Base de dados : MEDLINE
Pesquisa : D08.811.913.696.650.550.200.500 [Categoria DeCS]
Referências encontradas : 19 [refinar]
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  1 / 19 MEDLINE  
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[PMID]:26426123
[Au] Autor:Fujita Y; Fujiwara K; Zenitani S; Yamashita T
[Ad] Endereço:Department of Molecular Neuroscience, Graduate School of Medicine, Osaka University, 2-2 Yamadaoka, Suita, Osaka, Japan; Core Research for Evolutional Science and Technology, Japan Science and Technology Agency, 5, Sanbancho, Chiyoda-ku, Tokyo, Japan.
[Ti] Título:Acetylation of NDPK-D Regulates Its Subcellular Localization and Cell Survival.
[So] Source:PLoS One;10(10):e0139616, 2015.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nucleoside diphosphate kinases (NDPK) are ubiquitous enzymes that catalyze the reversible phosphotransfer of γ-phosphates between di- and triphosphonucleosides. NDPK-D (Nm23-H4) is the only member of the NDPK family with a mitochondrial targeting sequence. Despite the high expression of NDPK-D in the developing central nervous system, its function remains to be determined. In this study, we show that NDPK-D knockdown induces apoptosis in neuroblastoma cells as well as in mouse cortex, suggesting that NDPK-D is required for neuronal survival. We identified NDPK-D as a binding partner of NAD+-dependent histone deacetylase, SIRT1, by yeast two-hybrid screening. NDPK-D co-localized with SIRT1, and the association of these molecules was confirmed by co-immunoprecipitation. Inhibition of SIRT1 increases the acetylation of NDPK-D. Overexpression of NDPK-D along with SIRT1, or mutation in the acetylated lysine residues in NDPK-D, increases its nuclear accumulation. Furthermore, the NDPK-D acetylation-mimic mutant increased apoptosis in N1E-115 cells. Our data demonstrate that acetylation regulates the shuttling of NDPK-D between nucleus and cytoplasm, and increased acetylation of NDPK-D causes apoptosis.
[Mh] Termos MeSH primário: Apoptose
Encéfalo/metabolismo
Núcleo Celular/metabolismo
Mitocôndrias/metabolismo
Neuroblastoma/metabolismo
Neuroblastoma/patologia
Nucleosídeo Difosfato Quinase D/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Animais
Western Blotting
Encéfalo/citologia
Proliferação Celular
Células Cultivadas
Eletroporação
Feminino
Imunofluorescência
Células HEK293
Seres Humanos
Técnicas Imunoenzimáticas
Imunoprecipitação
Hibridização In Situ
Camundongos
Camundongos Endogâmicos C57BL
Neuroblastoma/genética
Nucleosídeo Difosfato Quinase D/genética
RNA Mensageiro/genética
Reação em Cadeia da Polimerase em Tempo Real
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Sirtuína 1/genética
Sirtuína 1/metabolismo
Frações Subcelulares
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (RNA, Messenger); EC 2.7.4.6 (Nucleoside Diphosphate Kinase D); EC 3.5.1.- (SIRT1 protein, human); EC 3.5.1.- (Sirtuin 1)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151002
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0139616


  2 / 19 MEDLINE  
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[PMID]:25231795
[Au] Autor:Schlattner U; Tokarska-Schlattner M; Epand RM; Boissan M; Lacombe ML; Klein-Seetharaman J; Kagan VE
[Ad] Endereço:Laboratory of Fundamental and Applied Bioenergetics (LBFA) and SFR Environmental and Systems Biology (BEeSy), University Grenoble Alpes, Grenoble, France, uwe.schlattner@ujf-grenoble.fr.
[Ti] Título:Mitochondrial NM23-H4/NDPK-D: a bifunctional nanoswitch for bioenergetics and lipid signaling.
[So] Source:Naunyn Schmiedebergs Arch Pharmacol;388(2):271-8, 2015 Feb.
