AP-3 complex. AP-3 deficiency decreased HIV-1 Gag localization at the plasma membrane and late endosomes and increased the accumulation of HIV-1 Gag at an intermediate step between early and late endosomes. Blockage of the clathrin-mediated endocytic pathway in HPS2 cells did not reverse the inhibited virus assembly and release imposed by the AP-3 deficiency. These results demonstrate that the intact and stable AP-3 complex is required for HIV-1 assembly and release, and the involvement of the AP-3 complex in late stages of the HIV-1 replication cycle is independent of clathrin-mediated endocytosis.
[Mh] Termos MeSH primário: Complexo 3 de Proteínas Adaptadoras/metabolismo
Subunidades delta do Complexo de Proteínas Adaptadoras/metabolismo
HIV-1/fisiologia
Síndrome de Hermanski-Pudlak
Montagem de Vírus
Produtos do Gene gag do Vírus da Imunodeficiência Humana/metabolismo
[Mh] Termos MeSH secundário: Complexo 3 de Proteínas Adaptadoras/deficiência
Complexo 3 de Proteínas Adaptadoras/genética
Subunidades delta do Complexo de Proteínas Adaptadoras/deficiência
Subunidades delta do Complexo de Proteínas Adaptadoras/genética
Membrana Celular/metabolismo
Membrana Celular/virologia
Células Cultivadas
Clatrina/antagonistas & inibidores
Endocitose
Fibroblastos/virologia
HIV-1/metabolismo
Síndrome de Hermanski-Pudlak/genética
Síndrome de Hermanski-Pudlak/metabolismo
Síndrome de Hermanski-Pudlak/virologia
Seres Humanos
Mutação
Transdução de Sinais
Pele/virologia
Liberação de Vírus/genética
Produtos do Gene gag do Vírus da Imunodeficiência Humana/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (AP3D1 protein, human); 0 (Adaptor Protein Complex 3); 0 (Adaptor Protein Complex delta Subunits); 0 (Clathrin); 0 (gag Gene Products, Human Immunodeficiency Virus)
[Em] Mês de entrada:1212
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120810
[St] Status:MEDLINE


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[PMID]:22833563
[Au] Autor:Dores MR; Paing MM; Lin H; Montagne WA; Marchese A; Trejo J
[Ad] Endereço:Department of Pharmacology, School of Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
[Ti] Título:AP-3 regulates PAR1 ubiquitin-independent MVB/lysosomal sorting via an ALIX-mediated pathway.
[So] Source:Mol Biol Cell;23(18):3612-23, 2012 Sep.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The sorting of signaling receptors within the endocytic system is important for appropriate cellular responses. After activation, receptors are trafficked to early endosomes and either recycled or sorted to lysosomes and degraded. Most receptors trafficked to lysosomes are modified with ubiquitin and recruited into an endosomal subdomain enriched in hepatocyte growth factor-regulated tyrosine kinase substrate (HRS), a ubiquitin-binding component of the endosomal-sorting complex required for transport (ESCRT) machinery, and then sorted into intraluminal vesicles (ILVs) of multivesicular bodies (MVBs)/lysosomes. However, not all receptors use ubiquitin or the canonical ESCRT machinery to sort to MVBs/lysosomes. This is exemplified by protease-activated receptor-1 (PAR1), a G protein-coupled receptor for thrombin, which sorts to lysosomes independent of ubiquitination and HRS. We recently showed that the adaptor protein ALIX binds to PAR1, recruits ESCRT-III, and mediates receptor sorting to ILVs of MVBs. However, the mechanism that initiates PAR1 sorting at the early endosome is not known. We now report that the adaptor protein complex-3 (AP-3) regulates PAR1 ubiquitin-independent sorting to MVBs through an ALIX-dependent pathway. AP-3 binds to a PAR1 cytoplasmic tail-localized tyrosine-based motif and mediates PAR1 lysosomal degradation independent of ubiquitination. Moreover, AP-3 facilitates PAR1 interaction with ALIX, suggesting that AP-3 functions before PAR1 engagement of ALIX and MVB/lysosomal sorting.
[Mh] Termos MeSH primário: Complexo 3 de Proteínas Adaptadoras/metabolismo
Proteínas de Ligação ao Cálcio/metabolismo
Proteínas de Ciclo Celular/metabolismo
Complexos Endossomais de Distribuição Requeridos para Transporte/metabolismo
Lisossomos/metabolismo
Corpos Multivesiculares/metabolismo
Receptor PAR-1/metabolismo
[Mh] Termos MeSH secundário: Complexo 3 de Proteínas Adaptadoras/genética
Subunidades delta do Complexo de Proteínas Adaptadoras/genética
Subunidades delta do Complexo de Proteínas Adaptadoras/metabolismo
Proteínas de Ligação ao Cálcio/genética
Proteínas de Ciclo Celular/genética
Complexos Endossomais de Distribuição Requeridos para Transporte/genética
Células HeLa
Seres Humanos
Immunoblotting
Microscopia Confocal
Modelos Biológicos
Ligação Proteica
Transporte Proteico
Interferência de RNA
Receptor PAR-1/genética
Transdução de Sinais
Ubiquitina/metabolismo
Ubiquitinação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adaptor Protein Complex 3); 0 (Adaptor Protein Complex delta Subunits); 0 (Calcium-Binding Proteins); 0 (Cell Cycle Proteins); 0 (Endosomal Sorting Complexes Required for Transport); 0 (PDCD6IP protein, human); 0 (Receptor, PAR-1); 0 (Ubiquitin)
[Em] Mês de entrada:1303
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120727
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E12-03-0251


