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Pesquisa : A11.284.430.214.190.875.336.850 [Categoria DeCS]
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[PMID]:28468990
[Au] Autor:Yu CJ; Lee FJ
[Ad] Endereço:Department of Cell and Molecular Biology, College of Medicine, Chang Gung University, Linkou, Tao-Yuan 33302, Taiwan.
[Ti] Título:Multiple activities of Arl1 GTPase in the trans-Golgi network.
[So] Source:J Cell Sci;130(10):1691-1699, 2017 05 15.
[Is] ISSN:1477-9137
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:ADP-ribosylation factors (Arfs) and ADP-ribosylation factor-like proteins (Arls) are highly conserved small GTPases that function as main regulators of vesicular trafficking and cytoskeletal reorganization. Arl1, the first identified member of the large Arl family, is an important regulator of Golgi complex structure and function in organisms ranging from yeast to mammals. Together with its effectors, Arl1 has been shown to be involved in several cellular processes, including endosomal trans-Golgi network and secretory trafficking, lipid droplet and salivary granule formation, innate immunity and neuronal development, stress tolerance, as well as the response of the unfolded protein. In this Commentary, we provide a comprehensive summary of the Arl1-dependent cellular functions and a detailed characterization of several Arl1 effectors. We propose that involvement of Arl1 in these diverse cellular functions reflects the fact that Arl1 is activated at several late-Golgi sites, corresponding to specific molecular complexes that respond to and integrate multiple signals. We also provide insight into how the GTP-GDP cycle of Arl1 is regulated, and highlight a newly discovered mechanism that controls the sophisticated regulation of Arl1 activity at the Golgi complex.
[Mh] Termos MeSH primário: Fatores de Ribosilação do ADP/metabolismo
GTP Fosfo-Hidrolases/metabolismo
Proteínas de Membrana/metabolismo
Rede trans-Golgi/metabolismo
[Mh] Termos MeSH secundário: Animais
Membrana Celular/metabolismo
Seres Humanos
Transporte Proteico
Vesículas Transportadoras/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Membrane Proteins); EC 3.6.1.- (ADP-ribosylation factor related proteins); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.5.2 (ADP-Ribosylation Factors)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180223
[Lr] Data última revisão:
180223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1242/jcs.201319


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[PMID]:29223392
[Au] Autor:Fujimoto T; Kuwahara T; Eguchi T; Sakurai M; Komori T; Iwatsubo T
[Ad] Endereço:Department of Neuropathology, Graduate School of Medicine, The University of Tokyo, Tokyo, 113-0033, Japan.
[Ti] Título:Parkinson's disease-associated mutant LRRK2 phosphorylates Rab7L1 and modifies trans-Golgi morphology.
[So] Source:Biochem Biophys Res Commun;495(2):1708-1715, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mutations in leucine-rich repeat kinase 2 (LRRK2) are the major genetic cause of autosomal-dominantly inherited Parkinson's disease. LRRK2 is implicated in the regulation of intracellular trafficking, neurite outgrowth and PD risk in connection with Rab7L1, a putative interactor of LRRK2. Recently, a subset of Rab GTPases have been reported as substrates of LRRK2. Here we examine the kinase activity of LRRK2 on Rab7L1 in situ in cells. Phos-tag analyses and metabolic labeling assays revealed that LRRK2 readily phosphorylates Golgi-localized wild-type Rab7L1 but not mutant forms that are distributed in the cytoplasm. In vitro assays demonstrated direct phosphorylation of Rab7L1 by LRRK2. Subsequent screening using Rab7L1 mutants harboring alanine-substitution for every single Ser/Thr residue revealed that Ser72 is a major phosphorylation site, which was confirmed by using a phospho-Ser72-specific antibody. Moreover, LRRK2 pathogenic Parkinson mutants altogether markedly enhanced the phosphorylation at Ser72. The modulation of Ser72 phosphorylation in Rab7L1 resulted in an alteration of the morphology and distribution of the trans-Golgi network. These data collectively support the involvement of Rab7L1 phosphorylation in the LRRK2-mediated cellular and pathogenetic mechanisms.
