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Pesquisa : D12.776.543.990.150.500.400 [Categoria DeCS]
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  1 / 101 MEDLINE  
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[PMID]:28823958
[Au] Autor:Tao X; Lu Y; Qiu S; Wang Y; Qin J; Fan Z
[Ad] Endereço:Department of Oral Medicine, Guanghua School of Stomatology, Sun Yat-Sen University, Guangzhou, Guangdong 510055, China; Department of Experimental Therapeutics, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA.
[Ti] Título:AP1G1 is involved in cetuximab-mediated downregulation of ASCT2-EGFR complex and sensitization of human head and neck squamous cell carcinoma cells to ROS-induced apoptosis.
[So] Source:Cancer Lett;408:33-42, 2017 Nov 01.
[Is] ISSN:1872-7980
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:In this study, we expanded our recent work showing that ASCT2, a Na -dependent neutral amino acid transporter that plays a major role in glutamine uptake in cancer cells, is physically associated with EGFR in human head and neck squamous cell carcinoma cells and in several other types of cancer cells. We found in our current study that ASCT2 can be downregulated by cetuximab, an approved anti-EGFR therapeutic antibody, via cetuximab-induced EGFR endocytosis independently of cetuximab-mediated inhibition of EGFR tyrosine kinase. We further found that ASCT2-EGFR association involves the adaptor-related protein complex 1 gamma 1 subunit (AP1G1), a subunit of clathrin-associated adaptor protein complex 1, which plays a role in membrane protein sorting in endosomes after receptor-mediated endocytosis. We found that AP1G1 is physically associated with both ASCT2 and EGFR and, together with those molecules, forms a heterotrimeric molecular complex. Knockdown of AP1G1 lowered the level of ASCT2-EGFR association, inhibited cetuximab-mediated internalization of ASCT2-EGFR complex, and decreased intracellular glutamine uptake and glutathione biosynthesis. These findings suggest a new therapeutic strategy to overcome cetuximab resistance in cancer cells through combination of cetuximab, which co-targets ASCT2 along with EGFR, with an ROS-inducing agent.
[Mh] Termos MeSH primário: Subunidades gama do Complexo de Proteínas Adaptadoras/metabolismo
Sistema ASC de Transporte de Aminoácidos/antagonistas & inibidores
Apoptose/efeitos dos fármacos
Cetuximab/farmacologia
Resistência a Medicamentos Antineoplásicos
Neoplasias de Cabeça e Pescoço/patologia
Espécies Reativas de Oxigênio/metabolismo
Receptor do Fator de Crescimento Epidérmico/antagonistas & inibidores
[Mh] Termos MeSH secundário: Subunidades gama do Complexo de Proteínas Adaptadoras/genética
Sistema ASC de Transporte de Aminoácidos/genética
Sistema ASC de Transporte de Aminoácidos/metabolismo
Antineoplásicos/farmacologia
Carcinoma de Células Escamosas/tratamento farmacológico
Carcinoma de Células Escamosas/metabolismo
Carcinoma de Células Escamosas/patologia
Proliferação Celular/efeitos dos fármacos
Neoplasias de Cabeça e Pescoço/tratamento farmacológico
Neoplasias de Cabeça e Pescoço/metabolismo
Seres Humanos
Antígenos de Histocompatibilidade Menor/genética
Antígenos de Histocompatibilidade Menor/metabolismo
Receptor do Fator de Crescimento Epidérmico/genética
Receptor do Fator de Crescimento Epidérmico/metabolismo
Células Tumorais Cultivadas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Protein Complex gamma Subunits); 0 (Amino Acid Transport System ASC); 0 (Antineoplastic Agents); 0 (Minor Histocompatibility Antigens); 0 (Reactive Oxygen Species); 0 (SLC1A5 protein, human); EC 2.7.10.1 (EGFR protein, human); EC 2.7.10.1 (Receptor, Epidermal Growth Factor); PQX0D8J21J (Cetuximab)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170822
[St] Status:MEDLINE


  2 / 101 MEDLINE  
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[PMID]:27909244
[Au] Autor:Tavares LA; da Silva EM; da Silva-Januário ME; Januário YC; de Cavalho JV; Czernisz ÉS; Mardones GA; daSilva LL
[Ad] Endereço:Department of Cell and Molecular Biology, Ribeirão Preto Medical School, University of São Paulo, Ribeirão Preto, São Paulo 14049-900, Brazil.
