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  1 / 1353 MEDLINE  
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[PMID]:28977033
[Au] Autor:Zholobenko AV; Mouithys-Mickalad A; Dostal Z; Serteyn D; Modriansky M
[Ad] Endereço:Department of Medical Chemistry & Biochemistry, Faculty of Medicine and Dentistry, Palacky University, Olomouc, Czech Republic.
[Ti] Título:On the causes and consequences of the uncoupler-like effects of quercetin and dehydrosilybin in H9c2 cells.
[So] Source:PLoS One;12(10):e0185691, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Quercetin and dehydrosilybin are polyphenols which are known to behave like uncouplers of respiration in isolated mitochondria. Here we investigated whether the effect is conserved in whole cells. Following short term incubation, neither compound uncouples mitochondrial respiration in whole H9c2 cells below 50µM. However, following hypoxia, or long term incubation, leak (state IV with oligomycin) oxygen consumption is increased by quercetin. Both compounds partially protected complex I respiration, but not complex II in H9c2 cells following hypoxia. In a permeabilised H9c2 cell model, the increase in leak respiration caused by quercetin is lowered by increased [ADP] and is increased by adenine nucleotide transporter inhibitor, atractyloside, but not bongkrekic acid. Both quercetin and dehydrosilybin dissipate mitochondrial membrane potential in whole cells. In the case of quercetin, the effect is potentiated post hypoxia. Genetically encoded Ca++ sensors, targeted to the mitochondria, enabled the use of fluorescence microscopy to show that quercetin decreased mitochondrial [Ca++] while dehydrosilybin did not. Likewise, quercetin decreases accumulation of [Ca++] in mitochondria following hypoxia. Fluorescent probes were used to show that both compounds decrease plasma membrane potential and increase cytosolic [Ca++]. We conclude that the uncoupler-like effects of these polyphenols are attenuated in whole cells compared to isolated mitochondria, but downstream effects are nevertheless apparent. Results suggest that the effect of quercetin observed in whole and permeabilised cells may originate in the mitochondria, while the mechanism of action of cardioprotection by dehydrosilybin may be less dependent on mitochondrial uncoupling than originally thought. Rather, protective effects may originate due to interactions at the plasma membrane.
[Mh] Termos MeSH primário: Quercetina/farmacologia
Silimarina/farmacologia
[Mh] Termos MeSH secundário: Animais
Cálcio/metabolismo
Linhagem Celular
Digitonina/farmacologia
Potencial da Membrana Mitocondrial/efeitos dos fármacos
Microscopia Confocal
Microscopia de Fluorescência
Translocases Mitocondriais de ADP e ATP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Silymarin); 0 (dehydrosilybin); 9068-80-8 (Mitochondrial ADP, ATP Translocases); 9IKM0I5T1E (Quercetin); KOO5CM684H (Digitonin); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171005
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185691


  2 / 1353 MEDLINE  
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[PMID]:28947214
[Au] Autor:Dallabona C; Baruffini E; Goffrini P; Lodi T
[Ad] Endereço:Department of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, 43124 Parma, Italy.
[Ti] Título:Dominance of yeast aac2 and aac2 mutations, equivalent to pathological mutations in ant1, is due to gain of function.
[So] Source:Biochem Biophys Res Commun;493(2):909-913, 2017 Nov 18.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The mitochondrial ADP/ATP carrier is a nuclear encoded protein, which catalyzes the exchange of ATP generated in mitochondria with ADP produced in the cytosol. In humans, mutations in the major ADP/ATP carrier gene, ANT1, are involved in several degenerative mitochondrial pathologies, leading to instability of mitochondrial DNA. Recessive mutations have been associated with mitochondrial myopathy and cardiomyopathy whereas dominant mutations have been associated with autosomal dominant Progressive External Ophtalmoplegia (adPEO). Recently, two de novo dominant mutations, R80H and R235G, leading to extremely severe symptoms, have been identified. In order to evaluate if the dominance is due to haploinsufficiency or to a gain of function, the two mutations have been introduced in the equivalent positions of the AAC2 gene, the yeast orthologue of human ANT1, and their dominant effect has been studied in heteroallelic strains, containing both one copy of wild type AAC2 and one copy of mutant aac2 allele. Through phenotypic characterization of these yeast models we showed that the OXPHOS phenotypes in the heteroallelic strains were more affected than in the hemiallelic strain indicating that the dominant trait of the two mutations is due to gain of function.