[Is] ISSN:1432-1912
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:A novel paradigm for the function of the mitochondrial nucleoside diphosphate kinase NM23-H4/NDPK-D is proposed: acting as a bifunctional nanoswitch in bioenergetics and cardiolipin (CL) trafficking and signaling. Similar to some other mitochondrial proteins like cytochrome c or AIF, NM23-H4 seems to have dual functions in bioenergetics and apoptotic signaling. In its bioenergetic phosphotransfer mode, the kinase reversibly phosphorylates NDPs into NTPs, driven by mitochondrially generated ATP. Among others, this reaction can locally supply GTP to mitochondrial GTPases as shown for the dynamin-like GTPase OPA1, found in a complex together with NM23-H4. Further, NM23-H4 is functionally coupled to adenylate translocase (ANT) of the mitochondrial inner membrane (MIM), so generated ADP can stimulate respiration to rapidly regenerate ATP. The lipid transfer mode of NM23-H4 can support, dependent on the presence of CL, the transfer of anionic lipids between membranes in vitro and the sorting of CL from its mitochondrial sites of synthesis (MIM) to the mitochondrial outer membrane (MOM) in vivo. Such (partial) collapse of MIM/MOM CL asymmetry results in CL externalization on the mitochondrial surface, where CL can serve as pro-apoptotic or pro-mitophagic "eat me"-signal. The functional state of NM23-H4 depends on its degree of CL-membrane interaction. In vitro assays have shown that only NM23-H4 that fully cross-links two membranes is lipid transfer competent, but at the same time phosphotransfer (kinase) inactive. Thus, the two functions of NM23-H4 seem to be mutually exclusive. This novel mitochondrial regulatory circuit has potential for the development of interventions in various human pathologies.
[Mh] Termos MeSH primário: Metabolismo dos Lipídeos
Nucleosídeo Difosfato Quinase D/metabolismo
[Mh] Termos MeSH secundário: Apoptose
Cardiolipinas/metabolismo
Metabolismo Energético
Seres Humanos
Mitocôndrias/metabolismo
Nucleosídeo Difosfato Quinase D/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cardiolipins); EC 2.7.4.6 (Nucleoside Diphosphate Kinase D)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:170920
[Lr] Data última revisão:
170920
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140919
[St] Status:MEDLINE
[do] DOI:10.1007/s00210-014-1047-4


  3 / 19 MEDLINE  
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[PMID]:25233933
[Au] Autor:Lu YC; Chang JT; Liao CT; Kang CJ; Huang SF; Chen IH; Huang CC; Huang YC; Chen WH; Tsai CY; Wang HM; Yen TC; You GR; Chiang CH; Cheng AJ
[Ti] Título:OncomiR-196 promotes an invasive phenotype in oral cancer through the NME4-JNK-TIMP1-MMP signaling pathway.
[So] Source:Mol Cancer;13:218, 2014 Sep 19.
[Is] ISSN:1476-4598
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: MicroRNA-196 (miR-196), which is highly up-regulated in oral cancer cells, has been reported to be aberrantly expressed in several cancers; however, the significance of miR-196 in oral cancer has not yet been addressed. METHODS: Cellular functions in response to miR-196 modulation were examined, including cell growth, migration, invasion and radio/chemosensitivity. Algorithm-based studies were used to identify the regulatory target of miR-196. The miR-196 target gene and downstream molecular mechanisms were confirmed by RT-qPCR, western blot, luciferase reporter and confocal microscopy analyses. miR-196 expression was determined in paired cancer and adjacent normal tissues from oral cancer patients. RESULTS: Both miR-196a and miR-196b were highly over-expressed in the cancer tissue and correlated with lymph node metastasis (P = 0.001 and P = 0.006, respectively). Functionally, miR-196 actively promoted cell migration and invasion without affecting cell growth. Mechanistically, miR-196 performed it's their function by inhibiting NME4 expression and further activating p-JNK, suppressing TIMP1, and augmenting MMP1/9. CONCLUSION: miR-196 contributes to oral cancer by promoting cell migration and invasion. Clinically, miR-196a/b was significantly over-expressed in the cancer tissues and correlated with lymph node metastasis. Thus, our findings provide new knowledge of the underlying mechanism of cancer metastasis. miR-196 may serve as a promising marker for better oral cancer management.