[Ti] Título:CD4 downregulation by the HIV-1 protein Nef reveals distinct roles for the γ1 and γ2 subunits of the AP-1 complex in protein trafficking.
[So] Source:J Cell Sci;130(2):429-443, 2017 Jan 15.
[Is] ISSN:1477-9137
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The HIV accessory protein Nef is a major determinant of viral pathogenesis that facilitates viral particle release, prevents viral antigen presentation and increases infectivity of new virus particles. These functions of Nef involve its ability to remove specific host proteins from the surface of infected cells, including the CD4 receptor. Nef binds to the adaptor protein 2 (AP-2) and CD4 in clathrin-coated pits, forcing CD4 internalization and its subsequent targeting to lysosomes. Herein, we report that this lysosomal targeting requires a variant of AP-1 containing isoform 2 of γ-adaptin (AP1G2, hereafter γ2). Depletion of the γ2 or µ1A (AP1M1) subunits of AP-1, but not of γ1 (AP1G1), precludes Nef-mediated lysosomal degradation of CD4. In γ2-depleted cells, CD4 internalized by Nef accumulates in early endosomes and this alleviates CD4 removal from the cell surface. Depletion of γ2 also hinders EGFR-EGF-complex targeting to lysosomes, an effect that is not observed upon γ1 depletion. Taken together, our data provide evidence that the presence of γ1 or γ2 subunits delineates two distinct variants of AP-1 complexes, with different functions in protein sorting.
[Mh] Termos MeSH primário: Subunidades gama do Complexo de Proteínas Adaptadoras/metabolismo
Antígenos CD4/metabolismo
Regulação para Baixo
HIV-1/metabolismo
Produtos do Gene nef do Vírus da Imunodeficiência Humana/metabolismo
[Mh] Termos MeSH secundário: Endocitose
Complexos Endossomais de Distribuição Requeridos para Transporte/metabolismo
Endossomos/metabolismo
Fator de Crescimento Epidérmico/metabolismo
Técnicas de Silenciamento de Genes
Proteínas de Fluorescência Verde/metabolismo
Células HeLa
Seres Humanos
Lisossomos/metabolismo
Fosfoproteínas/metabolismo
Ligação Proteica
Transporte Proteico
Proteólise
Receptor do Fator de Crescimento Epidérmico/metabolismo
Técnicas do Sistema de Duplo-Híbrido
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Protein Complex gamma Subunits); 0 (CD4 Antigens); 0 (Endosomal Sorting Complexes Required for Transport); 0 (Phosphoproteins); 0 (hepatocyte growth factor-regulated tyrosine kinase substrate); 0 (nef Gene Products, Human Immunodeficiency Virus); 0 (nef protein, Human immunodeficiency virus 1); 147336-22-9 (Green Fluorescent Proteins); 62229-50-9 (Epidermal Growth Factor); EC 2.7.10.1 (Receptor, Epidermal Growth Factor)
[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:161203
[St] Status:MEDLINE
[do] DOI:10.1242/jcs.192104


  3 / 101 MEDLINE  
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[PMID]:25351491
[Au] Autor:Wang X; Cai Y; Wang H; Zeng Y; Zhuang X; Li B; Jiang L
[Ad] Endereço:School of Life Sciences, Centre for Cell and Developmental Biology and State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong, China.
[Ti] Título:Trans-Golgi network-located AP1 gamma adaptins mediate dileucine motif-directed vacuolar targeting in Arabidopsis.
[So] Source:Plant Cell;26(10):4102-18, 2014 Oct.
[Is] ISSN:1532-298X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Membrane proteins on the tonoplast are indispensible for vacuolar functions in plants. However, how these proteins are transported to the vacuole and how they become separated from plasma membrane proteins remain largely unknown. In this study, we used Arabidopsis thaliana vacuolar ion transporter1 (VIT1) as a reporter to study the mechanisms of tonoplast targeting. We showed that VIT1 reached the tonoplast through a pathway involving the endoplasmic reticulum (ER), Golgi, trans-Golgi network (TGN), prevacuolar compartment, and tonoplast. VIT1 contains a putative N-terminal dihydrophobic type ER export signal, and its N terminus has a conserved dileucine motif (EKQTLL), which is responsible for tonoplast targeting. In vitro peptide binding assays with synthetic VIT1 N terminus identified adaptor protein complex-1 (AP1) subunits that interacted with the dileucine motif. A deficiency of AP1 gamma adaptins in Arabidopsis cells caused relocation of tonoplast proteins containing the dileucine motif, such as VIT1 and inositol transporter1, to the plasma membrane. The dileucine motif also effectively rerouted the plasma membrane protein SCAMP1 to the tonoplast. Together with subcellular localization studies showing that AP1 gamma adaptins localize to the TGN, we propose that the AP1 complex on the TGN mediates tonoplast targeting of membrane proteins with the dileucine motif.
