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Pesquisa : D08.811.277.040.025.047 [Categoria DeCS]
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[PMID]:28104892
[Au] Autor:Shao S; Rodrigo-Brenni MC; Kivlen MH; Hegde RS
[Ad] Endereço:Medical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge CB2 0QH, UK.
[Ti] Título:Mechanistic basis for a molecular triage reaction.
[So] Source:Science;355(6322):298-302, 2017 01 20.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Newly synthesized proteins are triaged between biosynthesis and degradation to maintain cellular homeostasis, but the decision-making mechanisms are unclear. We reconstituted the core reactions for membrane targeting and ubiquitination of nascent tail-anchored membrane proteins to understand how their fate is determined. The central six-component triage system is divided into an uncommitted client-SGTA complex, a self-sufficient targeting module, and an embedded but self-sufficient quality control module. Client-SGTA engagement of the targeting module induces rapid, private, and committed client transfer to TRC40 for successful biosynthesis. Commitment to ubiquitination is dictated primarily by comparatively slower client dissociation from SGTA and nonprivate capture by the BAG6 subunit of the quality control module. Our results provide a paradigm for how priority and time are encoded within a multichaperone triage system.
[Mh] Termos MeSH primário: Proteínas de Membrana/química
Modelos Moleculares
Biossíntese de Proteínas
Proteólise
[Mh] Termos MeSH secundário: ATPases Transportadoras de Arsenito/química
Proteínas de Transporte/química
Chaperonas Moleculares/química
Ubiquitinação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (ASNA1 protein, human); 0 (BAG6 protein, human); 0 (Carrier Proteins); 0 (Membrane Proteins); 0 (Molecular Chaperones); 0 (SGTA protein, human); EC 3.6.3.16 (Arsenite Transporting ATPases)
[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:170121
[St] Status:MEDLINE
[do] DOI:10.1126/science.aah6130


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[PMID]:27765046
[Au] Autor:Ott M; Marques D; Funk C; Bailer SM
[Ad] Endereço:Max von Pettenkofer-Institut, Ludwig-Maximilians-Universität München, Pettenkoferstr. 9a, 80336, München, Germany.
[Ti] Título:Asna1/TRC40 that mediates membrane insertion of tail-anchored proteins is required for efficient release of Herpes simplex virus 1 virions.
[So] Source:Virol J;13(1):175, 2016 Oct 20.
[Is] ISSN:1743-422X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Herpes simplex virus type 1 (HSV1), a member of the alphaherpesvirinae, can cause recurrent facial lesions and encephalitis. Two membrane envelopment processes, one at the inner nuclear membrane and a second at cytoplasmic membranes are crucial for a productive viral infection. Depending on the subfamily, herpesviruses encode more than 11 different transmembrane proteins including members of the tail-anchored protein family. HSV1 encodes three tail-anchored proteins pUL34, pUL56 and pUS9 characterized by a single hydrophobic region positioned at their C-terminal end that needs to be released from the ribosome prior to posttranslational membrane insertion. Asna1/TRC40 is an ATPase that targets tail-anchored proteins to the endoplasmic reticulum in a receptor-dependent manner. Cell biological data point to a critical and general role of Asna1/TRC40 in tail-anchored protein biogenesis. With this study, we aimed to determine the importance of the tail-anchored insertion machinery for HSV1 infection. METHODS: To determine protein-protein interactions, the yeast-two hybrid system was applied. Asna1/TRC40 was depleted using RNA interference. Transient transfection and virus infection experiments followed by indirect immunofluorescence analysis were applied to analyse the localization of viral proteins as well as the impact of Asna1/TRC40 depletion on virus infection. RESULTS: All HSV1 tail-anchored proteins specifically bound to Asna1/TRC40 but independently localized to their target membranes. While non-essential for cell viability, Asna1/TRC40 is required for efficient HSV1 replication. We show that early events of the replication cycle like virion entry and overall viral gene expression were unaffected by depletion of Asna1/TRC40. Furthermore, equal amounts of infectious virions were formed and remained cell-associated. This indicated that both nuclear egress of capsids that requires the essential tail-anchored protein pUL34, and secondary envelopment to form infectious virions were successfully completed. Despite large part of the virus life cycle proceeding normally, viral propagation was more than 10 fold reduced. We show that depletion of Asna1/TRC40 specifically affected a step late in infection during release of infectious virions to the extracellular milieu. CONCLUSIONS: Asna1/TRC40 is required at a late step of herpesviral infection for efficient release of mature virions to the extracellular milieu. This study reveals novel tools to decipher exocytosis of newly formed virions as well as hitherto unknown cellular targets for antiviral therapy.
