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[PMID]: 28057533 [Au] Autor: Haglerød C; Hussain S; Nakamura Y; Xia J; Haug FS; Ottersen OP; Henley JM; Davanger S [Ad] Endereço: Institute of Basic Medical Sciences, Division of Anatomy, University of Oslo, Oslo, Norway. [Ti] Título: Presynaptic PICK1 facilitates trafficking of AMPA-receptors between active zone and synaptic vesicle pool. [So] Source: Neuroscience;344:102-112, 2017 Mar 06. [Is] ISSN: 1873-7544 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Previous studies have indicated that presynaptic α-amino-3-hydroxy-5-methyl-4-isoxazole propionate receptors (AMPARs) contribute to the regulation of neurotransmitter release. In hippocampal synapses, the presynaptic surface expression of several AMPAR subunits, including GluA2, is regulated in a ligand-dependent manner. However, the molecular mechanisms underlying the presynaptic trafficking of AMPARs are still unknown. Here, using bright-field immunocytochemistry, western blots, and quantitative immunogold electron microscopy of the hippocampal CA1 area from intact adult rat brain, we demonstrate the association of AMPA receptors with the presynaptic active zone and with small presynaptic vesicles, in Schaffer collateral synapses in CA1 of the hippocampus. Furthermore, we show that GluA2 and protein interacting with C kinase 1 (PICK1) are colocalized at presynaptic vesicles. Similar to postsynaptic mechanisms, overexpression of either PICK1 or pep2m, which inhibit the N-ethylmaleimide sensitive fusion protein (NSF)-GluA2 interaction, decreases the concentration of GluA2 in the presynaptic active zone membrane. These data suggest that the interacting proteins PICK1 and NSF act as regulators of presynaptic GluA2-containing AMPAR trafficking between the active zone and a vesicle pool that may provide the basis of presynaptic components of synaptic plasticity. [Mh] Termos MeSH primário: Proteínas de Transporte/metabolismo Proteínas Nucleares/metabolismo Terminações Pré-Sinápticas/metabolismo Receptores de AMPA/metabolismo Vesículas Sinápticas/metabolismo [Mh] Termos MeSH secundário: Animais Encéfalo/metabolismo Encéfalo/ultraestrutura Citoplasma/metabolismo Citoplasma/ultraestrutura Immunoblotting Imuno-Histoquímica Masculino Microscopia Eletrônica Proteínas Sensíveis a N-Etilmaleimida/metabolismo Terminações Pré-Sinápticas/ultraestrutura Ratos Wistar Vesículas Sinápticas/ultraestrutura Técnicas de Cultura de Tecidos [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Carrier Proteins); 0 (Nuclear Proteins); 0 (Prkcabp protein, rat); 0 (Receptors, AMPA); 0 (glutamate receptor ionotropic, AMPA 2); EC 3.6.4.6 (N-Ethylmaleimide-Sensitive Proteins); EC 3.6.4.6 (Nsf protein, rat) [Em] Mês de entrada: 1711 [Cu] Atualização por classe: 171116 [Lr] Data última revisão: 171116 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170107 [St] Status: MEDLINE

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[PMID]: 27995606 [Au] Autor: Fan J; Zhou X; Wang Y; Kuang C; Sun Y; Liu X; Toomre D; Xu Y [Ad] Endereço: Department of Biomedical Engineering, Key Laboratory of Biomedical Engineering of Ministry of Education, Zhejiang University, Hangzhou, China. [Ti] Título: Differential requirement for N-ethylmaleimide-sensitive factor in endosomal trafficking of transferrin receptor from anterograde trafficking of vesicular stomatitis virus glycoprotein G. [So] Source: FEBS Lett;591(2):273-281, 2017 Jan. [Is] ISSN: 1873-3468 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: N-ethylmaleimide-sensitive fusion factor (NSF) is an ATPase that plays a crucial role in vesicular transport. Here, we examined the effects of NSF knockdown on Golgi structure and