[Mh] Termos MeSH primário: Translocador 1 do Nucleotídeo Adenina/genética
DNA Mitocondrial/genética
Translocases Mitocondriais de ADP e ATP/genética
Miopatias Mitocondriais/genética
Mutação Puntual
Proteínas de Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/genética
[Mh] Termos MeSH secundário: Alelos
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adenine Nucleotide Translocator 1); 0 (DNA, Mitochondrial); 0 (PET9 protein, S cerevisiae); 0 (SLC25A4 protein, human); 0 (Saccharomyces cerevisiae Proteins); 9068-80-8 (Mitochondrial ADP, ATP Translocases)
[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:170927
[St] Status:MEDLINE


  3 / 1353 MEDLINE  
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[PMID]:28727843
[Au] Autor:Tamura K; Hayashi S
[Ad] Endereço:Department of Chemistry, Graduate School of Science, Kyoto University, Kyoto, Japan.
[Ti] Título:Atomistic modeling of alternating access of a mitochondrial ADP/ATP membrane transporter with molecular simulations.
[So] Source:PLoS One;12(7):e0181489, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The mitochondrial ADP/ATP carrier (AAC) is a membrane transporter that exchanges a cytosolic ADP for a matrix ATP. Atomic structures in an outward-facing (OF) form which binds an ADP from the intermembrane space have been solved by X-ray crystallography, and revealed their unique pseudo three-fold symmetry fold which is qualitatively different from pseudo two-fold symmetry of most transporters of which atomic structures have been solved. However, any atomic-level information on an inward-facing (IF) form, which binds an ATP from the matrix side and is fixed by binding of an inhibitor, bongkrekic acid (BA), is not available, and thus its alternating access mechanism for the transport process is unknown. Here, we report an atomic structure of the IF form predicted by atomic-level molecular dynamics (MD) simulations of the alternating access transition with a recently developed accelerating technique. We successfully obtained a significantly stable IF structure characterized by newly formed well-packed and -organized inter-domain interactions through the accelerated simulations of unprecedentedly large conformational changes of the alternating access without a prior knowledge of the target protein structure. The simulation also shed light on an atomistic mechanism of the strict transport selectivity of adenosine nucleotides over guanosine and inosine ones. Furthermore, the IF structure was shown to bind ATP and BA, and thus revealed their binding mechanisms. The present study proposes a qualitatively novel view of the alternating access of transporters having the unique three-fold symmetry in atomic details and opens the way for rational drug design targeting the transporter in the dynamic functional cycle.
[Mh] Termos MeSH primário: Translocases Mitocondriais de ADP e ATP/metabolismo
Simulação de Dinâmica Molecular
[Mh] Termos MeSH secundário: Difosfato de Adenosina/química
Trifosfato de Adenosina/metabolismo
Ácido Bongcréquico/química
Translocases Mitocondriais de ADP e ATP/química
Ligação Proteica
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; VIDEO-AUDIO MEDIA
[Nm] Nome de substância:
11076-19-0 (Bongkrekic Acid); 61D2G4IYVH (Adenosine Diphosphate); 8L70Q75FXE (Adenosine Triphosphate); 9068-80-8 (Mitochondrial ADP, ATP Translocases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170721
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0181489


  4 / 1353 MEDLINE  
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[PMID]:28504211
[Au] Autor:Cardouat G; Duparc T; Fried S; Perret B; Najib S; Martinez LO
[Ad] Endereço:Institute of Metabolic and Cardiovascular diseases, I2MC, Inserm, Université de Toulouse, UMR 1048, Toulouse 31000, France.
[Ti] Título:Ectopic adenine nucleotide translocase activity controls extracellular ADP levels and regulates the F -ATPase-mediated HDL endocytosis pathway on hepatocytes.