[Mh] Termos MeSH primário: ATPases Transportadoras de Arsenito/metabolismo
Herpesvirus Humano 1/fisiologia
Interações Hospedeiro-Patógeno
Liberação de Vírus
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Técnicas de Silenciamento de Genes
Seres Humanos
Microscopia de Fluorescência
Mapeamento de Interação de Proteínas
Técnicas do Sistema de Duplo-Híbrido
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ASNA1 protein, human); EC 3.6.3.16 (Arsenite Transporting ATPases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161022
[St] Status:MEDLINE


  3 / 214 MEDLINE  
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[PMID]:27736728
[Au] Autor:Chen J; Cheng J; Yi J; Xie B; Lin L; Liu Z; Zhao H; Wang B; Ai Z; Yang Y; Wei H
[Ad] Endereço:Key Laboratory of Preclinical Study for New Drugs of Gansu Province, School of Basic Medical Sciences, Lanzhou University, Lanzhou, Gansu, China.
[Ti] Título:Differential expression and response to arsenic stress of MRPs and ASAN1 determine sensitivity of classical multidrug-resistant leukemia cells to arsenic trioxide.
[So] Source:Leuk Res;50:116-122, 2016 Nov.
[Is] ISSN:1873-5835
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:There is no cross-resistance between arsenic trioxide and conventional chemotherapeutics. Classical multi-drug resistant (MDR) cells remain sensitive to arsenic trioxide, which may even reverse the drug resistance. Arsenic trioxide is also effective in leukemias/tumors that persist despite conventional cytotoxic or targeted drugs. We obtained a highly arsenic-resistant MDR leukemic cell line, HL-60/RS, by exposing leukemic HL-60 cells to adriamycin selection. We compared the arsenic sensitivity, and the expression and responses to arsenic of the arsenic-related transporters, MRP1, MRP2, and ASNA1, in paired parent/arsenic-resistant HL-60/RS/HL-60 and arsenic-sensitive/parental K562/ADM/K562 cells. Expression levels of MRP1, MRP2, and ASNA1 were negatively correlated with cell sensitivities to arsenic trioxide, and ASNA1 expression notably was highest in HL-60/RS cells and lowest in K562/ADM cells. Expression levels of MRP1, MRP2, and ASNA1 were significantly enhanced in HL-60/RS cells and inhibited in K562/ADM cells by arsenic trioxide treatment, compared with their parental sensitive cells, in accord with the high-resistance of HL-60/RS cells and high-sensitivity of K562/ADM cells. In conclusion, the cross-resistance of conventional chemotherapeutics-resistant leukemic cells to arsenic trioxide is determined by both levels of MRP1, MRP2, and ASNA1, and also by the responses of these transporters to arsenic stress.
[Mh] Termos MeSH primário: Arsenicais/farmacologia
ATPases Transportadoras de Arsenito/efeitos dos fármacos
Resistência a Múltiplos Medicamentos/efeitos dos fármacos
Leucemia/patologia
Óxidos/farmacologia
[Mh] Termos MeSH secundário: Antineoplásicos/farmacologia
Arsênico/farmacologia
ATPases Transportadoras de Arsenito/análise
Resistência a Medicamentos Antineoplásicos/efeitos dos fármacos
Expressão Gênica/efeitos dos fármacos
Células HL-60
Seres Humanos
Células K562
Leucemia/tratamento farmacológico
Proteínas Associadas à Resistência a Múltiplos Medicamentos/análise
Proteínas Associadas à Resistência a Múltiplos Medicamentos/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ASNA1 protein, human); 0 (Antineoplastic Agents); 0 (Arsenicals); 0 (Multidrug Resistance-Associated Proteins); 0 (Oxides); 4AF605U6JN (multidrug resistance-associated protein 2); EC 3.6.3.16 (Arsenite Transporting ATPases); N712M78A8G (Arsenic); S7V92P67HO (arsenic trioxide); Y49M64GZ4Q (multidrug resistance-associated protein 1)
[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:161014
[St] Status:MEDLINE


  4 / 214 MEDLINE  
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[PMID]:27458190
[Au] Autor:Vogl C; Panou I; Yamanbaeva G; Wichmann C; Mangosing SJ; Vilardi F; Indzhykulian AA; Pangrsic T; Santarelli R; Rodriguez-Ballesteros M; Weber T; Jung S; Cardenas E; Wu X; Wojcik SM; Kwan KY; Del Castillo I; Schwappach B; Strenzke N; Corey DP; Lin SY; Moser T
[Ad] Endereço:Institute for Auditory Neuroscience and InnerEarLab, University Medical Center Göttingen, Göttingen, Germany.