different vesicle trafficking pathways in mammalian cells. NSF knockdown caused Golgi fragmentation and abolished transferrin receptor exocytosis, defects that were rescued by RNAi-resistant NSF. Strikingly, NSF deficiency in HeLa cells barely affected cell viability, anterograde trafficking of vesicular stomatitis virus glycoprotein G and transferrin endocytosis. These results confirm the central role of NSF in Golgi structure and reveal differential requirement of NSF for exocytic recycling and constitutive trafficking pathways. [Mh] Termos MeSH primário: Endossomos/metabolismo Glicoproteínas de Membrana/metabolismo Proteínas Sensíveis a N-Etilmaleimida/metabolismo Receptores da Transferrina/metabolismo Proteínas do Envelope Viral/metabolismo [Mh] Termos MeSH secundário: Adenosina Trifosfatases/metabolismo Endocitose Exocitose Técnicas de Silenciamento de Genes Complexo de Golgi/metabolismo Células HeLa Seres Humanos Mutação/genética Transporte Proteico Interferência de RNA Vesículas Transportadoras/metabolismo [Pt] Tipo de publicação: LETTER [Nm] Nome de substância: 0 (G protein, vesicular stomatitis virus); 0 (Membrane Glycoproteins); 0 (Receptors, Transferrin); 0 (Viral Envelope Proteins); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.4.6 (N-Ethylmaleimide-Sensitive Proteins) [Em] Mês de entrada: 1705 [Cu] Atualização por classe: 170512 [Lr] Data última revisão: 170512 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 161221 [St] Status: MEDLINE [do] DOI: 10.1002/1873-3468.12532

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[PMID]: 27821621 [Au] Autor: Selvakumar D; Drescher MJ; Deckard NA; Ramakrishnan NA; Morley BJ; Drescher DG [Ad] Endereço: Laboratory of Bio-otology, Department of Otolaryngology, Wayne State University School of Medicine, Detroit, MI 48201, U.S.A. [Ti] Título: Dopamine D1A directly interacts with otoferlin synaptic pathway proteins: Ca2+ and phosphorylation underlie an NSF-to-AP2mu1 molecular switch. [So] Source: Biochem J;474(1):79-104, 2017 Jan 01. [Is] ISSN: 1470-8728 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: Dopamine receptors regulate exocytosis via protein-protein interactions (PPIs) as well as via adenylyl cyclase transduction pathways. Evidence has been obtained for PPIs in inner ear hair cells coupling D1A to soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein receptor (SNARE)-related proteins snapin, otoferlin, N-ethylmaleimide-sensitive factor (NSF), and adaptor-related protein complex 2, mu 1 (AP2mu1), dependent on [Ca ] and phosphorylation. Specifically, the carboxy terminus of dopamine D1A was found to directly bind t-SNARE-associated protein snapin in teleost and mammalian hair cell models by yeast two-hybrid (Y2H) and pull-down assays, and snapin directly interacts with hair cell calcium-sensor otoferlin. Surface plasmon resonance (SPR) analysis, competitive pull-downs, and co-immunoprecipitation indicated that these interactions were promoted by Ca and occur together. D1A was also found to separately interact with NSF, but with an inverse dependence on Ca Evidence was obtained, for the first time, that otoferlin domains C2A, C2B, C2D, and C2F interact with NSF and AP2mu1, whereas C2C or C2E do not bind to either protein, representing binding characteristics consistent with respective inclusion or omission in individual C2 domains of the tyrosine motif YXXΦ. In competitive pull-down assays, as predicted by K values from SPR (+Ca ), C2F pulled down primarily NSF as opposed to AP2mu1. Phosphorylation of AP2mu1 gave rise to a reversal: an increase in binding by C2F to phosphorylated AP2mu1 was accompanied by a decrease in binding to NSF, consistent with a molecular switch