  8 / 35 MEDLINE  
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[PMID]:22705971
[Au] Autor:Kyere SK; Mercredi PY; Dong X; Spearman P; Summers MF
[Ad] Endereço:Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Maryland, Baltimore County, Baltimore, MD 21250, USA.
[Ti] Título:The HIV-1 matrix protein does not interact directly with the protein interactive domain of AP-3δ.
[So] Source:Virus Res;169(2):411-4, 2012 Nov.
[Is] ISSN:1872-7492
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:During the late phase of the Human Immunodeficiency Virus Type-1 (HIV-1) replication cycle, viral Gag proteins and the intact RNA genome are trafficked to specific sub-cellular membranes where virus assembly and budding occurs. Targeting to the plasma membranes of T cells and macrophages is mediated by interactions between the N-terminal matrix (MA) domain of Gag and cellular phosphatidylinositol-4,5-bisphosphate [PI(4,5)P(2)] molecules. However, in macrophages and dendritic cells, a subset of Gag proteins appears to be targeted to tetraspanin enriched viral compartments, a process that appears to be mediated by MA interactions with the Delta subunit of the cellular Adaptor Protein AP-3 (AP-3δ). We cloned, overexpressed and purified the protein interactive domain of AP-3δ and probed for MA binding by NMR. Unexpectedly, no evidence of binding was observed in these in vitro experiments, even at relatively high protein concentrations (200µM), suggesting that AP-3δ plays an alternative role in HIV-1 assembly.
[Mh] Termos MeSH primário: Complexo 3 de Proteínas Adaptadoras/metabolismo
Subunidades delta do Complexo de Proteínas Adaptadoras/metabolismo
Antígenos HIV/metabolismo
HIV-1/fisiologia
Mapeamento de Interação de Proteínas
Montagem de Vírus
Produtos do Gene gag do Vírus da Imunodeficiência Humana/metabolismo
[Mh] Termos MeSH secundário: Complexo 3 de Proteínas Adaptadoras/genética
Subunidades delta do Complexo de Proteínas Adaptadoras/genética
Clonagem Molecular
Expressão Gênica
Seres Humanos
Espectroscopia de Ressonância Magnética
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (AP3D1 protein, human); 0 (Adaptor Protein Complex 3); 0 (Adaptor Protein Complex delta Subunits); 0 (HIV Antigens); 0 (gag Gene Products, Human Immunodeficiency Virus); 0 (p17 protein, Human Immunodeficiency Virus Type 1)
[Em] Mês de entrada:1304
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120619
[St] Status:MEDLINE