[So] Source:Biochim Biophys Acta;1862(9):832-841, 2017 09.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Ecto-F -ATPase is a complex related to mitochondrial ATP synthase which has been identified as a plasma membrane receptor for apolipoprotein A-I (apoA-I), the major protein of high-density lipoprotein (HDL), and has been shown to contribute to HDL endocytosis in several cell types. On hepatocytes, apoA-I binding to ecto-F -ATPase stimulates extracellular ATP hydrolysis into ADP, which subsequently activates a P2Y -mediated HDL endocytosis pathway. Interestingly, other mitochondrial proteins have been found to be expressed at the plasma membrane of several cell types. Among these, adenine nucleotide translocase (ANT) is an ADP/ATP carrier but its role in controlling extracellular ADP levels and F -ATPase-mediated HDL endocytosis has never been investigated. Here we confirmed the presence of ANT at the plasma membrane of human hepatocytes. We then showed that ecto-ANT activity increases or reduces extracellular ADP level, depending on the extracellular ADP/ATP ratio. Interestingly, ecto-ANT co-localized with ecto-F -ATPase at the hepatocyte plasma membrane and pharmacological inhibition of ecto-ANT activity increased extracellular ADP level when ecto-F -ATPase was activated by apoA-I. This increase in the bioavailability of extracellular ADP accordingly translated into an increase of HDL endocytosis on human hepatocytes. This study thus uncovered a new location and function of ANT for which activity at the cell surface of hepatocytes modulates the concentration of extracellular ADP and regulates HDL endocytosis.
[Mh] Termos MeSH primário: Difosfato de Adenosina/metabolismo
Trifosfato de Adenosina/metabolismo
Endocitose/fisiologia
Hepatócitos/metabolismo
Lipoproteínas HDL/metabolismo
Translocases Mitocondriais de ADP e ATP/metabolismo
ATPases Translocadoras de Prótons/metabolismo
[Mh] Termos MeSH secundário: Apolipoproteína A-I/metabolismo
Linhagem Celular
Linhagem Celular Tumoral
Membrana Celular/metabolismo
Células Hep G2
Seres Humanos
Proteínas Mitocondriais/metabolismo
Transdução de Sinais/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apolipoprotein A-I); 0 (Lipoproteins, HDL); 0 (Mitochondrial Proteins); 61D2G4IYVH (Adenosine Diphosphate); 8L70Q75FXE (Adenosine Triphosphate); 9068-80-8 (Mitochondrial ADP, ATP Translocases); EC 3.6.3.14 (Proton-Translocating ATPases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170516
[St] Status:MEDLINE


  5 / 1353 MEDLINE  
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[PMID]:28404750
[Au] Autor:Lu YW; Acoba MG; Selvaraju K; Huang TC; Nirujogi RS; Sathe G; Pandey A; Claypool SM
[Ad] Endereço:Department of Physiology, Johns Hopkins University School of Medicine, Baltimore, MD 21205-2185.
[Ti] Título:Human adenine nucleotide translocases physically and functionally interact with respirasomes.
[So] Source:Mol Biol Cell;28(11):1489-1506, 2017 Jun 01.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Members of the adenine nucleotide translocase (ANT) family exchange ADP for ATP across the mitochondrial inner membrane, an activity that is essential for oxidative phosphorylation (OXPHOS). Mutations in or dysregulation of ANTs is associated with progressive external ophthalmoplegia, cardiomyopathy, nonsyndromic intellectual disability, apoptosis, and the Warburg effect. Binding partners of human ANTs have not been systematically identified. The absence of such information has prevented a detailed molecular understanding of the assorted ANT-associated diseases, including insight into their disparate phenotypic manifestations. To fill this void, in this study, we define the interactomes of two human ANT isoforms. Analogous to its yeast counterpart, human ANTs associate with heterologous partner proteins, including the respiratory supercomplex (RSC) and other solute carriers. The evolutionarily conserved ANT-RSC association is particularly noteworthy because the composition, and thereby organization, of RSCs in yeast and human is different. Surprisingly, absence of the major ANT isoform only modestly impairs OXPHOS in HEK293 cells, indicating that the low levels of other isoforms provide functional redundancy. In contrast, pharmacological inhibition of OXPHOS expression and function inhibits ANT-dependent ADP/ATP exchange. Thus ANTs and the OXPHOS machinery physically interact and functionally cooperate to enhance ANT transport capacity and mitochondrial respiration.
