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Pesquisa : D12.776.543.990.150.500.500 [Categoria DeCS]
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[PMID]:28743825
[Au] Autor:Navarro Negredo P; Edgar JR; Wrobel AG; Zaccai NR; Antrobus R; Owen DJ; Robinson MS
[Ad] Endereço:Cambridge Institute for Medical Research, University of Cambridge, Cambridge, England, UK.
[Ti] Título:Contribution of the clathrin adaptor AP-1 subunit µ1 to acidic cluster protein sorting.
[So] Source:J Cell Biol;216(9):2927-2943, 2017 Sep 04.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Acidic clusters act as sorting signals for packaging cargo into clathrin-coated vesicles (CCVs), and also facilitate down-regulation of MHC-I by HIV-1 Nef. To find acidic cluster sorting machinery, we performed a gene-trap screen and identified the medium subunit (µ1) of the clathrin adaptor AP-1 as a top hit. In µ1 knockout cells, intracellular CCVs still form, but acidic cluster proteins are depleted, although several other CCV components were either unaffected or increased, indicating that cells can compensate for long-term loss of AP-1. In vitro experiments showed that the basic patch on µ1 that interacts with the Nef acidic cluster also contributes to the binding of endogenous acidic cluster proteins. Surprisingly, µ1 mutant proteins lacking the basic patch and/or the tyrosine-based motif binding pocket could rescue the µ1 knockout phenotype completely. In contrast, these mutants failed to rescue Nef-induced down-regulation of MHC class I, suggesting a possible mechanism for attacking the virus while sparing the host cell.
[Mh] Termos MeSH primário: Complexo 1 de Proteínas Adaptadoras/metabolismo
Subunidades mu do Complexo de Proteínas Adaptadoras/metabolismo
Vesículas Revestidas por Clatrina/metabolismo
HIV-1/metabolismo
Produtos do Gene nef do Vírus da Imunodeficiência Humana/metabolismo
[Mh] Termos MeSH secundário: Complexo 1 de Proteínas Adaptadoras/química
Complexo 1 de Proteínas Adaptadoras/genética
Subunidades mu do Complexo de Proteínas Adaptadoras/química
Subunidades mu do Complexo de Proteínas Adaptadoras/genética
Sistemas CRISPR-Cas
Citometria de Fluxo
Técnicas de Silenciamento de Genes
Genótipo
Células HEK293
HIV-1/genética
Células HeLa
Antígenos de Histocompatibilidade Classe I/genética
Antígenos de Histocompatibilidade Classe I/metabolismo
Interações Hospedeiro-Patógeno
Seres Humanos
Modelos Moleculares
Mutação
Fenótipo
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Transporte Proteico
Relação Estrutura-Atividade
Fatores de Tempo
Transfecção
Produtos do Gene nef do Vírus da Imunodeficiência Humana/química
Produtos do Gene nef do Vírus da Imunodeficiência Humana/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (AP1M1 protein, human); 0 (Adaptor Protein Complex 1); 0 (Adaptor Protein Complex mu Subunits); 0 (Histocompatibility Antigens Class I); 0 (nef Gene Products, Human Immunodeficiency Virus); 0 (nef protein, Human immunodeficiency virus 1)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201602058


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[PMID]:28235798
[Au] Autor:Dib K; Tikhonova IG; Ivetic A; Schu P
[Ad] Endereço:From the Max Planck Institute for Biochemistry, Department of Molecular Medicine, 82152 Martinsried, Germany, k.dib@qub.ac.uk.
[Ti] Título:The cytoplasmic tail of L-selectin interacts with the adaptor-protein complex AP-1 subunit µ1A via a novel basic binding motif.