[Ti] Título:Tryptophan-rich basic protein (WRB) mediates insertion of the tail-anchored protein otoferlin and is required for hair cell exocytosis and hearing.
[So] Source:EMBO J;35(23):2536-2552, 2016 Dec 01.
[Is] ISSN:1460-2075
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The transmembrane recognition complex (TRC40) pathway mediates the insertion of tail-anchored (TA) proteins into membranes. Here, we demonstrate that otoferlin, a TA protein essential for hair cell exocytosis, is inserted into the endoplasmic reticulum (ER) via the TRC40 pathway. We mutated the TRC40 receptor tryptophan-rich basic protein (Wrb) in hair cells of zebrafish and mice and studied the impact of defective TA protein insertion. Wrb disruption reduced otoferlin levels in hair cells and impaired hearing, which could be restored in zebrafish by transgenic Wrb rescue and otoferlin overexpression. Wrb-deficient mouse inner hair cells (IHCs) displayed normal numbers of afferent synapses, Ca channels, and membrane-proximal vesicles, but contained fewer ribbon-associated vesicles. Patch-clamp of IHCs revealed impaired synaptic vesicle replenishment. In vivo recordings from postsynaptic spiral ganglion neurons showed a use-dependent reduction in sound-evoked spiking, corroborating the notion of impaired IHC vesicle replenishment. A human mutation affecting the transmembrane domain of otoferlin impaired its ER targeting and caused an auditory synaptopathy. We conclude that the TRC40 pathway is critical for hearing and propose that otoferlin is an essential substrate of this pathway in hair cells.
[Mh] Termos MeSH primário: ATPases Transportadoras de Arsenito/metabolismo
Exocitose
Células Ciliadas Auditivas/metabolismo
Audição
Proteínas de Membrana/metabolismo
Proteínas Nucleares/metabolismo
[Mh] Termos MeSH secundário: Animais
Técnicas de Inativação de Genes
Teste de Complementação Genética
Seres Humanos
Camundongos
Proteínas Nucleares/genética
Peixe-Zebra
Proteínas de Peixe-Zebra/genética
Proteínas de Peixe-Zebra/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Membrane Proteins); 0 (Nuclear Proteins); 0 (OTOF protein, human); 0 (WRB protein, human); 0 (Zebrafish Proteins); 0 (otoferlin protein, mouse); 0 (wrb protein, zebrafish); EC 3.6.3.16 (Arsenite Transporting ATPases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170703
[Lr] Data última revisão:
170703
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160727
[St] Status:MEDLINE


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[PMID]:27226539
[Au] Autor:Colombo SF; Cardani S; Maroli A; Vitiello A; Soffientini P; Crespi A; Bram RF; Benfante R; Borgese N
[Ad] Endereço:From the CNR Institute of Neuroscience and BIOMETRA Department, Università degli Studi di Milano and s.colombo@in.cnr.it.
[Ti] Título:Tail-anchored Protein Insertion in Mammals: FUNCTION AND RECIPROCAL INTERACTIONS OF THE TWO SUBUNITS OF THE TRC40 RECEPTOR.