[Mh] Termos MeSH primário: Serina-Treonina Proteína Quinase-2 com Repetições Ricas em Leucina/genética
Serina-Treonina Proteína Quinase-2 com Repetições Ricas em Leucina/metabolismo
Mutação
Doença de Parkinson/genética
Doença de Parkinson/metabolismo
Proteínas rab1 de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Substituição de Aminoácidos
Sítios de Ligação/genética
Células HEK293
Células HeLa
Seres Humanos
Modelos Moleculares
Proteínas Mutantes/genética
Proteínas Mutantes/metabolismo
Doença de Parkinson/patologia
Fosforilação
Conformação Proteica
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/metabolismo
Serina/química
Serina/genética
Especificidade por Substrato
Proteínas rab1 de Ligação ao GTP/química
Proteínas rab1 de Ligação ao GTP/genética
Rede trans-Golgi/metabolismo
Rede trans-Golgi/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Mutant Proteins); 0 (Rab29 protein, human); 0 (Recombinant Fusion Proteins); 452VLY9402 (Serine); EC 2.7.11.1 (LRRK2 protein, human); EC 2.7.11.1 (Leucine-Rich Repeat Serine-Threonine Protein Kinase-2); EC 3.6.5.2 (rab1 GTP-Binding Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171211
[St] Status:MEDLINE


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[PMID]:28463988
[Au] Autor:Calton CM; Bronnimann MP; Manson AR; Li S; Chapman JA; Suarez-Berumen M; Williamson TR; Molugu SK; Bernal RA; Campos SK
[Ad] Endereço:BIO5 Institute, University of Arizona, Tucson, Arizona, United States of America.
[Ti] Título:Translocation of the papillomavirus L2/vDNA complex across the limiting membrane requires the onset of mitosis.
[So] Source:PLoS Pathog;13(5):e1006200, 2017 May.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The human papillomavirus type 16 (HPV16) L2 protein acts as a chaperone to ensure that the viral genome (vDNA) traffics from endosomes to the trans-Golgi network (TGN) and eventually the nucleus, where HPV replication occurs. En route to the nucleus, the L2/vDNA complex must translocate across limiting intracellular membranes. The details of this critical process remain poorly characterized. We have developed a system based on subcellular compartmentalization of the enzyme BirA and its cognate substrate to detect membrane translocation of L2-BirA from incoming virions. We find that L2 translocation requires transport to the TGN and is strictly dependent on entry into mitosis, coinciding with mitotic entry in synchronized cells. Cell cycle arrest causes retention of L2/vDNA at the TGN; only release and progression past G2/M enables translocation across the limiting membrane and subsequent infection. Microscopy of EdU-labeled vDNA reveals a rapid and dramatic shift in vDNA localization during early mitosis. At late G2/early prophase vDNA egresses from the TGN to a pericentriolar location, accumulating there through prometaphase where it begins to associate with condensed chromosomes. By metaphase and throughout anaphase the vDNA is seen bound to the mitotic chromosomes, ensuring distribution into both daughter nuclei. Mutations in a newly defined chromatin binding region of L2 potently blocked translocation, suggesting that translocation is dependent on chromatin binding during prometaphase. This represents the first time a virus has been shown to functionally couple the penetration of limiting membranes to cellular mitosis, explaining in part the tropism of HPV for mitotic basal keratinocytes.
[Mh] Termos MeSH primário: Proteínas do Capsídeo/metabolismo
Genoma Viral/genética
Papillomavirus Humano 16/fisiologia
Mitose
Proteínas Oncogênicas Virais/metabolismo
Infecções por Papillomavirus/virologia
[Mh] Termos MeSH secundário: Transporte Biológico
Proteínas do Capsídeo/genética
Pontos de Checagem do Ciclo Celular
Linhagem Celular
Núcleo Celular/metabolismo
Núcleo Celular/virologia
DNA Viral/genética
DNA Viral/metabolismo
Endossomos/metabolismo
Endossomos/virologia
Papillomavirus Humano 16/genética
Seres Humanos
Queratinócitos/virologia
Mutação
Proteínas Oncogênicas Virais/genética
Tropismo Viral
Vírion
Internalização do Vírus
Rede trans-Golgi/metabolismo
Rede trans-Golgi/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Capsid Proteins); 0 (DNA, Viral); 0 (L2 protein, Human papillomavirus type 16); 0 (Oncogene Proteins, Viral)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006200


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[PMID]:29184172
[Au] Autor:Fromme JC; Munson M
[Ad] Endereço:Department of Molecular Biology and Genetics, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, New York 14853, USA.