[Mh] Termos MeSH primário: Subunidades gama do Complexo de Proteínas Adaptadoras/metabolismo
Proteínas de Arabidopsis/metabolismo
Arabidopsis/metabolismo
Oligopeptídeos/metabolismo
Vacúolos/metabolismo
Rede trans-Golgi/metabolismo
[Mh] Termos MeSH secundário: Subunidades gama do Complexo de Proteínas Adaptadoras/genética
Motivos de Aminoácidos/genética
Sequência de Aminoácidos
Arabidopsis/genética
Proteínas de Arabidopsis/genética
Proteínas de Transporte de Cátions/genética
Proteínas de Transporte de Cátions/metabolismo
Retículo Endoplasmático/metabolismo
Immunoblotting
Membranas Intracelulares/metabolismo
Leucina/genética
Leucina/metabolismo
Microscopia Confocal
Dados de Sequência Molecular
Mutação
Oligopeptídeos/genética
Peptídeos/genética
Peptídeos/metabolismo
Plantas Geneticamente Modificadas
Ligação Proteica
Transporte Proteico
Protoplastos/metabolismo
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adaptor Protein Complex gamma Subunits); 0 (Arabidopsis Proteins); 0 (Cation Transport Proteins); 0 (Oligopeptides); 0 (Peptides); 0 (VIT1 protein, Arabidopsis); GMW67QNF9C (Leucine)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141030
[St] Status:MEDLINE
[do] DOI:10.1105/tpc.114.129759


  4 / 101 MEDLINE  
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[PMID]:24006255
[Au] Autor:Perrin L; Laura P; Lacas-Gervais S; Sandra LG; Gilleron J; Jérôme G; Ceppo F; Franck C; Prodon F; François P; Benmerah A; Alexandre B; Tanti JF; Jean-François T; Cormont M; Mireille C
[Ti] Título:Rab4b controls an early endosome sorting event by interacting with the γ-subunit of the clathrin adaptor complex 1.
[So] Source:J Cell Sci;126(Pt 21):4950-62, 2013 Nov 01.
[Is] ISSN:1477-9137
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The endocytic pathway is essential for cell homeostasis and numerous small Rab GTPases are involved in its control. The endocytic trafficking step controlled by Rab4b has not been elucidated, although recent data suggested it could be important for glucose homeostasis, synaptic homeostasis or adaptive immunity. Here, we show that Rab4b is required for early endosome sorting of transferrin receptors (TfRs) to the recycling endosomes, and we identified the AP1γ subunit of the clathrin adaptor AP-1 as a Rab4b effector and key component of the machinery of early endosome sorting. We show that internalised transferrin (Tf) does not reach Vamp3/Rab11 recycling endosomes in the absence of Rab4b, whereas it is rapidly recycled back to the plasma membrane. By contrast, overexpression of Rab4b leads to the accumulation of internalised Tf within AP-1- and clathrin-coated vesicles. These vesicles are poor in early and recycling endocytic markers except for TfR and require AP1γ for their formation. Furthermore, the targeted overexpression of the Rab4b-binding domain of AP1γ to early endosome upon its fusion with FYVE domains inhibited the interaction between Rab4b and endogenous AP1γ, and perturbed Tf traffic. We thus proposed that the interaction between early endocytic Rab4b and AP1γ could allow the budding of clathrin-coated vesicles for subsequent traffic to recycling endosomes. The data also uncover a novel type of endosomes, characterised by low abundance of either early or recycling endocytic markers, which could potentially be generated in cell types that naturally express high level of Rab4b.