[So] Source:J Biol Chem;291(29):15292-306, 2016 07 15.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The GET (guided entry of tail-anchored proteins)/TRC (transmembrane recognition complex) pathway for tail-anchored protein targeting to the endoplasmic reticulum (ER) has been characterized in detail in yeast and is thought to function similarly in mammals, where the orthologue of the central ATPase, Get3, is known as TRC40 or Asna1. Get3/TRC40 function requires an ER receptor, which in yeast consists of the Get1/Get2 heterotetramer and in mammals of the WRB protein (tryptophan-rich basic protein), homologous to yeast Get1, in combination with CAML (calcium-modulating cyclophilin ligand), which is not homologous to Get2. To better characterize the mammalian receptor, we investigated the role of endogenous WRB and CAML in tail-anchored protein insertion as well as their association, concentration, and stoichiometry in rat liver microsomes and cultured cells. Functional proteoliposomes, reconstituted from a microsomal detergent extract, lost their activity when made with an extract depleted of TRC40-associated proteins or of CAML itself, whereas in vitro synthesized CAML and WRB together were sufficient to confer insertion competence to liposomes. CAML was found to be in ∼5-fold excess over WRB, and alteration of this ratio did not inhibit insertion. Depletion of each subunit affected the levels of the other one; in the case of CAML silencing, this effect was attributable to destabilization of the WRB transcript and not of WRB protein itself. These results reveal unanticipated complexity in the mutual regulation of the TRC40 receptor subunits and raise the question as to the role of the excess CAML in the mammalian ER.
[Mh] Termos MeSH primário: ATPases Transportadoras de Arsenito/química
ATPases Transportadoras de Arsenito/metabolismo
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/química
Proteínas Adaptadoras de Transdução de Sinal/genética
Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Adenosina Trifosfatases/química
Adenosina Trifosfatases/metabolismo
Animais
ATPases Transportadoras de Arsenito/genética
Linhagem Celular
Células Cultivadas
Síndrome de Down/genética
Síndrome de Down/metabolismo
Retículo Endoplasmático/metabolismo
Regulação da Expressão Gênica
Fatores de Troca do Nucleotídeo Guanina/química
Fatores de Troca do Nucleotídeo Guanina/metabolismo
Células HeLa
Seres Humanos
Microssomos Hepáticos/metabolismo
Proteínas Nucleares/química
Proteínas Nucleares/genética
Proteínas Nucleares/metabolismo
Subunidades Proteicas
Transporte Proteico
Proteolipídeos/metabolismo
Ratos
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (ASNA1 protein, human); 0 (Adaptor Proteins, Signal Transducing); 0 (CAMLG protein, human); 0 (Camlg protein, rat); 0 (Guanine Nucleotide Exchange Factors); 0 (Nuclear Proteins); 0 (Protein Subunits); 0 (Proteolipids); 0 (Recombinant Proteins); 0 (Saccharomyces cerevisiae Proteins); 0 (WRB protein, human); 0 (proteoliposomes); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.3.16 (Arsenite Transporting ATPases); EC 3.6.3.16 (Get3 protein, S cerevisiae)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171124
[Lr] Data última revisão:
171124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160527
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.707752


  6 / 214 MEDLINE  
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[PMID]:26675233
[Au] Autor:Pfaff J; Rivera Monroy J; Jamieson C; Rajanala K; Vilardi F; Schwappach B; Kehlenbach RH
[Ad] Endereço:Department of Molecular Biology, Faculty of Medicine, Georg-August-University, GZMB, Humboldtallee 23, Göttingen 37073, Germany.
[Ti] Título:Emery-Dreifuss muscular dystrophy mutations impair TRC40-mediated targeting of emerin to the inner nuclear membrane.
[So] Source:J Cell Sci;129(3):502-16, 2016 Feb 01.
[Is] ISSN:1477-9137
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Emerin is a tail-anchored protein that is found predominantly at the inner nuclear membrane (INM), where it associates with components of the nuclear lamina. Mutations in the emerin gene cause Emery-Dreifuss muscular dystrophy (EDMD), an X-linked recessive disease. Here, we report that the TRC40/GET pathway for post-translational insertion of tail-anchored proteins into membranes is involved in emerin-trafficking. Using proximity ligation assays, we show that emerin interacts with TRC40 in situ. Emerin expressed in bacteria or in a cell-free lysate was inserted into microsomal membranes in an ATP- and TRC40-dependent manner. Dominant-negative fragments of the TRC40-receptor proteins WRB and CAML (also known as CAMLG) inhibited membrane insertion. A rapamycin-based dimerization assay revealed correct transport of wild-type emerin to the INM, whereas TRC40-binding, membrane integration and INM-targeting of emerin mutant proteins that occur in EDMD was disturbed. Our results suggest that the mode of membrane integration contributes to correct targeting of emerin to the INM.