[Mh] Termos MeSH primário: Translocases Mitocondriais de ADP e ATP/genética
Translocases Mitocondriais de ADP e ATP/metabolismo
[Mh] Termos MeSH secundário: Difosfato de Adenosina/metabolismo
Trifosfato de Adenosina/metabolismo
Apoptose
Células HEK293
Células HeLa
Seres Humanos
Mitocôndrias/metabolismo
Membranas Mitocondriais/metabolismo
Fosforilação Oxidativa
Isoformas de Proteínas/metabolismo
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protein Isoforms); 61D2G4IYVH (Adenosine Diphosphate); 8L70Q75FXE (Adenosine Triphosphate); 9068-80-8 (Mitochondrial ADP, ATP Translocases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170414
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E17-03-0195


  6 / 1353 MEDLINE  
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[PMID]:28360103
[Au] Autor:Ludtmann MHR; Arber C; Bartolome F; de Vicente M; Preza E; Carro E; Houlden H; Gandhi S; Wray S; Abramov AY
[Ad] Endereço:From the Department of Molecular Neuroscience, UCL Institute of Neurology, London WC1N 3BG, United Kingdom.
[Ti] Título:Mutations in valosin-containing protein (VCP) decrease ADP/ATP translocation across the mitochondrial membrane and impair energy metabolism in human neurons.
[So] Source:J Biol Chem;292(21):8907-8917, 2017 May 26.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mutations in the gene encoding valosin-containing protein (VCP) lead to multisystem proteinopathies including frontotemporal dementia. We have previously shown that patient-derived mutant fibroblasts exhibit lower mitochondrial membrane potential, uncoupled respiration, and reduced ATP levels. This study addresses the underlying basis for mitochondrial uncoupling using knockdown neuroblastoma cell lines, induced pluripotent stem cells (iPSCs), and iPSC-derived cortical neurons from patients with pathogenic mutations in Using fluorescent live cell imaging and respiration analysis we demonstrate a mutation/knockdown-induced dysregulation in the adenine nucleotide translocase, which results in a slower rate of ADP or ATP translocation across the mitochondrial membranes. This deregulation can explain the mitochondrial uncoupling and lower ATP levels in VCP mutation-bearing neurons via reduced ADP availability for ATP synthesis. This study provides evidence for a role of adenine nucleotide translocase in the mechanism underlying altered mitochondrial function in VCP-related degeneration, and this new insight may inform efforts to better understand and manage neurodegenerative disease and other proteinopathies.
[Mh] Termos MeSH primário: Difosfato de Adenosina/metabolismo
Adenosina Trifosfatases
Trifosfato de Adenosina/metabolismo
Proteínas de Ciclo Celular
Membranas Mitocondriais/metabolismo
Mutação
Neurônios/metabolismo
[Mh] Termos MeSH secundário: Difosfato de Adenosina/genética
Adenosina Trifosfatases/genética
Adenosina Trifosfatases/metabolismo
Trifosfato de Adenosina/genética
Transporte Biológico Ativo/fisiologia
Proteínas de Ciclo Celular/genética
Proteínas de Ciclo Celular/metabolismo
Linhagem Celular Tumoral
Seres Humanos
Células-Tronco Pluripotentes Induzidas/metabolismo
Células-Tronco Pluripotentes Induzidas/patologia
Translocases Mitocondriais de ADP e ATP/genética
Translocases Mitocondriais de ADP e ATP/metabolismo
Doenças Neurodegenerativas/genética
Doenças Neurodegenerativas/metabolismo
Neurônios/patologia
Deficiências na Proteostase/genética
Deficiências na Proteostase/metabolismo
Proteína com Valosina
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Cycle Proteins); 61D2G4IYVH (Adenosine Diphosphate); 8L70Q75FXE (Adenosine Triphosphate); 9068-80-8 (Mitochondrial ADP, ATP Translocases); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.4.6 (VCP protein, human); EC 3.6.4.6 (Valosin Containing Protein)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170401
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.762898


  7 / 1353 MEDLINE  
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[PMID]:27592226
[Au] Autor:Zhang J; Li M; Zhang Z; Zhu R; Olcese R; Stefani E; Toro L
[Ad] Endereço:Department of Anesthesiology, Division of Molecular Medicine, University of California, Los Angeles, Los Angeles, CA, USA; Department of Molecular & Medical Pharmacology, University of California, Los Angeles, Los Angeles, CA, USA.