[So] Source:J Biol Chem;292(16):6703-6714, 2017 Apr 21.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:L-selectin regulates leukocyte adhesion and rolling along the endothelium. Proteins binding to the cytoplasmic tail of L-selectin regulate L-selectin functions. We used L-selectin cytoplasmic tail peptide pulldown assays combined with high sensitivity liquid chromatography/mass spectrometry to identify novel L-selectin tail-binding proteins. Incubation of the L-selectin tail with cell extracts from phorbol 12-myristate 13-acetate-stimulated Raw 264.7 macrophages resulted in the binding of µ1A of the clathrin-coated vesicle AP-1 complex. Furthermore, full-length GST-µ1A and the GST-µ1A C-terminal domain, but not the GST-µ1A N-terminal domain, bind to L-selectin tail peptide, and the intracellular pool of L-selectin colocalizes with AP-1 at the -Golgi network. We identified a novel basic protein motif consisting of a cluster of three dibasic residues ( RR , KK , and KK ) in the membrane-proximal domain of the L-selectin tail as well as a doublet of aspartic acid residues ( DD ) in the membrane-distal end of the L-selectin tail involved in µ1A binding. Stimulation of Raw 264.7 macrophages with PMA augmented the amount of µ1A associated with anti-L-selectin immunoprecipitates. However, full-length GST-µ1A did not bind to the phospho-L-selectin tail or phospho-mimetic S364D L-selectin tail. Accordingly, we propose that phosphorylation of µ1A is required for interaction with the L-selectin tail and that L-selectin tail phosphorylation may regulate this interaction Molecular docking of the L-selectin tail to µ1A was used to identify the µ1A surface domain binding the L-selectin tail and to explain how phosphorylation of the L-selectin tail abrogates µ1A interaction. Our findings indicate that L-selectin is transported constitutively by the AP-1 complex, leading to the formation of a -Golgi network reserve pool and that phosphorylation of the L-selectin tail blocks AP-1-dependent retrograde transport of L-selectin.
[Mh] Termos MeSH primário: Complexo 1 de Proteínas Adaptadoras/química
Subunidades mu do Complexo de Proteínas Adaptadoras/química
Selectina L/química
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Animais
Ácido Aspártico/química
Cristalografia por Raios X
Citoplasma/metabolismo
Endotélio Vascular/metabolismo
Glutationa Transferase/metabolismo
Proteínas de Fluorescência Verde/metabolismo
Imunoprecipitação
Macrófagos/metabolismo
Camundongos
Simulação de Acoplamento Molecular
Monócitos/metabolismo
Fosforilação
Ligação Proteica
Domínios Proteicos
Proteômica
Células RAW 264.7
Proteína Serina-Treonina Quinases de Interação com Receptores/metabolismo
Serina/química
Rede trans-Golgi/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Protein Complex 1); 0 (Adaptor Protein Complex mu Subunits); 0 (Ap1m1 protein, mouse); 126880-86-2 (L-Selectin); 147336-22-9 (Green Fluorescent Proteins); 30KYC7MIAI (Aspartic Acid); 452VLY9402 (Serine); EC 2.5.1.18 (Glutathione Transferase); EC 2.7.11.1 (Receptor-Interacting Protein Serine-Threonine Kinases); EC 2.7.11.1 (Ripk1 protein, mouse)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170621
[Lr] Data última revisão:
170621
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170226
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.768598


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[PMID]:28224728
[Au] Autor:Chen YT; Tai CY
[Ad] Endereço:Taiwan International Graduate Program, Molecular and Cellular Biology Program, Academia Sinica, Taiwan, Republic of China.
[Ti] Título:µ2-Dependent endocytosis of N-cadherin is regulated by ß-catenin to facilitate neurite outgrowth.
[So] Source:Traffic;18(5):287-303, 2017 May.