[Ti] Título:Capturing endosomal vesicles at the Golgi.
[So] Source:Nat Cell Biol;19(12):1384-1386, 2017 Nov 29.
[Is] ISSN:1476-4679
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Membrane trafficking specificity between distinct compartments ensures that cargo proteins and lipids are delivered to their target organelle. However, accurate recognition of cargo carriers by tethering factors on target membranes is poorly understood. TBC1D23 is now identified as an adaptor that links endosome-derived vesicles with golgins at the trans-Golgi.
[Mh] Termos MeSH primário: Endossomos/metabolismo
Complexo de Golgi/metabolismo
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Proteínas Ativadoras de GTPase/metabolismo
Proteínas de Membrana/metabolismo
Modelos Biológicos
Rede trans-Golgi/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (GTPase-Activating Proteins); 0 (Membrane Proteins)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171219
[Lr] Data última revisão:
171219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171130
[St] Status:MEDLINE
[do] DOI:10.1038/ncb3649


  5 / 1292 MEDLINE  
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[PMID]:28450044
[Au] Autor:Simm R; Kvalvaag AS; van Deurs B; Lindbäck T; Sandvig K
[Ad] Endereço:Centre for Cancer Biomedicine, Faculty of Medicine, University of Oslo, Oslo, Norway; Department of Molecular Cell Biology, Institute for Cancer Research, The Norwegian Radium Hospital, Oslo University Hospital, Oslo, Norway.
[Ti] Título:Benzyl alcohol induces a reversible fragmentation of the Golgi apparatus and inhibits membrane trafficking between endosomes and the trans-Golgi network.
[So] Source:Exp Cell Res;357(1):67-78, 2017 08 01.
[Is] ISSN:1090-2422
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Benzyl alcohol (BnOH) is widely used as a component of foods, cosmetics, household products and medical products. It is generally considered to be safe for human use, however, it has been connected to a number of adverse effects, including hypersensitivity reactions and neonatal deaths. BnOH is a membrane fluidizing agent that can affect membrane protein activity and cellular processes such as ligand binding to cell surface receptors, endocytosis and degradation of lysosomal cargo. In this study, we examined the effects of BnOH on intracellular transport using Shiga toxin (Stx), diphtheria toxin (DT) and ricin. BnOH caused reduced toxicity of all three toxins at BnOH concentrations that cause membrane fluidization. The reduced toxicity of Stx and ricin was mainly due to inhibition of retrograde transport between endosomes and the trans-Golgi network as BnOH had small effects on cell association and endocytosis of ricin and Stx. Strikingly, BnOH also induced a reversible fragmentation of the Golgi apparatus.
[Mh] Termos MeSH primário: Álcool Benzílico/farmacologia
Transporte Biológico/efeitos dos fármacos
Endossomos/efeitos dos fármacos
Complexo de Golgi/efeitos dos fármacos
Rede trans-Golgi/efeitos dos fármacos
[Mh] Termos MeSH secundário: Movimento Celular/efeitos dos fármacos
Endocitose/efeitos dos fármacos
Endossomos/metabolismo
Complexo de Golgi/metabolismo
Células HeLa
Seres Humanos
Transporte Proteico/efeitos dos fármacos
Toxina Shiga/metabolismo
Rede trans-Golgi/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
75757-64-1 (Shiga Toxin); LKG8494WBH (Benzyl Alcohol)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171209
[Lr] Data última revisão:
171209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE


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[PMID]:28978670
[Au] Autor:Mesmin B; Bigay J; Polidori J; Jamecna D; Lacas-Gervais S; Antonny B
[Ad] Endereço:Université Côte d'Azur, Inserm, CNRS, Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France.
[Ti] Título:Sterol transfer, PI4P consumption, and control of membrane lipid order by endogenous OSBP.
[So] Source:EMBO J;36(21):3156-3174, 2017 Nov 02.