[Ti] Título:The mitochondrial BK channel cardiac interactome reveals BK association with the mitochondrial import receptor subunit Tom22, and the adenine nucleotide translocator.
[So] Source:Mitochondrion;33:84-101, 2017 Mar.
[Is] ISSN:1872-8278
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Mitochondrial BK channel, mitoBK , regulates mitochondria function in the heart but information on its protein partnerships in cardiac mitochondria is missing. A directed proteomic approach discovered the novel interaction of BK with Tom22, a component of the mitochondrion outer membrane import system, and the adenine nucleotide translocator (ANT). The expressed protein partners co-immunoprecipitated and co-segregated into mitochondrial fractions in HEK293T cells. The BK 50 amino acid splice insert, DEC, facilitated BK interaction with ANT. Further, BK transmembrane domain was required for the association with both Tom22 and ANT. The results serve as a working framework to understand mitoBK import and functional relationships.
[Mh] Termos MeSH primário: Canais de Potássio Ativados por Cálcio de Condutância Alta/metabolismo
Translocases Mitocondriais de ADP e ATP/metabolismo
Proteínas de Transporte da Membrana Mitocondrial/metabolismo
Proteínas Mitocondriais/metabolismo
Miocárdio/enzimologia
[Mh] Termos MeSH secundário: Animais
Células HEK293
Seres Humanos
Imunoprecipitação
Masculino
Ligação Proteica
Mapas de Interação de Proteínas
Proteômica
Ratos Sprague-Dawley
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Large-Conductance Calcium-Activated Potassium Channels); 0 (Mitochondrial Membrane Transport Proteins); 0 (Mitochondrial Proteins); 0 (Tom22 protein, human); 9068-80-8 (Mitochondrial ADP, ATP Translocases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170509
[Lr] Data última revisão:
170509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160905
[St] Status:MEDLINE


  8 / 1353 MEDLINE  
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[PMID]:27786441
[Au] Autor:Hedger G; Rouse SL; Domanski J; Chavent M; Koldsø H; Sansom MS
[Ad] Endereço:Department of Biochemistry, University of Oxford , South Parks Road, Oxford OX1 3QU, U.K.
[Ti] Título:Lipid-Loving ANTs: Molecular Simulations of Cardiolipin Interactions and the Organization of the Adenine Nucleotide Translocase in Model Mitochondrial Membranes.
[So] Source:Biochemistry;55(45):6238-6249, 2016 Nov 15.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The exchange of ADP and ATP across the inner mitochondrial membrane is a fundamental cellular process. This exchange is facilitated by the adenine nucleotide translocase, the structure and function of which are critically dependent on the signature phospholipid of mitochondria, cardiolipin (CL). Here we employ multiscale molecular dynamics simulations to investigate CL interactions within a membrane environment. Using simulations at both coarse-grained and atomistic resolutions, we identify three CL binding sites on the translocase, in agreement with those seen in crystal structures and inferred from nuclear magnetic resonance measurements. Characterization of the free energy landscape for lateral lipid interaction via potential of mean force calculations demonstrates the strength of interaction compared to those of binding sites on other mitochondrial membrane proteins, as well as their selectivity for CL over other phospholipids. Extending the analysis to other members of the family, yeast Aac2p and mouse uncoupling protein 2, suggests a degree of conservation. Simulation of large patches of a model mitochondrial membrane containing multiple copies of the translocase shows that CL interactions persist in the presence of protein-protein interactions and suggests CL may mediate interactions between translocases. This study provides a key example of how computational microscopy may be used to shed light on regulatory lipid-protein interactions.