[Mh] Termos MeSH primário: ATPases Transportadoras de Arsenito/metabolismo
Proteínas de Membrana/metabolismo
Distrofia Muscular de Emery-Dreifuss/genética
Distrofia Muscular de Emery-Dreifuss/metabolismo
Mutação/genética
Membrana Nuclear/metabolismo
Proteínas Nucleares/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Linhagem Celular Tumoral
Células HeLa
Seres Humanos
Microssomos/metabolismo
Ligação Proteica/genética
Processamento de Proteína Pós-Traducional/genética
Transporte Proteico/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (ASNA1 protein, human); 0 (Membrane Proteins); 0 (Nuclear Proteins); 0 (emerin); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.3.16 (Arsenite Transporting ATPases)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151218
[St] Status:MEDLINE
[do] DOI:10.1242/jcs.179333


  7 / 214 MEDLINE  
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[PMID]:26438609
[Au] Autor:Norlin S; Parekh VS; Naredi P; Edlund H
[Ad] Endereço:Umeå Centre for Molecular Medicine, Umeå University, Umeå, Sweden.
[Ti] Título:Asna1/TRC40 Controls ß-Cell Function and Endoplasmic Reticulum Homeostasis by Ensuring Retrograde Transport.
[So] Source:Diabetes;65(1):110-9, 2016 Jan.
[Is] ISSN:1939-327X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Type 2 diabetes (T2D) is characterized by insulin resistance and ß-cell failure. Insulin resistance per se, however, does not provoke overt diabetes as long as compensatory ß-cell function is maintained. The increased demand for insulin stresses the ß-cell endoplasmic reticulum (ER) and secretory pathway, and ER stress is associated with ß-cell failure in T2D. The tail recognition complex (TRC) pathway, including Asna1/TRC40, is implicated in the maintenance of endomembrane trafficking and ER homeostasis. To gain insight into the role of Asna1/TRC40 in maintaining endomembrane homeostasis and ß-cell function, we inactivated Asna1 in ß-cells of mice. We show that Asna1(ß-/-) mice develop hypoinsulinemia, impaired insulin secretion, and glucose intolerance that rapidly progresses to overt diabetes. Loss of Asna1 function leads to perturbed plasma membrane-to-trans Golgi network and Golgi-to-ER retrograde transport as well as to ER stress in ß-cells. Of note, pharmacological inhibition of retrograde transport in isolated islets and insulinoma cells mimicked the phenotype of Asna1(ß-/-) ß-cells and resulted in reduced insulin content and ER stress. These data support a model where Asna1 ensures retrograde transport and, hence, ER and insulin homeostasis in ß-cells.
[Mh] Termos MeSH primário: ATPases Transportadoras de Arsenito/genética
Glicemia/metabolismo
Diabetes Mellitus Tipo 2/genética
Retículo Endoplasmático/metabolismo
Endossomos/metabolismo
Células Secretoras de Insulina/metabolismo
Insulina/secreção
Membranas Intracelulares/metabolismo
[Mh] Termos MeSH secundário: Animais
ATPases Transportadoras de Arsenito/metabolismo
Benzamidas/farmacologia
Western Blotting
Linhagem Celular Tumoral
Membrana Celular/efeitos dos fármacos
Membrana Celular/metabolismo
Diabetes Mellitus Tipo 2/metabolismo
Retículo Endoplasmático/efeitos dos fármacos
Estresse do Retículo Endoplasmático
Endossomos/efeitos dos fármacos
Intolerância à Glucose/genética
Intolerância à Glucose/metabolismo
Complexo de Golgi/efeitos dos fármacos
Complexo de Golgi/metabolismo
Homeostase/genética
Técnicas In Vitro
Insulina/sangue
Membranas Intracelulares/efeitos dos fármacos
Ilhotas Pancreáticas/metabolismo
Camundongos
Camundongos Knockout
Proteínas Qa-SNARE/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Tiofenos/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (2-(((5-methyl-2-thienyl)methylene)amino)-N-phenylbenzamide); 0 (Benzamides); 0 (Blood Glucose); 0 (Insulin); 0 (Qa-SNARE Proteins); 0 (Thiophenes); EC 3.6.3.16 (Arsenite Transporting ATPases); EC 3.6.3.16 (Asna1 protein, mouse)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:151223
[Lr] Data última revisão:
151223
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:151007
[St] Status:MEDLINE
[do] DOI:10.2337/db15-0699


  8 / 214 MEDLINE  
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[PMID]:26627908
[Au] Autor:Buentzel J; Vilardi F; Lotz-Havla A; Gärtner J; Thoms S
[Ad] Endereço:University Medical Center, Department of Child and Adolescent Medicine, Robert Koch Str. 40, 37075 Göttingen, Germany.