[Is] ISSN:1600-0854
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Circuit formation in the brain requires neurite outgrowth throughout development to establish synaptic contacts with target cells. Active endocytosis of several adhesion molecules facilitates the dynamic exchange of these molecules at the surface and promotes neurite outgrowth in developing neurons. The endocytosis of N-cadherin, a calcium-dependent adhesion molecule, has been implicated in the regulation of neurite outgrowth, but the mechanism remains unclear. Here, we identified that a fraction of N-cadherin internalizes through clathrin-mediated endocytosis (CME). Two tyrosine-based motifs in the cytoplasmic domain of N-cadherin recognized by the µ2 subunit of the AP-2 adaptor complex are responsible for CME of N-cadherin. Moreover, ß-catenin, a core component of the N-cadherin adhesion complex, inhibits N-cadherin endocytosis by masking the 2 tyrosine-based motifs. Removal of ß-catenin facilitates µ2 binding to N-cadherin, thereby increasing clathrin-mediated N-cadherin endocytosis and neurite outgrowth without affecting the steady-state level of surface N-cadherin. These results identify and characterize the mechanism controlling N-cadherin endocytosis through ß-catenin-regulated µ2 binding to modulate neurite outgrowth.
[Mh] Termos MeSH primário: Subunidades mu do Complexo de Proteínas Adaptadoras/metabolismo
Caderinas/metabolismo
Endocitose/fisiologia
Crescimento Neuronal/fisiologia
beta Catenina/metabolismo
[Mh] Termos MeSH secundário: Animais
Células COS
Moléculas de Adesão Celular/metabolismo
Cercopithecus aethiops
Clatrina/metabolismo
Seres Humanos
Ligação Proteica/fisiologia
Tirosina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Protein Complex mu Subunits); 0 (Cadherins); 0 (Cell Adhesion Molecules); 0 (Clathrin); 0 (beta Catenin); 42HK56048U (Tyrosine); 709-16-0 (2-tyrosine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170919
[Lr] Data última revisão:
170919
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170223
[St] Status:MEDLINE
[do] DOI:10.1111/tra.12473


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[PMID]:28003333
[Au] Autor:Kadlecova Z; Spielman SJ; Loerke D; Mohanakrishnan A; Reed DK; Schmid SL
[Ad] Endereço:Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390.
[Ti] Título:Regulation of clathrin-mediated endocytosis by hierarchical allosteric activation of AP2.
[So] Source:J Cell Biol;216(1):167-179, 2017 Jan 02.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The critical initiation phase of clathrin-mediated endocytosis (CME) determines where and when endocytosis occurs. Heterotetrameric adaptor protein 2 (AP2) complexes, which initiate clathrin-coated pit (CCP) assembly, are activated by conformational changes in response to phosphatidylinositol-4,5-bisphosphate (PIP2) and cargo binding at multiple sites. However, the functional hierarchy of interactions and how these conformational changes relate to distinct steps in CCP formation in living cells remains unknown. We used quantitative live-cell analyses to measure discrete early stages of CME and show how sequential, allosterically regulated conformational changes activate AP2 to drive both nucleation and subsequent stabilization of nascent CCPs. Our data establish that cargoes containing Yxxφ motif, but not dileucine motif, play a critical role in the earliest stages of AP2 activation and CCP nucleation. Interestingly, these cargo and PIP2 interactions are not conserved in yeast. Thus, we speculate that AP2 has evolved as a key regulatory node to coordinate CCP formation and cargo sorting and ensure high spatial and temporal regulation of CME.