[Mh] Termos MeSH primário: Translocador 1 do Nucleotídeo Adenina/metabolismo
Cardiolipinas/metabolismo
Membranas Mitocondriais/metabolismo
Simulação de Dinâmica Molecular
[Mh] Termos MeSH secundário: Translocador 1 do Nucleotídeo Adenina/química
Animais
Sítios de Ligação
Cardiolipinas/química
Bovinos
Cristalografia por Raios X
Espectroscopia de Ressonância Magnética
Camundongos
Translocases Mitocondriais de ADP e ATP/química
Translocases Mitocondriais de ADP e ATP/metabolismo
Ligação Proteica
Domínios Proteicos
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/metabolismo
Termodinâmica
Proteína Desacopladora 2/química
Proteína Desacopladora 2/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adenine Nucleotide Translocator 1); 0 (Cardiolipins); 0 (PET9 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (Uncoupling Protein 2); 9068-80-8 (Mitochondrial ADP, ATP Translocases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170522
[Lr] Data última revisão:
170522
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161028
[St] Status:MEDLINE


  9 / 1353 MEDLINE  
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[PMID]:27479487
[Au] Autor:Curcio R; Muto L; Pierri CL; Montalto A; Lauria G; Onofrio A; Fiorillo M; Fiermonte G; Lunetti P; Vozza A; Capobianco L; Cappello AR; Dolce V
[Ad] Endereço:Department of Pharmacy, Health and Nutritional Sciences, University of Calabria, 87036 Arcavacata di Rende, Cosenza, Italy.
[Ti] Título:New insights about the structural rearrangements required for substrate translocation in the bovine mitochondrial oxoglutarate carrier.
[So] Source:Biochim Biophys Acta;1864(11):1473-80, 2016 11.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The oxoglutarate carrier (OGC) belongs to the mitochondrial carrier family and plays a key role in important metabolic pathways. Here, site-directed mutagenesis was used to conservatively replace lysine 122 by arginine, in order to investigate new structural rearrangements required for substrate translocation. K122R mutant was kinetically characterized, exhibiting a significant Vmax reduction with respect to the wild-type (WT) OGC, whereas Km value was unaffected, implying that this substitution does not interfere with 2-oxoglutarate binding site. Moreover, K122R mutant was more inhibited by several sulfhydryl reagents with respect to the WT OGC, suggesting that the reactivity of some cysteine residues towards these Cys-specific reagents is increased in this mutant. Different sulfhydryl reagents were employed in transport assays to test the effect of the cysteine modifications on single-cysteine OGC mutants named C184, C221, C224 (constructed in the WT background) and K122R/C184, K122R/C221, K122R/C224 (constructed in the K122R background). Cysteines 221 and 224 were more deeply influenced by some sulfhydryl reagents in the K122R background. Furthermore, the presence of 2-oxoglutarate significantly enhanced the degree of inhibition of K122R/C221, K122R/C224 and C224 activity by the sulfhydryl reagent 2-Aminoethyl methanethiosulfonate hydrobromide (MTSEA), suggesting that cysteines 221 and 224, together with K122, take part to structural rearrangements required for the transition from the c- to the m-state during substrate translocation. Our results are interpreted in the light of the homology model of BtOGC, built by using as a template the X-ray structure of the bovine ADP/ATP carrier isoform 1 (AAC1).