for otoferlin from membrane fusion (NSF) to endocytosis (AP2mu1). An increase in phosphorylated AP2mu1 at the base of the cochlear inner hair cell was the observed response elicited by a dopamine D1A agonist, as predicted. [Mh] Termos MeSH primário: Sinalização do Cálcio/fisiologia Proteínas de Peixes Células Ciliadas Vestibulares/metabolismo Proteínas Sensíveis a N-Etilmaleimida Receptores de Dopamina D1 Sinapses Truta [Mh] Termos MeSH secundário: Animais Proteínas de Peixes/genética Proteínas de Peixes/metabolismo Camundongos Proteínas Sensíveis a N-Etilmaleimida/genética Proteínas Sensíveis a N-Etilmaleimida/metabolismo Ratos Receptores de Dopamina D1/genética Receptores de Dopamina D1/metabolismo Proteínas SNARE/genética Proteínas SNARE/metabolismo Sinapses/genética Sinapses/metabolismo Truta/genética Truta/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Fish Proteins); 0 (Receptors, Dopamine D1); 0 (SNARE Proteins); 0 (dopamine D1A receptor); EC 3.6.4.6 (N-Ethylmaleimide-Sensitive Proteins) [Em] Mês de entrada: 1706 [Cu] Atualização por classe: 170609 [Lr] Data última revisão: 170609 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 161109 [St] Status: MEDLINE [do] DOI: 10.1042/BCJ20160690

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[PMID]: 27543417 [Au] Autor: Cao F; Zhou Z; Pan X; Leung C; Xie W; Collingridge G; Jia Z [Ad] Endereço: Neurosciences & Mental Health, The Hospital for Sick Children, 555 University Ave., Toronto, Ontario M5G 1X8, Canada; Department of Physiology, Faculty of Medicine, University of Toronto, Canada; The Key Laboratory of Developmental Genes and Human Disease, Jiangsu Co-innovation Center of Neurore [Ti] Título: Developmental regulation of hippocampal long-term depression by cofilin-mediated actin reorganization. [So] Source: Neuropharmacology;112(Pt A):66-75, 2017 Jan. [Is] ISSN: 1873-7064 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: Long lasting synaptic plasticity involves both functional and morphological changes, but how these processes are molecularly linked to achieve coordinated plasticity remains poorly understood. Cofilin is a common target of multiple signaling pathways at the synapse and is required for both functional and spine plasticity, but how it is regulated is unclear. In this study, we investigate whether the involvement of cofilin in plasticity is developmentally regulated by examining the role of cofilin in hippocampal long-term depression (LTD) in both young (2 weeks) and mature (2 months) mice. We show that both total protein level of cofilin and its activation undergo significant changes as the brain matures, so that although the amount of cofilin decreases significantly in mature mice, its regulation by protein phosphorylation becomes increasingly important. Consistent with these biochemical data, we show that cofilin-mediated actin reorganization is essential for LTD in mature, but not in young mice. In contrast to cofilin, the GluA2 interactions with NSF and PICK1 appear to be required in both young and mature mice, indicating that AMPAR internalization is a common key mechanism for LTD expression regardless of the developmental stages. These results establish the temporal specificity of cofilin in LTD regulation and suggest that cofilin-mediated actin reorganization may serve as a key mechanism underlying developmental regulation of synaptic and spine plasticity. This article is part of the Special Issue entitled 'Ionotropic glutamate receptors'. [Mh] Termos MeSH primário: Fatores de Despolimerização de Actina/fisiologia Actinas/fisiologia Hipocampo/fisiologia Depressão Sináptica de Longo Prazo [Mh] Termos MeSH secundário: Fatores de Despolimerização de Actina/metabolismo