[Mh] Termos MeSH primário: Complexo 2 de Proteínas Adaptadoras/metabolismo
Vesículas Revestidas por Clatrina/metabolismo
Clatrina/metabolismo
Invaginações Revestidas da Membrana Celular/metabolismo
Endocitose
Epitélio Pigmentado da Retina/metabolismo
[Mh] Termos MeSH secundário: Complexo 2 de Proteínas Adaptadoras/química
Complexo 2 de Proteínas Adaptadoras/genética
Subunidades alfa do Complexo de Proteínas Adaptadoras/genética
Subunidades alfa do Complexo de Proteínas Adaptadoras/metabolismo
Subunidades mu do Complexo de Proteínas Adaptadoras/genética
Subunidades mu do Complexo de Proteínas Adaptadoras/metabolismo
Motivos de Aminoácidos
Linhagem Celular
Seres Humanos
Fosfatidilinositol 4,5-Difosfato/metabolismo
Ligação Proteica
Conformação Proteica
Estabilidade Proteica
Transporte Proteico
Proteínas Serina-Treonina Quinases/metabolismo
Interferência de RNA
Transdução de Sinais
Relação Estrutura-Atividade
Fatores de Tempo
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Protein Complex 2); 0 (Adaptor Protein Complex alpha Subunits); 0 (Adaptor Protein Complex mu Subunits); 0 (Clathrin); 0 (Phosphatidylinositol 4,5-Diphosphate); 0 (adaptor protein complex 2, alpha 2 subunit); 0 (adaptor protein complex 2, mu 1 subunit); EC 2.7.11.1 (AAK1 protein, human); EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161223
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201608071


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[PMID]:27603315
[Au] Autor:Marcote MJ; Sancho-Andrés G; Soriano-Ortega E; Aniento F
[Ad] Endereço:a Departamento de Bioquímica y Biología Molecular , Estructura de Recerca Interdisciplinar en Biotecnologia i Biomedicina (ERI BIOTECMED), Universitat de València , Burjassot , Spain.
[Ti] Título:Sorting signals for PIN1 trafficking and localization.
[So] Source:Plant Signal Behav;11(8):e1212801, 2016 Aug 02.
[Is] ISSN:1559-2324
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:PIN-FORMED (PIN) family proteins direct polar auxin transport based on their asymmetric (polar) localization at the plasma membrane. In the case of PIN1, it mainly localizes to the basal (rootward) plasma membrane domain of stele cells in root meristems. Vesicular trafficking events, such as clathrin-dependent PIN1 endocytosis and polar recycling, are probably the main determinants for PIN1 polar localization. However, very little is known about the signals which may be involved in binding the µ-adaptin subunit of clathrin adaptor complexes (APs) for sorting of PIN1 within clathrin-coated vesicles, which can determine its trafficking and localization. We have performed a systematic mutagenesis analysis to investigate putative sorting motifs in the hydrophilic loop of PIN1. We have found that a non-canonical motif, based in a phenylalanine residue, through the binding of µA(µ2)- and µD(µ3)-adaptin, is important for PIN1 endocytosis and for PIN1 traffcking along the secretory pathway, respectively. In addition, tyrosine-based motifs, which also bind different µ-adaptins, could also contribute to PIN1 trafficking and localization.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transporte Vesicular/metabolismo
Proteínas de Arabidopsis/metabolismo
Proteínas de Membrana Transportadoras/metabolismo
[Mh] Termos MeSH secundário: Subunidades mu do Complexo de Proteínas Adaptadoras/genética
Subunidades mu do Complexo de Proteínas Adaptadoras/metabolismo
Proteínas Adaptadoras de Transporte Vesicular/genética
Proteínas de Arabidopsis/genética
Membrana Celular/metabolismo
Endocitose/genética
Endocitose/fisiologia
Proteínas de Membrana Transportadoras/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Protein Complex mu Subunits); 0 (Adaptor Proteins, Vesicular Transport); 0 (Arabidopsis Proteins); 0 (Membrane Transport Proteins); 0 (PIN1 protein, Arabidopsis)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171020
[Lr] Data última revisão:
171020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160908
[St] Status:MEDLINE
[do] DOI:10.1080/15592324.2016.1212801


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[PMID]:26908601
[Au] Autor:Hinds DA; Buil A; Ziemek D; Martinez-Perez A; Malik R; Folkersen L; Germain M; Mälarstig A; Brown A; Soria JM; Dichgans M; Bing N; Franco-Cereceda A; Souto JC; Dermitzakis ET; Hamsten A; Worrall BB; Tung JY; Sabater-Lleal M; METASTROKE Consortium, INVENT Consortium
[Ad] Endereço:23andMe, Inc., Mountain View, CA, USA.