[Mh] Termos MeSH primário: Subunidades gama do Complexo de Proteínas Adaptadoras/metabolismo
Endossomos/metabolismo
Proteínas rab4 de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Subunidades gama do Complexo de Proteínas Adaptadoras/genética
Transporte Biológico
Membrana Celular/enzimologia
Membrana Celular/genética
Membrana Celular/metabolismo
Vesículas Revestidas por Clatrina/metabolismo
Endocitose
Endossomos/enzimologia
Endossomos/genética
Células HeLa
Seres Humanos
Ligação Proteica
Transporte Proteico
Transferrina/genética
Transferrina/metabolismo
Proteínas rab4 de Ligação ao GTP/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adaptor Protein Complex gamma Subunits); 0 (Transferrin); EC 3.6.5.2 (rab4 GTP-Binding Proteins)
[Em] Mês de entrada:1406
[Cu] Atualização por classe:131031
[Lr] Data última revisão:
131031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130906
[St] Status:MEDLINE
[do] DOI:10.1242/jcs.130575


  5 / 101 MEDLINE  
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[PMID]:23851574
[Au] Autor:Jürgens MC; Vörös J; Rautureau GJ; Shepherd DA; Pye VE; Muldoon J; Johnson CM; Ashcroft AE; Freund SM; Ferguson N
[Ad] Endereço:1] School of Medicine and Medical Science, University College Dublin, Dublin, Ireland. [2].
[Ti] Título:The hepatitis B virus preS1 domain hijacks host trafficking proteins by motif mimicry.
[So] Source:Nat Chem Biol;9(9):540-7, 2013 Sep.
[Is] ISSN:1552-4469
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hepatitis B virus (HBV) is an infectious, potentially lethal human pathogen. However, there are no effective therapies for chronic HBV infections. Antiviral development is hampered by the lack of high-resolution structures for essential HBV protein-protein interactions. The interaction between preS1, an HBV surface-protein domain, and its human binding partner, γ2-adaptin, subverts the membrane-trafficking apparatus to mediate virion export. This interaction is a putative drug target. We report here atomic-resolution descriptions of the binding thermodynamics and structural biology of the interaction between preS1 and the EAR domain of γ2-adaptin. NMR, protein engineering, X-ray crystallography and MS showed that preS1 contains multiple γ2-EAR-binding motifs that mimic the membrane-trafficking motifs (and binding modes) of host proteins. These motifs localize together to a relatively rigid, functionally important region of preS1, an intrinsically disordered protein. The preS1-γ2-EAR interaction was relatively weak and efficiently outcompeted by a synthetic peptide. Our data provide the structural road map for developing peptidomimetic antivirals targeting the γ2-EAR-preS1 interaction.
[Mh] Termos MeSH primário: Subunidades gama do Complexo de Proteínas Adaptadoras/metabolismo
Antígenos de Superfície da Hepatite B/química
Antígenos de Superfície da Hepatite B/metabolismo
Vírus da Hepatite B/metabolismo
Mimetismo Molecular
Precursores de Proteínas/química
Precursores de Proteínas/metabolismo
[Mh] Termos MeSH secundário: Subunidades gama do Complexo de Proteínas Adaptadoras/química
Motivos de Aminoácidos
Estrutura Terciária de Proteína
Termodinâmica
[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 gamma Subunits); 0 (Hepatitis B Surface Antigens); 0 (Protein Precursors); 0 (presurface protein 1, hepatitis B surface antigen)
[Em] Mês de entrada:1311
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130716
[St] Status:MEDLINE
[do] DOI:10.1038/nchembio.1294


  6 / 101 MEDLINE  
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[PMID]:23733933
[Au] Autor:Park M; Song K; Reichardt I; Kim H; Mayer U; Stierhof YD; Hwang I; Jürgens G
[Ad] Endereço:Entwicklungsgenetik and Microscopy, Zentrum für Molekularbiologie der Pflanzen (ZMBP), University of Tübingen, 72076 Tübingen, Germany.
[Ti] Título:Arabidopsis µ-adaptin subunit AP1M of adaptor protein complex 1 mediates late secretory and vacuolar traffic and is required for growth.
[So] Source:Proc Natl Acad Sci U S A;110(25):10318-23, 2013 Jun 18.