Actinas/metabolismo Animais Proteínas de Transporte/metabolismo Proteínas de Transporte/fisiologia Potenciais Pós-Sinápticos Excitadores Hipocampo/crescimento & desenvolvimento Hipocampo/metabolismo Camundongos Camundongos Endogâmicos C57BL Proteínas Sensíveis a N-Etilmaleimida/metabolismo Proteínas Sensíveis a N-Etilmaleimida/fisiologia Proteínas Nucleares/metabolismo Proteínas Nucleares/fisiologia [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Actin Depolymerizing Factors); 0 (Actins); 0 (Carrier Proteins); 0 (Nuclear Proteins); 0 (Prkcabp protein, mouse); EC 3.6.4.6 (N-Ethylmaleimide-Sensitive Proteins); EC 3.6.4.6 (Nsf protein, mouse) [Em] Mês de entrada: 1707 [Cu] Atualização por classe: 171116 [Lr] Data última revisão: 171116 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 160821 [St] Status: MEDLINE

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[PMID]: 27902705 [Au] Autor: Fontenas L; De Santis F; Di Donato V; Degerny C; Chambraud B; Del Bene F; Tawk M [Ad] Endereço: U1195, Inserm, University Paris Sud, University Paris-Saclay, Kremlin-Bicêtre, France. [Ti] Título: Neuronal Ndrg4 Is Essential for Nodes of Ranvier Organization in Zebrafish. [So] Source: PLoS Genet;12(11):e1006459, 2016 Nov. [Is] ISSN: 1553-7404 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Axon ensheathment by specialized glial cells is an important process for fast propagation of action potentials. The rapid electrical conduction along myelinated axons is mainly due to its saltatory nature characterized by the accumulation of ion channels at the nodes of Ranvier. However, how these ion channels are transported and anchored along axons is not fully understood. We have identified N-myc downstream-regulated gene 4, ndrg4, as a novel factor that regulates sodium channel clustering in zebrafish. Analysis of chimeric larvae indicates that ndrg4 functions autonomously within neurons for sodium channel clustering at the nodes. Molecular analysis of ndrg4 mutants shows that expression of snap25 and nsf are sharply decreased, revealing a role of ndrg4 in controlling vesicle exocytosis. This uncovers a previously unknown function of ndrg4 in regulating vesicle docking and nodes of Ranvier organization, at least through its ability to finely tune the expression of the t-SNARE/NSF machinery. [Mh] Termos MeSH primário: Proteínas Musculares/genética Proteínas Sensíveis a N-Etilmaleimida/biossíntese Nós Neurofibrosos/genética Proteína 25 Associada a Sinaptossoma/biossíntese Proteínas de Peixe-Zebra/biossíntese Proteínas de Peixe-Zebra/genética Peixe-Zebra/genética [Mh] Termos MeSH secundário: Animais Axônios/metabolismo Exocitose/genética Regulação da Expressão Gênica Seres Humanos Proteínas Musculares/metabolismo Proteínas Sensíveis a N-Etilmaleimida/genética Neuroglia/metabolismo Neurônios/metabolismo Nós Neurofibrosos/metabolismo Células de Schwann Canais de Sódio/genética Canais de Sódio/metabolismo Transmissão Sináptica/genética Proteína 25 Associada a Sinaptossoma/genética Peixe-Zebra/metabolismo Proteínas de Peixe-Zebra/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Muscle Proteins); 0 (Ndrg4 protein, zebrafish); 0 (Sodium Channels); 0 (Synaptosomal-Associated Protein 25); 0 (Zebrafish Proteins); EC 3.6.4.6 (N-Ethylmaleimide-Sensitive Proteins); EC 3.6.4.6 (N-ethylmaleimide sensitive factor, zebrafish) [Em] Mês de entrada: 1704 [Cu] Atualização por classe: 170428 [Lr] Data última revisão: 170428 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 161201 [St] Status: MEDLINE [do] DOI: 10.1371/journal.pgen.1006459