[Mh] Termos MeSH primário: Proteínas Quinases JNK Ativadas por Mitógeno/metabolismo
Metaloproteinases da Matriz/metabolismo
MicroRNAs/metabolismo
Neoplasias Bucais/genética
Neoplasias Bucais/patologia
Nucleosídeo Difosfato Quinase D/metabolismo
Inibidor Tecidual de Metaloproteinase-1/metabolismo
[Mh] Termos MeSH secundário: Adulto
Idoso
Sequência de Bases
Linhagem Celular Tumoral
Movimento Celular/genética
Proliferação Celular
Feminino
Seres Humanos
Masculino
MicroRNAs/genética
Meia-Idade
Dados de Sequência Molecular
Neoplasias Bucais/enzimologia
Invasividade Neoplásica
Estadiamento de Neoplasias
Fenótipo
Transdução de Sinais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (MIRN196 microRNA, human); 0 (MicroRNAs); 0 (TIMP1 protein, human); 0 (Tissue Inhibitor of Metalloproteinase-1); EC 2.7.11.24 (JNK Mitogen-Activated Protein Kinases); EC 2.7.4.6 (NME4 protein, human); EC 2.7.4.6 (Nucleoside Diphosphate Kinase D); EC 3.4.24.- (Matrix Metalloproteinases)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140920
[St] Status:MEDLINE
[do] DOI:10.1186/1476-4598-13-218


  4 / 19 MEDLINE  
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[PMID]:25010650
[Au] Autor:Francois-Moutal L; Marcillat O; Granjon T
[Ad] Endereço:Université de Lyon, Université Lyon 1, CNRS, UMR 5246 ICBMS, Institut de Chimie et Biochimie Moléculaires et Supramoléculaires, IMBL, 43 Bd du 11 Novembre 1918, F-69622 Villeurbanne cedex, France.
[Ti] Título:Structural comparison of highly similar nucleoside-diphosphate kinases: Molecular explanation of distinct membrane-binding behavior.
[So] Source:Biochimie;105:110-8, 2014 Oct.
[Is] ISSN:1638-6183
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:NDPK-A, NDPK-B and NDPK-D are three enzymes which belong to the NDPK group I isoforms and are not only involved in metabolism process but also in transcriptional regulation, DNA cleavage, histidine protein kinase activity and metastasis development. Those enzymes were reported to bind to membranes either in mitochondria where NDPK-D influences cardiolipin lateral organization and is thought to be involved in apoptotic pathway or in cytosol where NDPK-A and NDPK-B membrane association was shown to influence several cellular processes like endocytosis, cellular adhesion, ion transport, etc. However, despite numerous studies, the role of NDPK-membrane association and the molecular details of the binding process are still elusive. In the present work, a comparative study of the three NDPK isoforms allowed us to show that although membrane binding is a common feature of these enzymes, mechanisms differ at the molecular scale. NDPK-A was not able to bind to model membranes mimicking the inner leaflet of plasma membrane, suggesting that its in vivo membrane association is mediated by a non-lipidic partner or other partners than the studied phospholipids. On the contrary, NDPK-B and NDPK-D were shown to bind efficiently to liposomes mimicking plasma membrane and mitochondrial inner membrane respectively but details of the binding mechanism differ between the two enzymes as NDPK-B binding necessarily involved an anionic phospholipid partner while NDPK-D can bind either zwitterionic or anionic phospholipids. Although sharing similar secondary structure and homohexameric quaternary arrangement, tryptophan fluorescence revealed fine disparities in NDPK tertiary structures. Interfacial behavior as well as ANS fluorescence showed further dissimilarities between NDPK isoforms, notably the presence of distinct accessible hydrophobic areas as well as different capacity to form Gibbs monolayers related to their surface activity properties. Those distinct features may contribute to explain the differences in the protein behavior towards membrane binding.