[Ti] Título:Genome-wide association analysis of self-reported events in 6135 individuals and 252 827 controls identifies 8 loci associated with thrombosis.
[So] Source:Hum Mol Genet;25(9):1867-74, 2016 May 01.
[Is] ISSN:1460-2083
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Thrombotic diseases are among the leading causes of morbidity and mortality in the world. To add insights into the genetic regulation of thrombotic disease, we conducted a genome-wide association study (GWAS) of 6135 self-reported blood clots events and 252 827 controls of European ancestry belonging to the 23andMe cohort of research participants. Eight loci exceeded genome-wide significance. Among the genome-wide significant results, our study replicated previously known venous thromboembolism (VTE) loci near the F5, FGA-FGG, F11, F2, PROCR and ABO genes, and the more recently discovered locus near SLC44A2 In addition, our study reports for the first time a genome-wide significant association between rs114209171, located upstream of the F8 structural gene, and thrombosis risk. Analyses of expression profiles and expression quantitative trait loci across different tissues suggested SLC44A2, ILF3 and AP1M2 as the three most plausible candidate genes for the chromosome 19 locus, our only genome-wide significant thrombosis-related locus that does not harbor likely coagulation-related genes. In addition, we present data showing that this locus also acts as a novel risk factor for stroke and coronary artery disease (CAD). In conclusion, our study reveals novel common genetic risk factors for VTE, stroke and CAD and provides evidence that self-reported data on blood clots used in a GWAS yield results that are comparable with those obtained using clinically diagnosed VTE. This observation opens up the potential for larger meta-analyses, which will enable elucidation of the genetics of thrombotic diseases, and serves as an example for the genetic study of other diseases.
[Mh] Termos MeSH primário: Loci Gênicos/genética
Predisposição Genética para Doença
Estudo de Associação Genômica Ampla
Polimorfismo de Nucleotídeo Único/genética
Trombose/genética
[Mh] Termos MeSH secundário: Complexo 1 de Proteínas Adaptadoras/genética
Subunidades mu do Complexo de Proteínas Adaptadoras/genética
Adolescente
Adulto
Biomarcadores/metabolismo
Estudos de Casos e Controles
Criança
Pré-Escolar
Feminino
Seres Humanos
Lactente
Recém-Nascido
Masculino
Glicoproteínas de Membrana/genética
Proteínas de Membrana Transportadoras/genética
Meia-Idade
Proteínas do Fator Nuclear 90/genética
Fatores de Risco
Autorrelato
Adulto Jovem
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (AP1M2 protein, human); 0 (Adaptor Protein Complex 1); 0 (Adaptor Protein Complex mu Subunits); 0 (Biomarkers); 0 (ILF3 protein, human); 0 (Membrane Glycoproteins); 0 (Membrane Transport Proteins); 0 (Nuclear Factor 90 Proteins); 0 (SLC44A2 protein, human)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160225
[St] Status:MEDLINE
[do] DOI:10.1093/hmg/ddw037


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[PMID]:26658609
[Au] Autor:Whitfield ST; Burston HE; Bean BD; Raghuram N; Maldonado-Báez L; Davey M; Wendland B; Conibear E
[Ad] Endereço:Centre for Molecular Medicine and Therapeutics, Child and Family Research Institute, Vancouver, University of British Columbia, Vancouver, BC V5Z 4H4, Canada Department of Biochemistry and Molecular Biology and Department of Medical Genetics, Faculty of Medicine, University of British Columbia, Vanc
[Ti] Título:The alternate AP-1 adaptor subunit Apm2 interacts with the Mil1 regulatory protein and confers differential cargo sorting.