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[PMID]: 27355324 [Au] Autor: Lee JY; Linge HM; Ochani K; Lin K; Miller EJ [Ad] Endereço: The Elmezzi Graduate School of Molecular Medicine, Manhasset, New York, United States of America. [Ti] Título: N-Ethylmaleimide Sensitive Factor (NSF) Inhibition Prevents Vascular Instability following Gram-Positive Pulmonary Challenge. [So] Source: PLoS One;11(6):e0157837, 2016. [Is] ISSN: 1932-6203 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: BACKGROUND: The Acute Respiratory Distress Syndrome (ARDS), remains a significant source of morbidity and mortality in critically ill patients. Pneumonia and sepsis are leading causes of ARDS, the pathophysiology of which includes increased pulmonary microvascular permeability and hemodynamic instability resulting in organ dysfunction. We hypothesized that N-ethylmaleimide sensitive factor (NSF) regulates exocytosis of inflammatory mediators, such as Angiopoietin-2 (Ang-2), and cytoskeletal stability by modulating myosin light chain (MLC) phosphorylation. Therefore, we challenged pulmonary cells, in vivo and in vitro, with Gram Positive bacterial cell wall components, lipoteichoic acid (LTA), and peptidoglycan (PGN) and examined the effects of NSF inhibition. METHODS: Mice were pre-treated with an inhibitor of NSF, TAT-NSF700 (to prevent Ang-2 release). After 30min, LTA and PGN (or saline alone) were instilled intratracheally. Pulse oximetry was assessed in awake mice prior to, and 6 hour post instillation. Post mortem, tissues were collected for studies of inflammation and Ang-2. In vitro, pulmonary endothelial cells were assessed for their responses to LTA and PGN. RESULTS: Pulmonary challenge induced signs of airspace and systemic inflammation such as changes in neutrophil counts and protein concentration in bronchoalveolar lavage fluid and tissue Ang-2 concentration, and decreased physiological parameters including oxygen saturation and pulse distention. TAT-NSF700 pre-treatment reduced LTA-PGN induced changes in lung tissue Ang-2, oxygen saturation and pulse distention. In vitro, LTA-PGN induced a rapid (<2 min) release of Ang-2, which was significantly attenuated by TAT-NSF700 or anti TLR2 antibody. Furthermore, TAT-NSF700 reduced LTA-PGN-induced MLC phosphorylation at low concentrations of 1-10 nM. CONCLUSIONS: TAT-NSF700 decreased Ang-2 release, improved oxygen saturation and pulse distention following pulmonary challenge by inhibiting MLC phosphorylation, an important component of endothelial cell retraction. The data suggest that inhibition of NSF in pneumonia and sepsis may be beneficial to prevent the pulmonary microvascular and hemodynamic instability associated with ARDS. [Mh] Termos MeSH primário: Infecções Bacterianas/complicações Pulmão/microbiologia Proteínas Sensíveis a N-Etilmaleimida/fisiologia Síndrome do Desconforto Respiratório do Adulto/complicações [Mh] Termos MeSH secundário: Angiopoietina-1/metabolismo Animais Vasos Sanguíneos/patologia Linhagem Celular Parede Celular/efeitos dos fármacos Citoesqueleto/metabolismo Modelos Animais de Doenças Exocitose Bactérias Gram-Positivas Seres Humanos Inflamação Lipopolissacarídeos/química Masculino Camundongos Camundongos Endogâmicos BALB C Microcirculação Proteínas Sensíveis a N-Etilmaleimida/antagonistas & inibidores Oxigênio/química Peptidoglicano/química Fosforilação Pneumonia/metabolismo Síndrome do Desconforto Respiratório do Adulto/microbiologia Sepse/metabolismo Ácidos Teicoicos/química Doenças Vasculares/metabolismo Doenças Vasculares/prevenção & controle [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Angiopoietin-1); 0 (Lipopolysaccharides); 0 (Peptidoglycan); 0 (Teichoic Acids); 56411-57-5 (lipoteichoic acid); EC 3.6.4.6 (N-Ethylmaleimide-Sensitive Proteins); EC 3.6.4.6 (Nsf protein, mouse); S88TT14065 (Oxygen) [Em] Mês de entrada: 1707 [Cu] Atualização por classe: 171116 [Lr] Data última revisão: 171116 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 160630 [St] Status: MEDLINE [do] DOI: 10.1371/journal.pone.0157837