[Is] ISSN:1091-6490
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Adaptor protein (AP) complexes are the predominant coat proteins of membrane vesicles in post-Golgi trafficking of mammalian cells. Each AP complex contains a specific medium subunit, µ-adaptin, that selects cargo proteins bearing sequence-specific sorting motifs. Much less is known about the AP complexes and their µ subunits in plants. Because of uncertain homology, the µ-adaptins of Arabidopsis have been designated muA through muD [Happel et al. (2004) Plant J 37(5):678-693]. Furthermore, only muD has been assigned to a specific AP complex, AP-3, involved in Golgi-vacuolar trafficking [Niihama et al. (2009) Plant Cell Physiol 50(12):2057-2068, Zwiewka et al. (2011) Cell Res 21(12):1711-1722, and Wolfenstetter et al. (2012) Plant Cell 24(1):215-232]. In contrast, the µ subunit of neither the post-Golgi trafficking AP-1 complex nor the endocytic AP-2 complex has been identified. Here, we report the functional analysis of redundant AP-1 µ-adaptins AP1M1 (also known as muB1) and AP1M2 (also known as muB2). Coimmunoprecipitation revealed that both AP1M2 and its less strongly expressed isoform AP1M1 are complexed with the large subunit γ-adaptin of AP-1. In addition, AP1M2 was localized at or near the trans-Golgi network. Knockout mutations of AP1M2 impaired pollen function and arrested plant growth whereas the ap1m1 ap1m2 double mutant was nearly pollen-lethal. At the cellular level, the absence of AP1M2 entailed inhibition of multiple trafficking pathways from the trans-Golgi network to the vacuole and to the plasma membrane in interphase and to the plane of cell division in cytokinesis. Thus, AP-1 is crucial in post-Golgi trafficking in plant cells and required for cell division and plant growth.
[Mh] Termos MeSH primário: Complexo 1 de Proteínas Adaptadoras/metabolismo
Subunidades mu do Complexo de Proteínas Adaptadoras/metabolismo
Proteínas de Arabidopsis/metabolismo
Arabidopsis/crescimento & desenvolvimento
Arabidopsis/genética
Transporte Proteico/fisiologia
[Mh] Termos MeSH secundário: Complexo 1 de Proteínas Adaptadoras/genética
Subunidades alfa do Complexo de Proteínas Adaptadoras/metabolismo
Subunidades gama do Complexo de Proteínas Adaptadoras/metabolismo
Subunidades mu do Complexo de Proteínas Adaptadoras/genética
Arabidopsis/metabolismo
Proteínas de Arabidopsis/genética
Membrana Celular/fisiologia
Membrana Celular/ultraestrutura
Citocinese/fisiologia
Complexo de Golgi/metabolismo
Complexo de Golgi/ultraestrutura
Interfase/fisiologia
Microscopia Eletrônica de Transmissão
Mutagênese Insercional
Vesículas Secretórias/metabolismo
Vesículas Secretórias/ultraestrutura
Vacúolos/metabolismo
Vacúolos/ultraestrutura
Rede trans-Golgi/metabolismo
Rede trans-Golgi/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (AP1M1 protein, Arabidopsis); 0 (AP1M2 protein, Arabidopsis); 0 (Adaptor Protein Complex 1); 0 (Adaptor Protein Complex alpha Subunits); 0 (Adaptor Protein Complex gamma Subunits); 0 (Adaptor Protein Complex mu Subunits); 0 (Arabidopsis Proteins); 0 (adaptor protein complex 1, mu 1 subunit); 0 (adaptor protein complex 1, mu 2 subunit)
[Em] Mês de entrada:1309
[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:10.1073/pnas.1300460110


  7 / 101 MEDLINE  
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[PMID]:23326640
[Au] Autor:Guo Y; Zanetti G; Schekman R
[Ad] Endereço:Department of Molecular and Cell Biology , Howard Hughes Medical Institute, University of California-Berkeley , Berkeley , United States.
[Ti] Título:A novel GTP-binding protein-adaptor protein complex responsible for export of Vangl2 from the trans Golgi network.
[So] Source:Elife;2:e00160, 2013 Jan 08.