[Mh] Termos MeSH primário: Proteínas de Membrana/química
Nucleosídeo NM23 Difosfato Quinases/química
Nucleosídeo Difosfato Quinase D/química
[Mh] Termos MeSH secundário: Membrana Celular/enzimologia
Regulação Enzimológica da Expressão Gênica
Seres Humanos
Lipossomos/metabolismo
Proteínas de Membrana/biossíntese
Proteínas de Membrana/genética
Membranas Mitocondriais/enzimologia
Nucleosídeo NM23 Difosfato Quinases/biossíntese
Nucleosídeo NM23 Difosfato Quinases/genética
Nucleosídeo Difosfato Quinase D/biossíntese
Nucleosídeo Difosfato Quinase D/genética
Núcleosídeo-Difosfato Quinase/biossíntese
Núcleosídeo-Difosfato Quinase/química
Núcleosídeo-Difosfato Quinase/genética
Fosforilação
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Liposomes); 0 (Membrane Proteins); 0 (NM23 Nucleoside Diphosphate Kinases); EC 2.7.4.6 (NME1 protein, human); EC 2.7.4.6 (NME4 protein, human); EC 2.7.4.6 (Nucleoside Diphosphate Kinase D); EC 2.7.4.6 (Nucleoside-Diphosphate Kinase); EC 2.7.4.6. (NDPK-B protein, human)
[Em] Mês de entrada:1505
[Cu] Atualização por classe:140913
[Lr] Data última revisão:
140913
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140711
[St] Status:MEDLINE


  5 / 19 MEDLINE  
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[PMID]:24970086
[Au] Autor:Boissan M; Montagnac G; Shen Q; Griparic L; Guitton J; Romao M; Sauvonnet N; Lagache T; Lascu I; Raposo G; Desbourdes C; Schlattner U; Lacombe ML; Polo S; van der Bliek AM; Roux A; Chavrier P
[Ad] Endereço:Institut Curie, Research Center, Paris, France. Membrane and Cytoskeleton Dynamics, CNRS UMR 144, Paris, France. Université Pierre et Marie Curie, University Paris 06, Paris, France. Saint-Antoine Research Center, INSERM UMR-S 938, Paris, France. mathieu.boissan@inserm.fr philippe.chavrier@curie.fr.
[Ti] Título:Membrane trafficking. Nucleoside diphosphate kinases fuel dynamin superfamily proteins with GTP for membrane remodeling.
[So] Source:Science;344(6191):1510-5, 2014 Jun 27.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Dynamin superfamily molecular motors use guanosine triphosphate (GTP) as a source of energy for membrane-remodeling events. We found that knockdown of nucleoside diphosphate kinases (NDPKs) NM23-H1/H2, which produce GTP through adenosine triphosphate (ATP)-driven conversion of guanosine diphosphate (GDP), inhibited dynamin-mediated endocytosis. NM23-H1/H2 localized at clathrin-coated pits and interacted with the proline-rich domain of dynamin. In vitro, NM23-H1/H2 were recruited to dynamin-induced tubules, stimulated GTP-loading on dynamin, and triggered fission in the presence of ATP and GDP. NM23-H4, a mitochondria-specific NDPK, colocalized with mitochondrial dynamin-like OPA1 involved in mitochondria inner membrane fusion and increased GTP-loading on OPA1. Like OPA1 loss of function, silencing of NM23-H4 but not NM23-H1/H2 resulted in mitochondrial fragmentation, reflecting fusion defects. Thus, NDPKs interact with and provide GTP to dynamins, allowing these motor proteins to work with high thermodynamic efficiency.