[Is] ISSN:1460-2075
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The network of proteins that orchestrate the distribution of cholesterol among cellular organelles is not fully characterized. We previously proposed that oxysterol-binding protein (OSBP) drives cholesterol/PI4P exchange at contact sites between the endoplasmic reticulum (ER) and the -Golgi network (TGN). Using the inhibitor OSW-1, we report here that the sole activity of endogenous OSBP makes a major contribution to cholesterol distribution, lipid order, and PI4P turnover in living cells. Blocking OSBP causes accumulation of sterols at ER/lipid droplets at the expense of TGN, thereby reducing the gradient of lipid order along the secretory pathway. OSBP consumes about half of the total cellular pool of PI4P, a consumption that depends on the amount of cholesterol to be transported. Inhibiting the spatially restricted PI4-kinase PI4KIIIß triggers large periodic traveling waves of PI4P across the TGN These waves are cadenced by long-range PI4P production by PI4KIIα and PI4P consumption by OSBP Collectively, these data indicate a massive spatiotemporal coupling between cholesterol transport and PI4P turnover via OSBP and PI4-kinases to control the lipid composition of subcellular membranes.
[Mh] Termos MeSH primário: Colesterol/metabolismo
Células Epiteliais/metabolismo
Antígenos de Histocompatibilidade Menor/metabolismo
Fosfatos de Fosfatidilinositol/metabolismo
Fosfotransferases (Aceptor do Grupo Álcool)/metabolismo
Receptores de Esteroides/metabolismo
[Mh] Termos MeSH secundário: Transporte Biológico
Colestenonas/farmacologia
Dicarbetoxi-Di-Hidrocolidina/análogos & derivados
Dicarbetoxi-Di-Hidrocolidina/química
Retículo Endoplasmático/metabolismo
Células Epiteliais/citologia
Corantes Fluorescentes/química
Expressão Gênica
Células HeLa
Seres Humanos
Gotículas Lipídicas/metabolismo
Antígenos de Histocompatibilidade Menor/genética
Fosfotransferases (Aceptor do Grupo Álcool)/genética
Receptores de Esteroides/antagonistas & inibidores
Receptores de Esteroides/genética
Epitélio Pigmentado da Retina/citologia
Epitélio Pigmentado da Retina/metabolismo
Saponinas/farmacologia
Imagem com Lapso de Tempo
Rede trans-Golgi/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cholestenones); 0 (Fluorescent Dyes); 0 (Minor Histocompatibility Antigens); 0 (Phosphatidylinositol Phosphates); 0 (Receptors, Steroid); 0 (Saponins); 0 (dihydroethidine); 0 (oxysterol binding protein); 0 (phosphatidylinositol 4-phosphate); 145075-81-6 (OSW 1); 632-93-9 (Dicarbethoxydihydrocollidine); 97C5T2UQ7J (Cholesterol); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor)); EC 2.7.1.67 (phosphatidylinositol 4-kinase IIIbeta, human); EC 2.7.1.67 (phosphatidylinositol phosphate 4-kinase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171006
[St] Status:MEDLINE
[do] DOI:10.15252/embj.201796687


  7 / 1292 MEDLINE  
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Soares, Maurílio José
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[PMID]:28759609
[Au] Autor:Moreira CMDN; Batista CM; Fernandes JC; Kessler RL; Soares MJ; Fragoso SP
[Ad] Endereço:Laboratory of Molecular Biology of Trypanosomatids, Instituto Carlos Chagas/Fiocruz, Curitiba - PR, Brazil.
[Ti] Título:Knockout of the gamma subunit of the AP-1 adaptor complex in the human parasite Trypanosoma cruzi impairs infectivity and differentiation and prevents the maturation and targeting of the major protease cruzipain.
[So] Source:PLoS One;12(7):e0179615, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The AP-1 Adaptor Complex assists clathrin-coated vesicle assembly in the trans-Golgi network (TGN) of eukaryotic cells. However, the role of AP-1 in the protozoan Trypanosoma cruzi-the Chagas disease parasite-has not been addressed. Here, we studied the function and localization of AP-1 in different T. cruzi life cycle forms, by generating a gene knockout of the large AP-1 subunit gamma adaptin (TcAP1-γ), and raising a monoclonal antibody against TcAP1-γ. Co-localization with a Golgi marker and with the clathrin light chain showed that TcAP1-γ is located in the Golgi, and it may interact with clathrin in vivo, at the TGN. Epimastigote (insect form) parasites lacking TcAP1-γ (TcγKO) have reduced proliferation and differentiation into infective metacyclic trypomastigotes (compared with wild-type parasites). TcγKO parasites have also displayed significantly reduced infectivity towards mammalian cells. Importantly, TcAP1-γ knockout impaired maturation and transport to lysosome-related organelles (reservosomes) of a key cargo-the major cysteine protease cruzipain, which is important for parasite nutrition, differentiation and infection. In conclusion, the defective processing and transport of cruzipain upon AP-1 ablation may underlie the phenotype of TcγKO parasites.