[So] Source:Mol Biol Cell;27(3):588-98, 2016 Feb 01.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Heterotetrameric adaptor protein complexes are important mediators of cargo protein sorting in clathrin-coated vesicles. The cell type-specific expression of alternate µ chains creates distinct forms of AP-1 with altered cargo sorting, but how these subunits confer differential function is unclear. Whereas some studies suggest the µ subunits specify localization to different cellular compartments, others find that the two forms of AP-1 are present in the same vesicle but recognize different cargo. Yeast have two forms of AP-1, which differ only in the µ chain. Here we show that the variant µ chain Apm2 confers distinct cargo-sorting functions. Loss of Apm2, but not of Apm1, increases cell surface levels of the v-SNARE Snc1. However, Apm2 is unable to replace Apm1 in sorting Chs3, which requires a dileucine motif recognized by the γ/σ subunits common to both complexes. Apm2 and Apm1 colocalize at Golgi/early endosomes, suggesting that they do not associate with distinct compartments. We identified a novel, conserved regulatory protein that is required for Apm2-dependent sorting events. Mil1 is a predicted lipase that binds Apm2 but not Apm1 and contributes to its membrane recruitment. Interactions with specific regulatory factors may provide a general mechanism to diversify the functional repertoire of clathrin adaptor complexes.
[Mh] Termos MeSH primário: Subunidades mu do Complexo de Proteínas Adaptadoras/metabolismo
Lipase/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Complexo 1 de Proteínas Adaptadoras/metabolismo
Subunidades mu do Complexo de Proteínas Adaptadoras/química
Sequência de Aminoácidos
Domínio Catalítico
Endossomos/metabolismo
Complexo de Golgi/metabolismo
Lipase/química
Dados de Sequência Molecular
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Transporte Proteico
Proteínas de Saccharomyces cerevisiae/química
Tirosina/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (APM2 protein, S cerevisiae); 0 (Adaptor Protein Complex 1); 0 (Adaptor Protein Complex mu Subunits); 0 (Saccharomyces cerevisiae Proteins); 42HK56048U (Tyrosine); EC 3.1.1.3 (Lipase); EC 3.1.1.3 (Mil1 protein, S cerevisiae)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151215
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E15-09-0621


  8 / 142 MEDLINE  
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[PMID]:25449265
[Au] Autor:Hirata Y; Funato Y; Miki H
[Ad] Endereço:Department of Cellular Regulation, Research Institute for Microbial Diseases, Osaka University, 3-1 Yamadaoka, Suita, Osaka 565-0871, Japan; Laboratory of Health Chemistry, Graduate School of Pharmaceutical Sciences, Tohoku University, 6-3 Aoba, Aramaki, Aoba-ku, Sendai, Miyagi 980-8578, Japan.
[Ti] Título:Basolateral sorting of the Mg²âº transporter CNNM4 requires interaction with AP-1A and AP-1B.
[So] Source:Biochem Biophys Res Commun;455(3-4):184-9, 2014 Dec 12.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ancient conserved domain protein/cyclin M (CNNM) 4 is an evolutionarily conserved Mg(2+) transporter that localizes at the basolateral membrane of the intestinal epithelia. Here, we show the complementary importance of clathrin adaptor protein (AP) complexes AP-1A and AP-1B in basolateral sorting of CNNM4. We first confirmed the basolateral localization of both endogenous and ectopically expressed CNNM4 in Madin-Darby Canine Kidney cells, which form highly polarized epithelia in culture. Single knockdown of µ1B, a cargo-recognition subunit of AP-1B, did not affect basolateral localization, but simultaneous knockdown of the µ1A subunit of AP-1A abrogated localization. Mutational analyses showed the importance of three conserved dileucine motifs in CNNM4 for both basolateral sorting and interaction with µ1A and µ1B. These results imply that CNNM4 is sorted to the basolateral membrane by the complementary function of AP-1A and AP-1B.