[Mh] Termos MeSH primário: Membrana Celular/metabolismo
Dinaminas/metabolismo
Guanosina Trifosfato/metabolismo
Nucleosídeo NM23 Difosfato Quinases/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Animais
Linhagem Celular
Invaginações Revestidas da Membrana Celular/metabolismo
Endocitose
GTP Fosfo-Hidrolases/metabolismo
Guanosina Difosfato/metabolismo
Seres Humanos
Membranas Intracelulares/metabolismo
Fusão de Membrana
Mitocôndrias/metabolismo
Nucleosídeo NM23 Difosfato Quinases/genética
Nucleosídeo Difosfato Quinase D/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (NM23 Nucleoside Diphosphate Kinases); 146-91-8 (Guanosine Diphosphate); 86-01-1 (Guanosine Triphosphate); 8L70Q75FXE (Adenosine Triphosphate); EC 2.7.4.6 (NME1 protein, human); EC 2.7.4.6 (NME2 protein, human); EC 2.7.4.6 (NME4 protein, human); EC 2.7.4.6 (Nucleoside Diphosphate Kinase D); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.1.- (OPA1 protein, human); EC 3.6.5.5 (Dynamins)
[Em] Mês de entrada:1407
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140628
[St] Status:MEDLINE
[do] DOI:10.1126/science.1253768


  6 / 19 MEDLINE  
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[PMID]:23616472
[Au] Autor:Lower KM; De Gobbi M; Hughes JR; Derry CJ; Ayyub H; Sloane-Stanley JA; Vernimmen D; Garrick D; Gibbons RJ; Higgs DR
[Ad] Endereço:MRC Molecular Haematology Unit, Weatherall Institute of Molecular Medicine, John Radcliffe Hospital, Oxford, UK.
[Ti] Título:Analysis of sequence variation underlying tissue-specific transcription factor binding and gene expression.
[So] Source:Hum Mutat;34(8):1140-8, 2013 Aug.
[Is] ISSN:1098-1004
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Although mutations causing monogenic disorders most frequently lie within the affected gene, sequence variation in complex disorders is more commonly found in noncoding regions. Furthermore, recent genome- wide studies have shown that common DNA sequence variants in noncoding regions are associated with "normal" variation in gene expression resulting in cell-specific and/or allele-specific differences. The mechanism by which such sequence variation causes changes in gene expression is largely unknown. We have addressed this by studying natural variation in the binding of key transcription factors (TFs) in the well-defined, purified cell system of erythropoiesis. We have shown that common polymorphisms frequently directly perturb the binding sites of key TFs, and detailed analysis shows how this causes considerable (~10-fold) changes in expression from a single allele in a tissue-specific manner. We also show how a SNP, located at some distance from the recognized TF binding site, may affect the recruitment of a large multiprotein complex and alter the associated chromatin modification of the variant regulatory element. This study illustrates the principles by which common sequence variation may cause changes in tissue-specific gene expression, and suggests that such variation may underlie an individual's propensity to develop complex human genetic diseases.