[Is] ISSN:2050-084X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Planar cell polarity (PCP) requires the asymmetric sorting of distinct signaling receptors to distal and proximal surfaces of polarized epithelial cells. We have examined the transport of one PCP signaling protein, Vangl2, from the trans Golgi network (TGN) in mammalian cells. Using siRNA knockdown experiments, we find that the GTP-binding protein, Arfrp1, and the clathrin adaptor complex 1 (AP-1) are required for Vangl2 transport from the TGN. In contrast, TGN export of Frizzled 6, which localizes to the opposing epithelial surface from Vangl2, does not depend on Arfrp1 or AP-1. Mutagenesis studies identified a YYXXF sorting signal in the C-terminal cytosolic domain of Vangl2 that is required for Vangl2 traffic and interaction with the µ subunit of AP-1. We propose that Arfrp1 exposes a binding site on AP-1 that recognizes the Vangl2 sorting motif for capture into a transport vesicle destined for the proximal surface of a polarized epithelial cell.DOI:http://dx.doi.org/10.7554/eLife.00160.001.
[Mh] Termos MeSH primário: Fatores de Ribosilação do ADP/metabolismo
Polaridade Celular
Células Epiteliais/metabolismo
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Proteínas de Membrana/metabolismo
Rede trans-Golgi/metabolismo
[Mh] Termos MeSH secundário: Fatores de Ribosilação do ADP/genética
Complexo 1 de Proteínas Adaptadoras/metabolismo
Subunidades gama do Complexo de Proteínas Adaptadoras/metabolismo
Subunidades mu do Complexo de Proteínas Adaptadoras/metabolismo
Sequência de Aminoácidos
Animais
Sítios de Ligação
Células COS
Caderinas/metabolismo
Moléculas de Adesão Celular/metabolismo
Cercopithecus aethiops
Receptores Frizzled/metabolismo
Células HeLa
Seres Humanos
Peptídeos e Proteínas de Sinalização Intracelular/genética
Proteínas de Membrana/genética
Dados de Sequência Molecular
Mutação
Fosforilação
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Proteína Quinase C/metabolismo
Transporte Proteico
Interferência de RNA
Receptores Proteína Tirosina Quinases/metabolismo
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adaptor Protein Complex 1); 0 (Adaptor Protein Complex gamma Subunits); 0 (Adaptor Protein Complex mu Subunits); 0 (CELSR1 cadherin, human); 0 (Cadherins); 0 (Cell Adhesion Molecules); 0 (FZD6 protein, human); 0 (Frizzled Receptors); 0 (Intracellular Signaling Peptides and Proteins); 0 (Membrane Proteins); 0 (VANGL2 protein, human); EC 2.7.10.- (protein kinase D); EC 2.7.10.1 (PTK7 protein, human); EC 2.7.10.1 (Receptor Protein-Tyrosine Kinases); EC 2.7.11.13 (Protein Kinase C); EC 3.6.5.2 (ADP-Ribosylation Factors); EC 3.6.5.2 (ARFRP1 protein, human)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130118
[St] Status:MEDLINE
[do] DOI:10.7554/eLife.00160


  8 / 101 MEDLINE  
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[PMID]:22389401
[Au] Autor:Kametaka S; Kametaka A; Yonekura S; Haruta M; Takenoshita S; Goto S; Waguri S
[Ad] Endereço:Department of Anatomy and Histology, Fukushima Medical University, 1 Hikarigaoka, Fukushima, Fukushima 960-1295, Japan. kametaks@fmu.ac.jp
[Ti] Título:AP-1 clathrin adaptor and CG8538/Aftiphilin are involved in Notch signaling during eye development in Drosophila melanogaster.
[So] Source:J Cell Sci;125(Pt 3):634-48, 2012 Feb 01.
[Is] ISSN:1477-9137
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Clathrin adaptor protein complex-1 (AP-1) and its accessory proteins play a role in the sorting of integral membrane proteins at the trans-Golgi network and endosomes. Their physiological functions in complex organisms, however, are not fully understood. In this study, we found that CG8538p, an uncharacterized Drosophila protein, shares significant structural and functional characteristics with Aftiphilin, a mammalian AP-1 accessory protein. The Drosophila Aftiphilin was shown to interact directly with the ear domain of γ-adaptin of Drosophila AP-1, but not with the GAE domain of Drosophila GGA. In S2 cells, Drosophila Aftiphilin and AP-1 formed a complex and colocalized at the Golgi compartment. Moreover, tissue-specific depletion of AP-1 or Aftiphilin in the developing eyes resulted in a disordered alignment of photoreceptor neurons in larval stage and roughened eyes with aberrant ommatidia in adult flies. Furthermore, AP-1-depleted photoreceptor neurons showed an intracellular accumulation of a Notch regulator, Scabrous, and downregulation of Notch by promoting its degradation in the lysosomes. These results suggest that AP-1 and Aftiphilin are cooperatively involved in the intracellular trafficking of Notch during eye development in Drosophila.