[Mh] Termos MeSH primário: Doença de Chagas/parasitologia
Cisteína Endopeptidases/química
Fator de Transcrição AP-1/genética
Fator de Transcrição AP-1/fisiologia
Trypanosoma cruzi/genética
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Anticorpos Monoclonais/química
Vesículas Revestidas por Clatrina
Endocitose
Teste de Complementação Genética
Complexo de Golgi/metabolismo
Masculino
Camundongos
Camundongos Endogâmicos BALB C
Organelas
Plasmídeos/metabolismo
Proteínas Recombinantes/química
Rede trans-Golgi/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Recombinant Proteins); 0 (Transcription Factor AP-1); EC 3.4.22.- (Cysteine Endopeptidases); EC 3.4.22.- (cruzipain)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170801
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0179615


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[PMID]:28636623
[Au] Autor:Pedersen GA; Jensen HH; Schelde AB; Toft C; Pedersen HN; Ulrichsen M; Login FH; Amieva MR; Nejsum LN
[Ad] Endereço:Department of Clinical Medicine, Aarhus University, Aarhus, Denmark.
[Ti] Título:The basolateral vesicle sorting machinery and basolateral proteins are recruited to the site of enteropathogenic E. coli microcolony growth at the apical membrane.
[So] Source:PLoS One;12(6):e0179122, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Foodborne Enteropathogenic Escherichia coli (EPEC) infections of the small intestine cause diarrhea especially in children and are a major cause of childhood death in developing countries. EPEC infects the apical membrane of the epithelium of the small intestine by attaching, effacing the microvilli under the bacteria and then forming microcolonies on the cell surface. We first asked the question where on epithelial cells EPEC attaches and grows. Using models of polarized epithelial monolayers, we evaluated the sites of initial EPEC attachment to the apical membrane and found that EPEC preferentially attached over the cell-cell junctions and formed microcolonies preferentially where three cells come together at tricellular tight junctions. The ability of EPEC to adhere increased when host cell polarity was compromised yielding EPEC access to basolateral proteins. EPEC pedestals contain basolateral cytoskeletal proteins. Thus, we asked if attached EPEC causes reorganization the protein composition of the host cell plasma membrane at sites of microcolony formation. We found that EPEC microcolony growth at the apical membrane resulted in a local accumulation of basolateral plasma membrane proteins surrounding the microcolony. Basolateral marker protein aquaporin-3 localized to forming EPEC microcolonies. Components of the basolateral vesicle targeting machinery were re-routed. The Exocyst (Exo70) was recruited to individual EPEC as was the basolateral vesicle SNARE VAMP-3. Moreover, several Rab variants were also recruited to the infection site, and their dominant-negative equivalents were not. To quantitatively study the recruitment of basolateral proteins, we created a pulse of the temperature sensitive basolateral VSVG, VSVG3-SP-GFP, from the trans-Golgi Network. We found that after release from the TGN, significantly more VSVG3-SP-GFP accumulated at the site of microcolony growth than on equivalent membrane regions of uninfected cells. This suggests that trafficking of vesicles destined for the basolateral membrane are redirected to the apical site of microcolony growth. Thus, in addition to disrupting host cell fence function, local host cell plasma membrane protein composition is changed by altered protein trafficking and recruitment of basolateral proteins to the apical microcolony. This may aid EPEC attachment and subsequent microcolony growth.
[Mh] Termos MeSH primário: Membrana Celular/metabolismo
Escherichia coli Enteropatogênica/metabolismo
Infecções por Escherichia coli/metabolismo
Proteínas de Escherichia coli/metabolismo
Rede trans-Golgi/metabolismo
[Mh] Termos MeSH secundário: Animais
Aderência Bacteriana
Membrana Celular/microbiologia
Polaridade Celular
Cães
Escherichia coli Enteropatogênica/crescimento & desenvolvimento
Infecções por Escherichia coli/microbiologia
Infecções por Escherichia coli/patologia
Células Madin Darby de Rim Canino
Transporte Proteico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170622
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0179122


  9 / 1292 MEDLINE  
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[PMID]:28626002
[Au] Autor:Sørensen JB
[Ad] Endereço:Center for Neuroscience, University of Copenhagen, Copenhagen, Denmark jakobbs@sund.ku.dk.