[Mh] Termos MeSH primário: Células Eritroides/metabolismo
Expressão Gênica
Peptídeos e Proteínas de Sinalização Intracelular/genética
Nucleosídeo Difosfato Quinase D/genética
Nucleosídeo Difosfato Quinase D/metabolismo
Polimorfismo de Nucleotídeo Único
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Sequência de Bases
Sítios de Ligação/genética
Variação Genética
Estudo de Associação Genômica Ampla
Seres Humanos
Peptídeos e Proteínas de Sinalização Intracelular/química
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Dados de Sequência Molecular
Ligação Proteica
Sequências Reguladoras de Ácido Nucleico
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Intracellular Signaling Peptides and Proteins); 0 (STIL protein, human); 0 (Transcription Factors); EC 2.7.4.6 (NME4 protein, human); EC 2.7.4.6 (Nucleoside Diphosphate Kinase D)
[Em] Mês de entrada:1401
[Cu] Atualização por classe:130716
[Lr] Data última revisão:
130716
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130426
[St] Status:MEDLINE
[do] DOI:10.1002/humu.22343


  7 / 19 MEDLINE  
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[PMID]:23150663
[Au] Autor:Schlattner U; Tokarska-Schlattner M; Ramirez S; Tyurina YY; Amoscato AA; Mohammadyani D; Huang Z; Jiang J; Yanamala N; Seffouh A; Boissan M; Epand RF; Epand RM; Klein-Seetharaman J; Lacombe ML; Kagan VE
[Ad] Endereço:From the Laboratory of Fundamental and Applied Bioenergetics and Federative Research Structure Environmental and Systems Biology, University Joseph Fourier, 38041 Grenoble Cedex 9, France.
[Ti] Título:Dual function of mitochondrial Nm23-H4 protein in phosphotransfer and intermembrane lipid transfer: a cardiolipin-dependent switch.
[So] Source:J Biol Chem;288(1):111-21, 2013 Jan 04.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The nucleoside diphosphate kinase Nm23-H4/NDPK-D forms symmetrical hexameric complexes in the mitochondrial intermembrane space with phosphotransfer activity using mitochondrial ATP to regenerate nucleoside triphosphates. We demonstrate the complex formation between Nm23-H4 and mitochondrial GTPase OPA1 in rat liver, suggesting its involvement in local and direct GTP delivery. Similar to OPA1, Nm23-H4 is further known to strongly bind in vitro to anionic phospholipids, mainly cardiolipin, and in vivo to the inner mitochondrial membrane. We show here that such protein-lipid complexes inhibit nucleoside diphosphate kinase activity but are necessary for another function of Nm23-H4, selective intermembrane lipid transfer. Mitochondrial lipid distribution was analyzed by liquid chromatography-mass spectrometry using HeLa cells expressing either wild-type Nm23-H4 or a membrane binding-deficient mutant at a site predicted based on molecular modeling to be crucial for cardiolipin binding and transfer mechanism. We found that wild type, but not the mutant enzyme, selectively increased the content of cardiolipin in the outer mitochondrial membrane, but the distribution of other more abundant phospholipids (e.g. phosphatidylcholine) remained unchanged. HeLa cells expressing the wild-type enzyme showed increased accumulation of Bax in mitochondria and were sensitized to rotenone-induced apoptosis as revealed by stimulated release of cytochrome c into the cytosol, elevated caspase 3/7 activity, and increased annexin V binding. Based on these data and molecular modeling, we propose that Nm23-H4 acts as a lipid-dependent mitochondrial switch with dual function in phosphotransfer serving local GTP supply and cardiolipin transfer for apoptotic signaling and putative other functions.
[Mh] Termos MeSH primário: Cardiolipinas/fisiologia
Membranas Intracelulares/metabolismo
Lipídeos/química
Nucleosídeo Difosfato Quinase D/química
Nucleosídeo Difosfato Quinase D/fisiologia
[Mh] Termos MeSH secundário: Animais
Apoptose
Cardiolipinas/química
GTP Fosfo-Hidrolases/química
Metabolismo dos Lipídeos
Fígado/metabolismo
Masculino
Modelos Moleculares
Fosfolipídeos/química
Ligação Proteica
Conformação Proteica
Ratos
Ratos Wistar
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Cardiolipins); 0 (Lipids); 0 (Phospholipids); EC 2.7.4.6 (NME4 protein, human); EC 2.7.4.6 (Nucleoside Diphosphate Kinase D); EC 3.6.1.- (GTP Phosphohydrolases)
[Em] Mês de entrada:1302
[Cu] Atualização por classe:161202
[Lr] Data última revisão:
161202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121115
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M112.408633


  8 / 19 MEDLINE  
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[PMID]:22974817
[Au] Autor:Francois-Moutal L; Maniti O; Marcillat O; Granjon T
[Ad] Endereço:Université de Lyon, Université Lyon 1, CNRS, UMR 5246, Institut de Chimie et Biochimie Moléculaires et Supramoléculaires, IMBL, 43 Bd du 11 Novembre 1918 F-69622 Villeurbanne, France.