[Mh] Termos MeSH primário: Proteínas de Drosophila/metabolismo
Drosophila melanogaster/crescimento & desenvolvimento
Drosophila melanogaster/metabolismo
Olho/crescimento & desenvolvimento
Olho/metabolismo
Receptores Notch/metabolismo
Fator de Transcrição AP-1/metabolismo
[Mh] Termos MeSH secundário: Subunidades gama do Complexo de Proteínas Adaptadoras/química
Subunidades gama do Complexo de Proteínas Adaptadoras/genética
Subunidades gama do Complexo de Proteínas Adaptadoras/metabolismo
Sequência de Aminoácidos
Animais
Proteínas de Transporte/genética
Proteínas de Transporte/metabolismo
Compartimento Celular
Linhagem Celular
Proteínas de Drosophila/química
Proteínas de Drosophila/genética
Drosophila melanogaster/genética
Endossomos/metabolismo
Anormalidades do Olho/genética
Anormalidades do Olho/metabolismo
Técnicas de Silenciamento de Genes
Glicoproteínas/metabolismo
Seres Humanos
Lisossomos/metabolismo
Dados de Sequência Molecular
Proteínas do Tecido Nervoso/genética
Proteínas do Tecido Nervoso/metabolismo
Células Fotorreceptoras de Invertebrados/citologia
Células Fotorreceptoras de Invertebrados/metabolismo
Domínios e Motivos de Interação entre Proteínas
Transporte Proteico
Interferência de RNA
Receptores Notch/genética
Homologia de Sequência de Aminoácidos
Transdução de Sinais
Fator de Transcrição AP-1/química
Fator de Transcrição AP-2/química
Fator de Transcrição AP-2/metabolismo
Rede trans-Golgi/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (AFTPH protein, human); 0 (AP-2 protein, Drosophila); 0 (Adaptor Protein Complex gamma Subunits); 0 (Carrier Proteins); 0 (Drosophila Proteins); 0 (Glycoproteins); 0 (Nerve Tissue Proteins); 0 (Receptors, Notch); 0 (Transcription Factor AP-1); 0 (Transcription Factor AP-2); 0 (notch protein, Drosophila); 0 (scabrous protein, Drosophila)
[Em] Mês de entrada:1209
[Cu] Atualização por classe:120305
[Lr] Data última revisão:
120305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120306
[St] Status:MEDLINE
[do] DOI:10.1242/jcs.090167


  9 / 101 MEDLINE  
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[PMID]:21448433
[Au] Autor:Antrobus R; Borner GH
[Ad] Endereço:Cambridge Institute for Medical Research, Wellcome Trust, Addenbrooke's Hospital, University of Cambridge, Cambridge, United Kingdom.
[Ti] Título:Improved elution conditions for native co-immunoprecipitation.
[So] Source:PLoS One;6(3):e18218, 2011 Mar 23.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Native immunoprecipitation followed by protein A-mediated recovery of the immuno-complex is a powerful tool to study protein-protein interactions. A limitation of this technique is the concomitant recovery of large amounts of immunoglobulin, which interferes with down-stream applications such as mass spectrometric analysis and Western blotting. Here we report a detergent-based "soft" elution protocol that allows effective recovery of immunoprecipitated antigen and binding partners, yet avoids elution of the bulk of the immunoglobulin. METHODOLOGY/PRINCIPAL FINDINGS: We assessed the performance of the soft elution protocol using immunoprecipitation of Adaptor protein complex 1 (AP-1) and associated proteins as a test case. Relative to conventional elution conditions, the novel protocol substantially improved the sensitivity of mass spectrometric identification of immunoprecipitated proteins from unfractionated solution digests. Averaging over three independent experiments, Mascot scores of identified AP-1 binding partners were increased by 39%. Conversely, the estimated amount of recovered immunoglobulin was reduced by 44%. We tested the protocol with five further antibodies derived from rabbit, mouse and goat. In each case we observed a significant reduction of co-eluting immunoglobulin. CONCLUSIONS/SIGNIFICANCE: The soft elution protocol presented here shows superior performance compared to standard elution conditions for subsequent protein identification by mass spectrometry from solution digests. The method was developed for rabbit polyclonal antibodies, but also performed well with the tested goat and mouse antibodies. Hence we expect the soft elution protocol to be widely applicable.