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[PMID]: 27277949 [Au] Autor: Zhou Y; Yang SX; Yue YN; Wei XF; Liu Y [Ad] Endereço: Department of Cardiology, Beijing Shijitan Hospital, Capital Medical University, Beijing 100038, P.R. China. [Ti] Título: N-ethylmaleimide­sensitive factor siRNA inhibits the release of Weibel-Palade bodies in endothelial cells. [So] Source: Mol Med Rep;14(2):1061-6, 2016 Aug. [Is] ISSN: 1791-3004 [Cp] País de publicação: Greece [La] Idioma: eng [Ab] Resumo: The aim of the present study was to examine the effect of small interfering RNA (siRNA) methods on the expression of N­ethylmaleimide sensitive factor (NSF) and Weibel­Palade body (WPB) release in endothelial cells. A small hairpin RNA (shRNA), mediated with an adenovirus vector, was designed to target the N­terminal functional area of NSF. Subsequently, viruses were transfected into human aortic endothelial cells. The mRNA and protein expression levels of NSF were detected using reverse transcription­quantitative polymerase chain reaction and Western blot analyses, respectively, and the release of WPBs in the endothelial cells was examined using immunofluorescence. The mRNA expression of NSF in the endothelial cells, which were transfected with the adenoviruses carrying the NSF­shRNA was significantly decreased, compared with the negative control group (P=0.035) and blank control group (P=0.02). In addition, the mRNA expression of NSF was gradually decreased as duration increased; there were marked differences between the 24, 48 and 72 h groups (P<0.05). The protein expression of NSF was significantly decreased in the experimental group, compared with the negative control group (P=0.004) and blank control group (P=0.031), however, no difference was observed between the negative control and blank control groups (P=0.249). The immunofluorescence staining showed that the release of WPBs in the endothelial cells induced with thrombin was inhibited markedly following transfection with the virus carrying the NSF­shRNA. Therefore NSF­siRNA inhibited the mRNA and protein expression levels of NSF, and inhibited the release of WPBs in endothelial cells induced with thrombin. These results suggested that NSF-siRNA may be valuable for preventing and treating atherosclerosis and acute coronary syndrome. [Mh] Termos MeSH primário: Células Endoteliais/metabolismo Regulação da Expressão Gênica Proteínas Sensíveis a N-Etilmaleimida/genética Interferência de RNA RNA Interferente Pequeno/genética Corpos de Weibel-Palade/metabolismo [Mh] Termos MeSH secundário: Adenoviridae/genética Células Cultivadas Expressão Gênica Vetores Genéticos/genética Seres Humanos Transdução Genética [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (RNA, Small Interfering); EC 3.6.4.6 (N-Ethylmaleimide-Sensitive Proteins) [Em] Mês de entrada: 1704 [Cu] Atualização por classe: 170406 [Lr] Data última revisão: 170406 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 160610 [St] Status: MEDLINE [do] DOI: 10.3892/mmr.2016.5372