[Ti] Título:Conserved targeting information in mammalian and fungal peroxisomal tail-anchored proteins.
[So] Source:Sci Rep;5:17420, 2015 Dec 02.
[Is] ISSN:2045-2322
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The targeting signals and mechanisms of soluble peroxisomal proteins are well understood, whereas less is known about the signals and targeting routes of peroxisomal membrane proteins (PMP). Pex15 and PEX26, tail-anchored proteins in yeast and mammals, respectively, exert a similar cellular function in the recruitment of AAA peroxins at the peroxisomal membrane. But despite their common role, Pex15 and PEX26 are neither homologs nor they are known to follow similar targeting principles. Here we show that Pex15 targets to peroxisomes in mammalian cells, and PEX26 reaches peroxisomes when expressed in yeast cells. In both proteins C-terminal targeting information is sufficient for correct sorting to the peroxisomal membrane. In yeast, PEX26 follows the pathway that also ensures correct targeting of Pex15: PEX26 enters the endoplasmic reticulum (ER) in a GET-dependent and Pex19-independent manner. Like in yeast, PEX26 enters the ER in mammalian cells, however, independently of GET/TRC40. These data show that conserved targeting information is employed in yeast and higher eukaryotes during the biogenesis of peroxisomal tail-anchored proteins.
[Mh] Termos MeSH primário: Proteínas de Membrana/metabolismo
Peroxissomos/metabolismo
Fosfoproteínas/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: ATPases Transportadoras de Arsenito/genética
ATPases Transportadoras de Arsenito/metabolismo
Células HeLa
Seres Humanos
Proteínas de Membrana/genética
Peroxissomos/genética
Fosfoproteínas/genética
Transporte Proteico/fisiologia
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (ASNA1 protein, human); 0 (Membrane Proteins); 0 (PEX15 protein, S cerevisiae); 0 (PEX26 protein, human); 0 (Phosphoproteins); 0 (Saccharomyces cerevisiae Proteins); EC 3.6.3.16 (Arsenite Transporting ATPases)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151203
[St] Status:MEDLINE
[do] DOI:10.1038/srep17420


  9 / 214 MEDLINE  
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[PMID]:26362251
[Au] Autor:Kun-Rodrigues C; Ganos C; Guerreiro R; Schneider SA; Schulte C; Lesage S; Darwent L; Holmans P; Singleton A; Bhatia K; Bras J; International Parkinson's Disease Genomics Consortium (IPDGC)
[Ad] Endereço:Department of Molecular Neuroscience, UCL Institute of Neurology, London WC1N 3AR, UK.
[Ti] Título:A systematic screening to identify de novo mutations causing sporadic early-onset Parkinson's disease.
[So] Source:Hum Mol Genet;24(23):6711-20, 2015 Dec 01.
[Is] ISSN:1460-2083
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Despite the many advances in our understanding of the genetic basis of Mendelian forms of Parkinson's disease (PD), a large number of early-onset cases still remain to be explained. Many of these cases, present with a form of disease that is identical to that underlined by genetic causes, but do not have mutations in any of the currently known disease-causing genes. Here, we hypothesized that de novo mutations may account for a proportion of these early-onset, sporadic cases. We performed exome sequencing in full parent-child trios where the proband presents with typical PD to unequivocally identify de novo mutations. This approach allows us to test all genes in the genome in an unbiased manner. We have identified and confirmed 20 coding de novo mutations in 21 trios. We have used publicly available population genetic data to compare variant frequencies and our independent in-house dataset of exome sequencing in PD (with over 1200 cases) to identify additional variants in the same genes. Of the genes identified to carry de novo mutations, PTEN, VAPB and ASNA1 are supported by various sources of data to be involved in PD. We show that these genes are reported to be within a protein-protein interaction network with PD genes and that they contain additional rare, case-specific, mutations in our independent cohort of PD cases. Our results support the involvement of these three genes in PD and suggest that testing for de novo mutations in sporadic disease may aid in the identification of novel disease-causing genes.