[Mh] Termos MeSH primário: Complexo 1 de Proteínas Adaptadoras/fisiologia
Subunidades beta do Complexo de Proteínas Adaptadoras/fisiologia
Subunidades mu do Complexo de Proteínas Adaptadoras/fisiologia
Proteínas de Transporte de Cátions/metabolismo
Regulação da Expressão Gênica
Magnésio/química
[Mh] Termos MeSH secundário: Complexo 1 de Proteínas Adaptadoras/química
Subunidades beta do Complexo de Proteínas Adaptadoras/química
Subunidades mu do Complexo de Proteínas Adaptadoras/química
Motivos de Aminoácidos
Sequência de Aminoácidos
Animais
Biotinilação
Células COS
Linhagem Celular
Membrana Celular/metabolismo
Cercopithecus aethiops
DNA Complementar/metabolismo
Cães
Seres Humanos
Proteínas de Membrana Transportadoras/metabolismo
Microscopia de Fluorescência
Dados de Sequência Molecular
Mutação
Transporte Proteico
Interferência de RNA
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (AP1B1 protein, human); 0 (Adaptor Protein Complex 1); 0 (Adaptor Protein Complex beta Subunits); 0 (Adaptor Protein Complex mu Subunits); 0 (CNNM4 protein, human); 0 (Cation Transport Proteins); 0 (DNA, Complementary); 0 (Membrane Transport Proteins); I38ZP9992A (Magnesium)
[Em] Mês de entrada:1502
[Cu] Atualização por classe:141206
[Lr] Data última revisão:
141206
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141203
[St] Status:MEDLINE


  9 / 142 MEDLINE  
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[PMID]:25074807
[Au] Autor:Hagemann AI; Kurz J; Kauffeld S; Chen Q; Reeves PM; Weber S; Schindler S; Davidson G; Kirchhausen T; Scholpp S
[Ad] Endereço:Karlsruhe Institute of Technology (KIT), Institute of Toxicology and Genetics (ITG), 76021 Karsruhe, Germany.
[Ti] Título:In vivo analysis of formation and endocytosis of the Wnt/ß-catenin signaling complex in zebrafish embryos.
[So] Source:J Cell Sci;127(Pt 18):3970-82, 2014 Sep 15.
[Is] ISSN:1477-9137
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:After activation by Wnt/ß-Catenin ligands, a multi-protein complex assembles at the plasma membrane as membrane-bound receptors and intracellular signal transducers are clustered into the so-called Lrp6-signalosome [Corrected]. However, the mechanism of signalosome formation and dissolution is yet not clear. Our imaging studies of live zebrafish embryos show that the signalosome is a highly dynamic structure. It is continuously assembled by Dvl2-mediated recruitment of the transducer complex to the activated receptors and partially disassembled by endocytosis. We find that, after internalization, the ligand-receptor complex and the transducer complex take separate routes. The Wnt-Fz-Lrp6 complex follows a Rab-positive endocytic path. However, when still bound to the transducer complex, Dvl2 forms intracellular aggregates. We show that this endocytic process is not only essential for ligand-receptor internalization but also for signaling. The µ2-subunit of the endocytic Clathrin adaptor Ap2 interacts with Dvl2 to maintain its stability during endocytosis. Blockage of Ap2µ2 function leads to Dvl2 degradation, inhibiton of signalosome formation at the plasma membrane and, consequently, reduction of signaling. We conclude that Ap2µ2-mediated endocytosis is important to maintain Wnt/ß-catenin signaling in vertebrates.