[Mh] Termos MeSH primário: Cisteína/química
Ácidos Cetoglutáricos/química
Proteínas de Membrana Transportadoras/química
Mitocôndrias/química
Translocases Mitocondriais de ADP e ATP/química
[Mh] Termos MeSH secundário: Animais
Arginina/química
Arginina/metabolismo
Sítios de Ligação
Bovinos
Cisteína/metabolismo
Metanossulfonato de Etila/análogos & derivados
Metanossulfonato de Etila/química
Expressão Gênica
Ácidos Cetoglutáricos/metabolismo
Cinética
Lisina/química
Lisina/metabolismo
Proteínas de Membrana Transportadoras/genética
Proteínas de Membrana Transportadoras/metabolismo
Mitocôndrias/metabolismo
Translocases Mitocondriais de ADP e ATP/genética
Translocases Mitocondriais de ADP e ATP/metabolismo
Simulação de Acoplamento Molecular
Mutagênese Sítio-Dirigida
Ligação Proteica
Domínios Proteicos
Estrutura Secundária de Proteína
Homologia Estrutural de Proteína
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Ketoglutaric Acids); 0 (Membrane Transport Proteins); 0 (methanethiosulfonate ethylammonium); 0 (oxoglutarate translocator); 8ID597Z82X (alpha-ketoglutaric acid); 9068-80-8 (Mitochondrial ADP, ATP Translocases); 94ZLA3W45F (Arginine); 9H154DI0UP (Ethyl Methanesulfonate); K3Z4F929H6 (Lysine); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170602
[Lr] Data última revisão:
170602
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160802
[St] Status:MEDLINE


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[PMID]:27348811
[Au] Autor:Nakazawa M; Matsubara H; Matsushita Y; Watanabe M; Vo N; Yoshida H; Yamaguchi M; Kataoka T
[Ad] Endereço:Department of Applied Biology, Kyoto Institute of Technology, Matsugasaki, Sakyo-ku, Kyoto 606-8585, Japan.
[Ti] Título:The Human Bcl-2 Family Member Bcl-rambo Localizes to Mitochondria and Induces Apoptosis and Morphological Aberrations in Drosophila.
[So] Source:PLoS One;11(6):e0157823, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bcl-2 family proteins play a central role in regulating apoptosis. We previously reported that human Bcl-rambo, also termed BCL2L13, localized to mitochondria and induced apoptosis when overexpressed in human embryonic kidney 293T cells. However, the physiological function of Bcl-rambo currently remains unclear. In the present study, human Bcl-rambo was ectopically expressed in Drosophila melanogaster. Bcl-rambo mainly localized to the mitochondria of Drosophila Schneider 2 (S2) cells. The overexpression of Bcl-rambo, but not Bcl-rambo lacking a C-terminal transmembrane domain, induced apoptosis in S2 cells. Moreover, the ectopic expression of Bcl-rambo by a GAL4-UAS system induced aberrant morphological changes characterized by atrophied wing, split thorax, and rough eye phenotypes. Bcl-rambo induced the activation of effector caspases in eye imaginal discs. The rough eye phenotype induced by Bcl-rambo was partly rescued by the co-expression of p35, Diap1, and Diap2. By using this Drosophila model, we showed that human Bcl-rambo interacted genetically with Drosophila homologues of adenine nucleotide translocators and the autophagy-related 8 protein. The results of the present study demonstrated that human Bcl-rambo localized to mitochondria and at least regulated an apoptosis signaling pathway in Drosophila.
[Mh] Termos MeSH primário: Apoptose
Drosophila melanogaster/genética
Mitocôndrias/metabolismo
Fenótipo
Proteínas Proto-Oncogênicas c-bcl-2/genética
[Mh] Termos MeSH secundário: Animais
Família da Proteína 8 Relacionada à Autofagia/genética
Linhagem Celular
Proteínas de Drosophila/genética
Proteínas de Drosophila/metabolismo
Drosophila melanogaster/crescimento & desenvolvimento
Drosophila melanogaster/metabolismo
Epistasia Genética
Seres Humanos
Proteínas Inibidoras de Apoptose/genética
Proteínas Inibidoras de Apoptose/metabolismo
Translocases Mitocondriais de ADP e ATP/genética
Transporte Proteico
Proteínas Proto-Oncogênicas c-bcl-2/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Autophagy-Related Protein 8 Family); 0 (BCL2L13 protein, human); 0 (DIAP2 protein, Drosophila); 0 (Drosophila Proteins); 0 (Inhibitor of Apoptosis Proteins); 0 (Proto-Oncogene Proteins c-bcl-2); 0 (thread protein, Drosophila); 9068-80-8 (Mitochondrial ADP, ATP Translocases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170724
[Lr] Data última revisão:
170724
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160628
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0157823



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