[Mh] Termos MeSH primário: Imunoprecipitação/métodos
Imunoprecipitação/normas
[Mh] Termos MeSH secundário: Subunidades gama do Complexo de Proteínas Adaptadoras/química
Subunidades gama do Complexo de Proteínas Adaptadoras/isolamento & purificação
Animais
Eletroforese em Gel de Poliacrilamida
Cabras
Células HeLa
Seres Humanos
Imunoglobulinas/isolamento & purificação
Espectrometria de Massas
Camundongos
Coelhos
Padrões de Referência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adaptor Protein Complex gamma Subunits); 0 (Immunoglobulins)
[Em] Mês de entrada:1107
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110331
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0018218


  10 / 101 MEDLINE  
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[PMID]:20708039
[Au] Autor:Döring T; Gotthardt K; Stieler J; Prange R
[Ad] Endereço:Department of Medicine Microbiology and Hygiene, Universitätsmedizin der Johannes Gutenberg-Universität Mainz, Augustusplatz, Mainz, Germany.
[Ti] Título:γ2-Adaptin is functioning in the late endosomal sorting pathway and interacts with ESCRT-I and -III subunits.
[So] Source:Biochim Biophys Acta;1803(11):1252-64, 2010 Nov.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:γ2-Adaptin is a clathrin adaptor-related protein with unclear physiological function. Previous studies indicated that γ2-adaptin might act within the multivesicular body (MVB) protein-sorting pathway that is central to receptor down-regulation, lysosome biogenesis, and budding of enveloped viruses. Here, we have analyzed the effects of excess and deficit γ2-adaptin on exogenous and endogenous MVB cargoes and on the MVB machinery itself. Foreign cargoes, like retroviral Gags, are entrapped by overexpressed γ2-adaptin in detergent-insoluble polymers and blocked in budding. When viral budding involves MVB/endosomal structures, excess γ2-adaptin acts by accelerating lysosomal Gag destruction. Consistently, depletion of γ2-adaptin avoids Gag routing to the lysosome and increases viral production. Functional studies with natural MVB cargoes support a role of γ2-adaptin in MVB-to-lysosome transition. Furthermore, we show that different members of the endosomal sorting complex required for transport (ESCRT) that drive sorting from endosomes to lysosomes are sequestered upon γ2-adaptin overexpression. If sequestered irreversibly, they are targeted to enhanced lysosomal degradation. The participation of γ2-adaptin in MVB sorting is further suggested by our finding that it specifically interacts with the ESCRT subunits Vps28 and CHMP2A. These observations identify γ2-adaptin as a critical factor in MVB trafficking, which likely is involved in endosome-to-lysosome maturation.
[Mh] Termos MeSH primário: Subunidades gama do Complexo de Proteínas Adaptadoras/fisiologia
Complexos Endossomais de Distribuição Requeridos para Transporte/metabolismo
Endossomos/metabolismo
Transdução de Sinais/fisiologia
[Mh] Termos MeSH secundário: Subunidades gama do Complexo de Proteínas Adaptadoras/genética
Subunidades gama do Complexo de Proteínas Adaptadoras/metabolismo
Biomarcadores Tumorais/genética
Biomarcadores Tumorais/metabolismo
Linhagem Celular Tumoral
Complexos Endossomais de Distribuição Requeridos para Transporte/genética
Produtos do Gene gag/genética
Produtos do Gene gag/metabolismo
Seres Humanos
Immunoblotting
Proteínas Luminescentes/genética
Proteínas Luminescentes/metabolismo
Lisossomos/metabolismo
Microscopia de Fluorescência
Corpos Multivesiculares/metabolismo
Ligação Proteica
Transporte Proteico
Interferência de RNA
Retroviridae/genética
Retroviridae/crescimento & desenvolvimento
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adaptor Protein Complex gamma Subunits); 0 (Biomarkers, Tumor); 0 (CHMP2A protein, human); 0 (Endosomal Sorting Complexes Required for Transport); 0 (Gene Products, gag); 0 (Luminescent Proteins); 0 (VPS28 protein, human)
[Em] Mês de entrada:1011
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100817
[St] Status:MEDLINE
[do] DOI:10.1016/j.bbamcr.2010.08.001



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