[Ti] Título:New insights into lipid-Nucleoside Diphosphate Kinase-D interaction mechanism: protein structural changes and membrane reorganisation.
[So] Source:Biochim Biophys Acta;1828(2):906-15, 2013 Feb.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Nucleoside Diphosphate Kinases (NDPKs) have long been considered merely as housekeeping enzymes. The discovery of the NME1 gene, an anti-metastatic gene coding for NDPK-A, led the scientific community to re-evaluate their role in the cell. It is now well established that the NDPK family is more complex than what was first thought, and despite the increasing amount of evidence suggesting the multifunctional role of nm23/NDPKs, the specific functions of each family member are still elusive. Among these isoforms, NDPK-D is the only one to present a mitochondria-targeting sequence. It has recently been shown that this protein is able to bind and cross-link with mitochondrial membranes, suggesting that NDPK-D can mediate contact sites and contributes to the mitochondrial intermembrane space structuring. To better understand the influence of NDPK-D on mitochondrial lipid organisation, we analysed its behaviour in different lipid environments. We found that NDPK-D not only interacts with CL or anionic lipids, but is also able to bind in a non negligible manner to zwitterionic PC. NDPK-D alters membrane organisation in terms of fluidity, hydration and lipid clustering, effects which depend on lipid structure. Changes in the protein structure after lipid binding were evidenced, both by fluorescence and infrared spectroscopy, regardless of membrane composition. Taking into account all these elements, a putative mechanism of interaction between NDPK-D and zwitterionic or anionic lipids was proposed.
[Mh] Termos MeSH primário: Membrana Celular/metabolismo
Lipídeos/química
Nucleosídeo Difosfato Quinase D/química
Fosfatidilcolinas/química
Proteínas/química
[Mh] Termos MeSH secundário: Ânions
Bactérias/metabolismo
Reagentes para Ligações Cruzadas/química
Seres Humanos
Lipossomos/química
Mitocôndrias/metabolismo
Modelos Biológicos
Conformação Molecular
Pressão
Ligação Proteica
Conformação Proteica
Espectrometria de Fluorescência/métodos
Espectrofotometria Infravermelho/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anions); 0 (Cross-Linking Reagents); 0 (Lipids); 0 (Liposomes); 0 (Phosphatidylcholines); 0 (Proteins); EC 2.7.4.6 (Nucleoside Diphosphate Kinase D)
[Em] Mês de entrada:1304
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120915
[St] Status:MEDLINE


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[PMID]:21099363
[Au] Autor:Gibbons RJ; Higgs DR
[Ti] Título:ATRX: taming tandem repeats.
[So] Source:Cell Cycle;9(23):4605-6, 2010 Dec 01.