[Mh] Termos MeSH primário: Análise Mutacional de DNA
Predisposição Genética para Doença
Mutação
Doença de Parkinson/genética
Mapas de Interação de Proteínas
[Mh] Termos MeSH secundário: Adulto
ATPases Transportadoras de Arsenito/genética
Exoma
Seres Humanos
Masculino
Meia-Idade
PTEN Fosfo-Hidrolase/genética
Doença de Parkinson/metabolismo
Linhagem
Proteínas de Transporte Vesicular/genética
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (ASNA1 protein, human); 0 (VAPB protein, human); 0 (Vesicular Transport Proteins); EC 3.1.3.67 (PTEN Phosphohydrolase); EC 3.1.3.67 (PTEN protein, human); EC 3.6.3.16 (Arsenite Transporting ATPases)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150913
[St] Status:MEDLINE
[do] DOI:10.1093/hmg/ddv376


  10 / 214 MEDLINE  
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[PMID]:26132104
[Au] Autor:Sousa T; Branco R; Piedade AP; Morais PV
[Ad] Endereço:IMAR-CMA, Coimbra, Portugal.
[Ti] Título:Hyper Accumulation of Arsenic in Mutants of Ochrobactrum tritici Silenced for Arsenite Efflux Pumps.
[So] Source:PLoS One;10(7):e0131317, 2015.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ochrobactrum tritici SCII24T is a highly As-resistant bacterium, with two previously described arsenic resistance operons, ars1 and ars2. Among a large number of genes, these operons contain the arsB and Acr3 genes that encode the arsenite efflux pumps responsible for arsenic resistance. Exploring the genome of O. tritici SCII24T, an additional putative operon (ars3) was identified and revealed the presence of the Acr3_2 gene that encodes for an arsenite efflux protein but which came to prove to not be required for full As resistance. The genes encoding for arsenite efflux pumps, identified in this strain, were inactivated to develop microbial accumulators of arsenic as new tools for bioremediation. Six different mutants were produced, studied and three were more useful as biotools. O. tritici wild type and the Acr3-mutants showed the highest resistance to As(III), being able to grow up to 50 mM of arsenite. On the other hand, arsB-mutants were not able to grow at concentrations higher than 1 mM As(III), and were the most As(III) sensitive mutants. In the presence of 1 mM As(III), the strain with arsB and Acr3_1 mutated showed the highest intracellular arsenic concentration (up to 17 ng(As)/mg protein), while in assays with 5 mM As(III), the single arsB-mutant was able to accumulate the highest concentration of arsenic (up to 10 ng(As)/mg protein). Therefore, arsB is the main gene responsible for arsenite resistance in O. tritici. However, both genes arsB and Acr3_1 play a crucial role in the resistance mechanism, depending on the arsenite concentration in the medium. In conclusion, at moderate arsenite concentrations, the double arsB- and Acr3_1-mutant exhibited a great ability to accumulate arsenite and can be seen as a promising bioremediation tool for environmental arsenic detoxification.
[Mh] Termos MeSH primário: Arsênico/toxicidade
ATPases Transportadoras de Arsenito/genética
Proteínas de Bactérias/genética
Poluentes Ambientais/toxicidade
Regulação Bacteriana da Expressão Gênica
Mutação
Ochrobactrum/efeitos dos fármacos
[Mh] Termos MeSH secundário: ATPases Transportadoras de Arsenito/deficiência
Proteínas de Bactérias/metabolismo
Biodegradação Ambiental
Farmacorresistência Bacteriana/genética
Engenharia Genética
Transporte de Íons
Ochrobactrum/genética
Ochrobactrum/metabolismo
Óperon
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Environmental Pollutants); EC 3.6.3.16 (Arsenite Transporting ATPases); N712M78A8G (Arsenic)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:150719
[Lr] Data última revisão:
150719
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150702
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0131317



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