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[PMID]: 27254316 [Au] Autor: Wehrendt DP; Carmona F; González Wusener AE; González Á; Martínez JM; Arregui CO [Ad] Endereço: Instituto de Investigaciones Biotecnológicas, (IIB-INTECH), Universidad de San Martín, San Martín, Argentina. [Ti] Título: P120-Catenin Regulates Early Trafficking Stages of the N-Cadherin Precursor Complex. [So] Source: PLoS One;11(6):e0156758, 2016. [Is] ISSN: 1932-6203 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: It is well established that binding of p120 catenin to the cytoplasmic domain of surface cadherin prevents cadherin endocytosis and degradation, contributing to cell-cell adhesion. In the present work we show that p120 catenin bound to the N-cadherin precursor, contributes to its anterograde movement from the endoplasmic reticulum (ER) to the Golgi complex. In HeLa cells, depletion of p120 expression, or blocking its binding to N-cadherin, increased the accumulation of the precursor in the ER, while it decreased the localization of mature N-cadherin at intercellular junctions. Reconstitution experiments in p120-deficient SW48 cells with all three major isoforms of p120 (1, 3 and 4) had similar capacity to promote the processing of the N-cadherin precursor to the mature form, and its localization at cell-cell junctions. P120 catenin and protein tyrosine phosphatase PTP1B facilitated the recruitment of the N-ethylmaleimide sensitive factor (NSF), an ATPase involved in vesicular trafficking, to the N-cadherin precursor complex. Dominant negative NSF E329Q impaired N-cadherin trafficking, maturation and localization at cell-cell junctions. Our results uncover a new role for p120 catenin bound to the N-cadherin precursor ensuring its trafficking through the biosynthetic pathway towards the cell surface. [Mh] Termos MeSH primário: Caderinas/metabolismo Cateninas/metabolismo [Mh] Termos MeSH secundário: Técnicas de Silenciamento de Genes Células HeLa Seres Humanos Modelos Biológicos Proteínas Sensíveis a N-Etilmaleimida/metabolismo Ligação Proteica Processamento de Proteína Pós-Traducional Transporte Proteico Via Secretória [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Cadherins); 0 (Catenins); 0 (delta catenin); EC 3.6.4.6 (N-Ethylmaleimide-Sensitive Proteins) [Em] Mês de entrada: 1707 [Cu] Atualização por classe: 170719 [Lr] Data última revisão: 170719 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 160603 [St] Status: MEDLINE [do] DOI: 10.1371/journal.pone.0156758

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[PMID]: 27226605 [Au] Autor: Codding SJ; Marty N; Abdullah N; Johnson CP [Ad] Endereço: From the Department of Biochemistry and Biophysics, Oregon State University, Corvallis, Oregon 97331. [Ti] Título: Dysferlin Binds SNAREs (Soluble N-Ethylmaleimide-sensitive Factor (NSF) Attachment Protein Receptors) and Stimulates Membrane Fusion in a Calcium-sensitive Manner. [So] Source: J Biol Chem;291(28):14575-84, 2016 Jul 08. [Is] ISSN: 1083-351X [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Resealing of tears in the sarcolemma of myofibers is a necessary step in the repair of muscle tissue. Recent work suggests a critical role for dysferlin in the membrane repair process and that mutations in dysferlin are responsible for limb girdle muscular dystrophy 2B and Miyoshi myopathy. Beyond membrane repair, dysferlin has been linked to SNARE-mediated exocytotic events including cytokine release and acid sphingomyelinase secretion. However, it is unclear whether dysferlin regulates SNARE-mediated membrane fusion. In this study we demonstrate a direct interaction between dysferlin and the SNARE proteins syntaxin 4 and SNAP-23. In addition, analysis of FRET and in vitro reconstituted lipid mixing assays indicate that dysferlin accelerates syntaxin 4/SNAP-23 heterodimer formation and SNARE-mediated lipid mixing in a calcium-sensitive manner. These results support a function for dysferlin as a calcium-sensing SNARE effector for membrane fusion events. [Mh] Termos MeSH primário: Cálcio/metabolismo Fusão de Membrana Proteínas de Membrana/metabolismo Proteínas Musculares/metabolismo Proteínas