[Mh] Termos MeSH primário: Endocitose
Complexos Multiproteicos/metabolismo
Via de Sinalização Wnt
Xenopus/metabolismo
beta Catenina/metabolismo
[Mh] Termos MeSH secundário: Complexo 2 de Proteínas Adaptadoras/genética
Complexo 2 de Proteínas Adaptadoras/metabolismo
Subunidades mu do Complexo de Proteínas Adaptadoras/genética
Subunidades mu do Complexo de Proteínas Adaptadoras/metabolismo
Proteínas Adaptadoras de Transdução de Sinal/genética
Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Animais
Proteínas Desgrenhadas
Feminino
Proteína-6 Relacionada a Receptor de Lipoproteína de Baixa Densidade/genética
Proteína-6 Relacionada a Receptor de Lipoproteína de Baixa Densidade/metabolismo
Complexos Multiproteicos/genética
Fosfoproteínas/genética
Fosfoproteínas/metabolismo
Ligação Proteica
Xenopus/embriologia
Xenopus/genética
[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 2); 0 (Adaptor Protein Complex mu Subunits); 0 (Adaptor Proteins, Signal Transducing); 0 (Dishevelled Proteins); 0 (LRP6 protein, Xenopus); 0 (Low Density Lipoprotein Receptor-Related Protein-6); 0 (Multiprotein Complexes); 0 (Phosphoproteins); 0 (adaptor protein complex 2, mu 2 subunit); 0 (beta Catenin)
[Em] Mês de entrada:1506
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140731
[St] Status:MEDLINE
[do] DOI:10.1242/jcs.148767


  10 / 142 MEDLINE  
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[PMID]:24923803
[Au] Autor:Bubier JA; Jay JJ; Baker CL; Bergeson SE; Ohno H; Metten P; Crabbe JC; Chesler EJ
[Ad] Endereço:The Jackson Laboratory, Bar Harbor, Maine 04609.
[Ti] Título:Identification of a QTL in Mus musculus for alcohol preference, withdrawal, and Ap3m2 expression using integrative functional genomics and precision genetics.
[So] Source:Genetics;197(4):1377-93, 2014 Aug.
[Is] ISSN:1943-2631
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Extensive genetic and genomic studies of the relationship between alcohol drinking preference and withdrawal severity have been performed using animal models. Data from multiple such publications and public data resources have been incorporated in the GeneWeaver database with >60,000 gene sets including 285 alcohol withdrawal and preference-related gene sets. Among these are evidence for positional candidates regulating these behaviors in overlapping quantitative trait loci (QTL) mapped in distinct mouse populations. Combinatorial integration of functional genomics experimental results revealed a single QTL positional candidate gene in one of the loci common to both preference and withdrawal. Functional validation studies in Ap3m2 knockout mice confirmed these relationships. Genetic validation involves confirming the existence of segregating polymorphisms that could account for the phenotypic effect. By exploiting recent advances in mouse genotyping, sequence, epigenetics, and phylogeny resources, we confirmed that Ap3m2 resides in an appropriately segregating genomic region. We have demonstrated genetic and alcohol-induced regulation of Ap3m2 expression. Although sequence analysis revealed no polymorphisms in the Ap3m2-coding region that could account for all phenotypic differences, there are several upstream SNPs that could. We have identified one of these to be an H3K4me3 site that exhibits strain differences in methylation. Thus, by making cross-species functional genomics readily computable we identified a common QTL candidate for two related bio-behavioral processes via functional evidence and demonstrate sufficiency of the genetic locus as a source of variation underlying two traits.
[Mh] Termos MeSH primário: Complexo 3 de Proteínas Adaptadoras/genética
Subunidades mu do Complexo de Proteínas Adaptadoras/genética
Consumo de Bebidas Alcoólicas/genética
Locos de Características Quantitativas
[Mh] Termos MeSH secundário: Complexo 3 de Proteínas Adaptadoras/metabolismo
Subunidades mu do Complexo de Proteínas Adaptadoras/metabolismo
Animais
Imunoprecipitação da Cromatina
Mapeamento Cromossômico
Biologia Computacional
Bases de Dados Genéticas
Modelos Animais de Doenças
Feminino
Genoma
Genômica
Técnicas de Genotipagem
Sequenciamento de Nucleotídeos em Larga Escala
Masculino
Camundongos
Camundongos Knockout
Fenótipo
Filogenia
Polimorfismo de Nucleotídeo Único
Reprodutibilidade dos Testes
Análise de Sequência de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Adaptor Protein Complex 3); 0 (Adaptor Protein Complex mu Subunits); 0 (Ap3m2 protein, mouse)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140614
[St] Status:MEDLINE
[do] DOI:10.1534/genetics.114.166165



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