[Is] ISSN:1551-4005
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: DNA Helicases/metabolismo
Proteínas Nucleares/metabolismo
Sequências de Repetição em Tandem
[Mh] Termos MeSH secundário: Ilhas de CpG
DNA Helicases/genética
Replicação do DNA
Quadruplex G
Histonas/genética
Histonas/metabolismo
Seres Humanos
Retardo Mental Ligado ao Cromossomo X/genética
Proteínas Mitocondriais/genética
Proteínas Mitocondriais/metabolismo
Nucleosídeo NM23 Difosfato Quinases/genética
Nucleosídeo NM23 Difosfato Quinases/metabolismo
Proteínas Nucleares/genética
Nucleosídeo Difosfato Quinase D
Proteína Nuclear Ligada ao X
Talassemia alfa/genética
[Pt] Tipo de publicação:EDITORIAL
[Nm] Nome de substância:
0 (Histones); 0 (Mitochondrial Proteins); 0 (NM23 Nucleoside Diphosphate Kinases); 0 (Nuclear Proteins); EC 2.7.4.6 (NME4 protein, human); EC 2.7.4.6 (Nucleoside Diphosphate Kinase D); EC 3.6.4.- (DNA Helicases); EC 3.6.4.12 (ATRX protein, human); EC 3.6.4.12 (X-linked Nuclear Protein)
[Em] Mês de entrada:1104
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:101125
[St] Status:MEDLINE


  10 / 19 MEDLINE  
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[PMID]:19254751
[Au] Autor:Lacombe ML; Tokarska-Schlattner M; Epand RF; Boissan M; Epand RM; Schlattner U
[Ad] Endereço:INSERM UMRS, UMPC Université Paris, France. Marie-Lise.Lacombe@inserm.fr
[Ti] Título:Interaction of NDPK-D with cardiolipin-containing membranes: Structural basis and implications for mitochondrial physiology.
[So] Source:Biochimie;91(6):779-83, 2009 Jun.
[Is] ISSN:1638-6183
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Nucleoside diphosphate kinases (NDPKs/Nm23), responsible for intracellular di- and tri-phosphonucleoside homeostasis, play multi-faceted roles in cellular energetic, signaling, proliferation, differentiation and tumor invasion. The mitochondrial NDPK-D, the NME4 gene product, is a peripheral protein of the inner membrane. Several new aspects of the interaction of NDPK-D with the inner mitochondrial membrane have been recently characterized. Surface plasmon resonance analysis using recombinant NDPK-D and different phospholipid liposomes showed that NDPK-D interacts electrostatically with anionic phospholipids, with highest affinity observed for cardiolipin, a phospholipid located mostly in the mitochondrial inner membrane. Mutation of the central arginine (R90) in a surface exposed cationic RRK motif unique to NDPK-D strongly reduced phospholipid interaction in vitro and in vivo. Stable expression of NDPK-D proteins in HeLa cells naturally almost devoid of this isoform revealed a tight functional coupling of NDPK-D with oxidative phosphorylation that depends on the membrane-bound state of the enzyme. Owing to its symmetrical hexameric structure exposing membrane binding motifs on two opposite sides, NDPK-D could bridge liposomes containing anionic phospholipids and promote lipid transfer between them. In vivo, NDPK-D could induce intermembrane contacts and facilitate lipid movements between mitochondrial membranes. Most of these properties are reminiscent to those of the mitochondrial creatine kinase. We review here the common properties of both kinases and we discuss their potential roles in mitochondrial functions such as energy production, apoptosis and mitochondrial dynamics.
[Mh] Termos MeSH primário: Cardiolipinas/metabolismo
Membranas Intracelulares/metabolismo
Mitocôndrias/metabolismo
Nucleosídeo NM23 Difosfato Quinases/metabolismo
[Mh] Termos MeSH secundário: Cardiolipinas/química
Membranas Intracelulares/química
Proteínas de Membrana/química
Proteínas de Membrana/metabolismo
Mitocôndrias/fisiologia
Modelos Moleculares
Nucleosídeo NM23 Difosfato Quinases/química
Nucleosídeo NM23 Difosfato Quinases/genética
Nucleosídeo Difosfato Quinase D
Ligação Proteica
Conformação Proteica
Ressonância de Plasmônio de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Cardiolipins); 0 (Membrane Proteins); 0 (NM23 Nucleoside Diphosphate Kinases); EC 2.7.4.6 (NME4 protein, human); EC 2.7.4.6 (Nucleoside Diphosphate Kinase D)
[Em] Mês de entrada:0909
[Cu] Atualização por classe:111117
[Lr] Data última revisão:
111117
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090304
[St] Status:MEDLINE
[do] DOI:10.1016/j.biochi.2009.02.006



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