Sensíveis a N-Etilmaleimida/metabolismo Proteínas SNARE/metabolismo [Mh] Termos MeSH secundário: Dimerização Disferlina Transferência Ressonante de Energia de Fluorescência Seres Humanos Metabolismo dos Lipídeos [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (DYSF protein, human); 0 (Dysferlin); 0 (Membrane Proteins); 0 (Muscle Proteins); 0 (SNARE Proteins); EC 3.6.4.6 (N-Ethylmaleimide-Sensitive Proteins); SY7Q814VUP (Calcium) [Em] Mês de entrada: 1701 [Cu] Atualização por classe: 171116 [Lr] Data última revisão: 171116 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 160527 [St] Status: MEDLINE [do] DOI: 10.1074/jbc.M116.727016

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[PMID]: 27105867 [Au] Autor: Nishizaki T [Ad] Endereço: Innovative Bioinformation Research Organization, Kobe, Japan. tnishizaki@bioresorganization.com. [Ti] Título: N-Ethylmaleimide Dissociates α7 ACh Receptor from a Complex with NSF and Promotes Its Delivery to the Presynaptic Membrane. [So] Source: Neurochem Res;41(8):2043-8, 2016 Aug. [Is] ISSN: 1573-6903 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: N-Ethylmaleimide (NEM)-sensitive factor (NSF) associates with soluble NSF attachment protein (SNAP), that binds to SNAP receptors (SNAREs) including syntaxin, SNAP25, and synaptobrevin. The complex of NSF/SNAP/SNAREs plays a critical role in the regulation of vesicular traffic. The present study investigated NEM-regulated α7 ACh receptor translocation. NSF associated with ß-SNAP and the SNAREs syntaxin 1 and synaptobrevin 2 in the rat hippocampus. NSF also associated with the α7 ACh receptor subunit, the α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor subunits GluA1 and GluA2, and the γ-aminobutyric acid A (GABAA) receptor γ2 subunit. NEM, an inhibitor of NSF, significantly dissociated the α7 ACh receptor subunit from a complex with NSF and increased cell surface localization of the receptor subunit, but such effect was not obtained with the GluA1, GluA2 or γ2 subunits. NEM, alternatively, dissociated synaptobrevin 2 from an assembly of NSF/ß-SNAP/syntaxin 1/synaptobrevin 2. NEM significantly increased the rate of nicotine-triggered AMPA receptor-mediated miniature excitatory postsynaptic currents, without affecting the amplitude, in rat hippocampal slices. The results of the present study indicate that NEM releases the α7 ACh receptor subunit and synaptobrevin 2 from an assembly of α7 ACh receptor subunit/NSF/ß-SNAP/syntaxin 1/synaptobrevin 2, thereby promoting delivery of the α7 ACh receptor subunit to presynaptic membrane. [Mh] Termos MeSH primário: Etilmaleimida/metabolismo Proteínas Sensíveis a N-Etilmaleimida/metabolismo Terminações Pré-Sinápticas/metabolismo Membranas Sinápticas/metabolismo Receptor Nicotínico de Acetilcolina alfa7/metabolismo [Mh] Termos MeSH secundário: Animais Relação Dose-Resposta a Droga Etilmaleimida/farmacologia Potenciais Pós-Sinápticos Excitadores/efeitos dos fármacos Potenciais Pós-Sinápticos Excitadores/fisiologia Hipocampo/efeitos dos fármacos Hipocampo/metabolismo Masculino Técnicas de Cultura de Órgãos Terminações Pré-Sinápticas/efeitos dos fármacos Ligação Proteica/efeitos dos fármacos Ligação Proteica/fisiologia Ratos Ratos Wistar Membranas Sinápticas/efeitos dos fármacos [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (alpha7 Nicotinic Acetylcholine Receptor); EC 3.6.4.6 (N-Ethylmaleimide-Sensitive Proteins); O3C74ACM9V (Ethylmaleimide) [Em] Mês de entrada: 1703 [Cu] Atualização por classe: 171031 [Lr] Data última revisão: 171031 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 160424 [St] Status: MEDLINE [do] DOI: 10.1007/s11064-016-1915-z

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