[Ti] Título:Ride the wave: Retrograde trafficking becomes Ca dependent with BAIAP3.
[So] Source:J Cell Biol;216(7):1887-1889, 2017 Jul 03.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The functions of four of the five proteins in the mammalian uncoordinated-13 (Munc13) family have been identified as priming factors in SNARE-dependent exocytosis. In this issue, Zhang et al. (2017. https://doi.org/10.1083/jcb.201702099) show that the fifth member, BAIAP3 (brain-specific angiogenesis inhibitor I-associated protein 3), acts in retrograde trafficking by returning secretory vesicle material to the trans-Golgi network. In its absence, secretory vesicle formation is impaired, leading to accumulation of immature vesicles, or lysosomal vesicle degradation.
[Mh] Termos MeSH primário: Exocitose
Vesículas Secretórias
[Mh] Termos MeSH secundário: Animais
Transporte Proteico
Proteínas SNARE
Rede trans-Golgi
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (SNARE Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170620
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201706007


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[PMID]:28626000
[Au] Autor:Zhang X; Jiang S; Mitok KA; Li L; Attie AD; Martin TFJ
[Ad] Endereço:Department of Biochemistry, University of Wisconsin, Madison, WI.
[Ti] Título:BAIAP3, a C2 domain-containing Munc13 protein, controls the fate of dense-core vesicles in neuroendocrine cells.
[So] Source:J Cell Biol;216(7):2151-2166, 2017 Jul 03.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Dense-core vesicle (DCV) exocytosis is a SNARE (soluble -ethylmaleimide-sensitive fusion attachment protein receptor)-dependent anterograde trafficking pathway that requires multiple proteins for regulation. Several C2 domain-containing proteins are known to regulate Ca -dependent DCV exocytosis in neuroendocrine cells. In this study, we identified others by screening all (∼139) human C2 domain-containing proteins by RNA interference in neuroendocrine cells. 40 genes were identified, including several encoding proteins with known roles (CAPS [calcium-dependent activator protein for secretion 1], Munc13-2, RIM1, and SYT10) and many with unknown roles. One of the latter, BAIAP3, is a secretory cell-specific Munc13-4 paralog of unknown function. BAIAP3 knockdown caused accumulation of fusion-incompetent DCVs in BON neuroendocrine cells and lysosomal degradation (crinophagy) of insulin-containing DCVs in INS-1 ß cells. BAIAP3 localized to endosomes was required for Golgi trans-Golgi network 46 (TGN46) recycling, exhibited Ca -stimulated interactions with TGN SNAREs, and underwent Ca -stimulated TGN recruitment. Thus, unlike other Munc13 proteins, BAIAP3 functions indirectly in DCV exocytosis by affecting DCV maturation through its role in DCV protein recycling. Ca rises that stimulate DCV exocytosis may stimulate BAIAP3-dependent retrograde trafficking to maintain DCV protein homeostasis and DCV function.
[Mh] Termos MeSH primário: Proteínas de Transporte/metabolismo
Exocitose
Proteínas do Tecido Nervoso/metabolismo
Células Neuroendócrinas/metabolismo
Vesículas Secretórias/metabolismo
[Mh] Termos MeSH secundário: Animais
Sinalização do Cálcio
Proteínas de Transporte/genética
Linhagem Celular Tumoral
Células HEK293
Seres Humanos
Insulina/metabolismo
Insulina/secreção
Células Secretoras de Insulina/metabolismo
Células Secretoras de Insulina/secreção
Proteínas do Tecido Nervoso/genética
Células Neuroendócrinas/secreção
Domínios Proteicos
Transporte Proteico
Interferência de RNA
Ratos
Vesículas Secretórias/secreção
Transfecção
Rede trans-Golgi/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (BAIAP3 protein, human); 0 (BAIAP3 protein, rat); 0 (Carrier Proteins); 0 (Insulin); 0 (Nerve Tissue Proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170913
[Lr] Data última revisão:
170913
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170620
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201702099



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