  9 / 35 MEDLINE  
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[PMID]:22521722
[Au] Autor:Kent HM; Evans PR; Schäfer IB; Gray SR; Sanderson CM; Luzio JP; Peden AA; Owen DJ
[Ad] Endereço:Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.
[Ti] Título:Structural basis of the intracellular sorting of the SNARE VAMP7 by the AP3 adaptor complex.
[So] Source:Dev Cell;22(5):979-88, 2012 May 15.
[Is] ISSN:1878-1551
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:VAMP7 is involved in the fusion of late endocytic compartments with other membranes. One possible mechanism of VAMP7 delivery to these late compartments is via the AP3 trafficking adaptor. We show that the linker of the δ-adaptin subunit of AP3 binds the VAMP7 longin domain and determines the structure of their complex. Mutation of residues on both partners abolishes the interaction in vitro and in vivo. The binding of VAMP7 to δ-adaptin requires the VAMP7 SNARE motif to be engaged in SNARE complex formation and hence AP3 must transport VAMP7 when VAMP7 is part of a cis-SNARE complex. The absence of δ-adaptin causes destabilization of the AP3 complex in mouse mocha fibroblasts and mislocalization of VAMP7. The mislocalization can be rescued by transfection with wild-type δ-adaptin but not by δ-adaptin containing mutations that abolish VAMP7 binding, despite in all cases intact AP3 being present and LAMP1 trafficking being rescued.
[Mh] Termos MeSH primário: Complexo 3 de Proteínas Adaptadoras/metabolismo
Subunidades delta do Complexo de Proteínas Adaptadoras/metabolismo
Transporte Proteico/fisiologia
Proteínas R-SNARE/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Linhagem Celular
Membrana Celular/metabolismo
Cristalografia por Raios X
Endocitose
Endossomos/metabolismo
Fibroblastos
Citometria de Fluxo
Seres Humanos
Camundongos
Dados de Sequência Molecular
Mutação
Ligação Proteica
Estrutura Terciária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adaptor Protein Complex 3); 0 (Adaptor Protein Complex delta Subunits); 0 (R-SNARE Proteins); 0 (Sybl1 protein, mouse)
[Em] Mês de entrada:1207
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120424
[St] Status:MEDLINE
[do] DOI:10.1016/j.devcel.2012.01.018


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[PMID]:21411634
[Au] Autor:Zlatic SA; Tornieri K; L'Hernault SW; Faundez V
[Ad] Endereço:Department of Cell Biology, Emory University, Atlanta, GA 30322, USA.
[Ti] Título:Clathrin-dependent mechanisms modulate the subcellular distribution of class C Vps/HOPS tether subunits in polarized and nonpolarized cells.
[So] Source:Mol Biol Cell;22(10):1699-715, 2011 May 15.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Coats define the composition of carriers budding from organelles. In addition, coats interact with membrane tethers required for vesicular fusion. The yeast AP-3 (Adaptor Protein Complex 3) coat and the class C Vps/HOPS (HOmotypic fusion and Protein Sorting) tether follow this model as their interaction occurs at the carrier fusion step. Here we show that mammalian Vps class C/HOPS subunits and clathrin interact and that acute perturbation of clathrin function disrupts the endosomal distribution of Vps class C/HOPS tethers in HEK293T and polarized neuronal cells. Vps class C/HOPS subunits and clathrin exist in complex with either AP-3 or hepatocyte growth factor receptor substrate (Hrs). Moreover, Vps class C/HOPS proteins cofractionate with clathrin-coated vesicles, which are devoid of Hrs. Expression of FK506 binding protein (FKBP)-clathrin light chain chimeras, to inhibit clathrin membrane association dynamics, increased Vps class C/HOPS subunit content in rab5 endosomal compartments. Additionally, Vps class C/HOPS subunits were concentrated at tips of neuronal processes, and their delivery was impaired by expression of FKBP-clathrin chimeras and AP20187 incubation. These data support a model in which Vps class C/HOPS subunits incorporate into clathrin-coated endosomal domains and carriers in mammalian cells. We propose that vesicular (AP-3) and nonvesicular (Hrs) clathrin mechanisms segregate class C Vps/HOPS tethers to organelles and domains of mammalian cells bearing complex architectures.
[Mh] Termos MeSH primário: Polaridade Celular
Clatrina/metabolismo
Proteínas de Transporte Vesicular/metabolismo
[Mh] Termos MeSH secundário: Complexo 3 de Proteínas Adaptadoras/metabolismo
Subunidades delta do Complexo de Proteínas Adaptadoras/metabolismo
Animais
Linhagem Celular
Clatrina/antagonistas & inibidores
Clatrina/genética
Vesículas Revestidas por Clatrina/efeitos dos fármacos
Vesículas Revestidas por Clatrina/metabolismo
Endossomos/efeitos dos fármacos
Endossomos/metabolismo
Seres Humanos
Imunoprecipitação
Complexos Multiproteicos/metabolismo
Neurônios/metabolismo
Ligação Proteica
Subunidades Proteicas/metabolismo
Ratos
Proteínas Recombinantes de Fusão/metabolismo
Tacrolimo/análogos & derivados
Tacrolimo/farmacologia
Proteínas de Transporte Vesicular/genética
Proteínas rab de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (AP20187); 0 (AP3D1 protein, human); 0 (Adaptor Protein Complex 3); 0 (Adaptor Protein Complex delta Subunits); 0 (Clathrin); 0 (Multiprotein Complexes); 0 (Protein Subunits); 0 (Recombinant Fusion Proteins); 0 (Vesicular Transport Proteins); EC 3.6.5.2 (rab GTP-Binding Proteins); WM0HAQ4WNM (Tacrolimus)
[Em] Mês de entrada:1109
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110318
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E10-10-0799



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