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Pesquisa : D08.811.913.050.134.423.500 [Categoria DeCS]
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  1 / 103 MEDLINE  
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[PMID]:28943313
[Au] Autor:Lee CC; Peng SH; Shen L; Lee CF; Du TH; Kang ML; Xu GL; Upadhyay AK; Cheng X; Yan YT; Zhang Y; Juan LJ
[Ad] Endereço:Genomics Research Center, Academia Sinica, Taipei 115, Taiwan, ROC.
[Ti] Título:The Role of N-α-acetyltransferase 10 Protein in DNA Methylation and Genomic Imprinting.
[So] Source:Mol Cell;68(1):89-103.e7, 2017 Oct 05.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Genomic imprinting is an allelic gene expression phenomenon primarily controlled by allele-specific DNA methylation at the imprinting control region (ICR), but the underlying mechanism remains largely unclear. N-α-acetyltransferase 10 protein (Naa10p) catalyzes N-α-acetylation of nascent proteins, and mutation of human Naa10p is linked to severe developmental delays. Here we report that Naa10-null mice display partial embryonic lethality, growth retardation, brain disorders, and maternal effect lethality, phenotypes commonly observed in defective genomic imprinting. Genome-wide analyses further revealed global DNA hypomethylation and enriched dysregulation of imprinted genes in Naa10p-knockout embryos and embryonic stem cells. Mechanistically, Naa10p facilitates binding of DNA methyltransferase 1 (Dnmt1) to DNA substrates, including the ICRs of the imprinted allele during S phase. Moreover, the lethal Ogden syndrome-associated mutation of human Naa10p disrupts its binding to the ICR of H19 and Dnmt1 recruitment. Our study thus links Naa10p mutation-associated Ogden syndrome to defective DNA methylation and genomic imprinting.
[Mh] Termos MeSH primário: DNA (Citosina-5-)-Metiltransferases/genética
Deficiências do Desenvolvimento/genética
Epigênese Genética
Impressão Genômica
Acetiltransferase N-Terminal A/genética
Acetiltransferase N-Terminal E/genética
RNA Longo não Codificante/genética
[Mh] Termos MeSH secundário: Animais
DNA/genética
DNA/metabolismo
DNA (Citosina-5-)-Metiltransferase 1
DNA (Citosina-5-)-Metiltransferases/metabolismo
Metilação de DNA
Deficiências do Desenvolvimento/metabolismo
Deficiências do Desenvolvimento/patologia
Modelos Animais de Doenças
Embrião de Mamíferos
Feminino
Deleção de Genes
Genes Letais
Estudo de Associação Genômica Ampla
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Células-Tronco Embrionárias Murinas/metabolismo
Células-Tronco Embrionárias Murinas/patologia
Acetiltransferase N-Terminal A/deficiência
Acetiltransferase N-Terminal E/deficiência
Ligação Proteica
RNA Longo não Codificante/metabolismo
Fase S/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (H19 long non-coding RNA); 0 (RNA, Long Noncoding); 9007-49-2 (DNA); EC 2.1.1.37 (DNA (Cytosine-5-)-Methyltransferase 1); EC 2.1.1.37 (DNA (Cytosine-5-)-Methyltransferases); EC 2.1.1.37 (DNMT1 protein, human); EC 2.1.1.37 (Dnmt1 protein, mouse); EC 2.3.1.88 (N-Terminal Acetyltransferase A); EC 2.3.1.88 (N-Terminal Acetyltransferase E); EC 2.3.1.88 (Naa10 protein, mouse)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170926
[St] Status:MEDLINE


  2 / 103 MEDLINE  
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[PMID]:28238651
[Au] Autor:Qian X; Li X; Cai Q; Zhang C; Yu Q; Jiang Y; Lee JH; Hawke D; Wang Y; Xia Y; Zheng Y; Jiang BH; Liu DX; Jiang T; Lu Z
[Ad] Endereço:Brain Tumor Center and Department of Neuro-Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA.
[Ti] Título:Phosphoglycerate Kinase 1 Phosphorylates Beclin1 to Induce Autophagy.
[So] Source:Mol Cell;65(5):917-931.e6, 2017 Mar 02.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Autophagy is crucial for maintaining cell homeostasis. However, the precise mechanism underlying autophagy initiation remains to be defined. Here, we demonstrate that glutamine deprivation and hypoxia result in inhibition of mTOR-mediated acetyl-transferase ARD1 S228 phosphorylation, leading to ARD1-dependent phosphoglycerate kinase 1 (PGK1) K388 acetylation and subsequent PGK1-mediated Beclin1 S30 phosphorylation. This phosphorylation enhances ATG14L-associated class III phosphatidylinositol 3-kinase VPS34 activity by increasing the binding of phosphatidylinositol to VPS34. ARD1-dependent PGK1 acetylation and PGK1-mediated Beclin1 S30 phosphorylation are required for glutamine deprivation- and hypoxia-induced autophagy and brain tumorigenesis. Furthermore, PGK1 K388 acetylation levels correlate with Beclin1 S30 phosphorylation levels and poor prognosis in glioblastoma patients. Our study unearths an important mechanism underlying cellular-stress-induced autophagy initiation in which the protein kinase activity of the metabolic enzyme PGK1 plays an instrumental role and reveals the significance of the mutual regulation of autophagy and cell metabolism in maintaining cell homeostasis.
[Mh] Termos MeSH primário: Autofagossomos/enzimologia
Autofagia
Beclina-1/metabolismo
Neoplasias Encefálicas/enzimologia
Glioblastoma/enzimologia
Fosfoglicerato Quinase/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Animais
Autofagossomos/patologia
Beclina-1/genética
Neoplasias Encefálicas/genética
Neoplasias Encefálicas/patologia
Linhagem Celular Tumoral
Proliferação Celular
Classe III de Fosfatidilinositol 3-Quinases/genética
Classe III de Fosfatidilinositol 3-Quinases/metabolismo
Feminino
Glioblastoma/genética
Glioblastoma/patologia
Glutamina/deficiência
Células HEK293
Seres Humanos
Camundongos Nus
Acetiltransferase N-Terminal A/genética
Acetiltransferase N-Terminal A/metabolismo
Acetiltransferase N-Terminal E/genética
Acetiltransferase N-Terminal E/metabolismo
Fosfoglicerato Quinase/genética
Fosforilação
Ligação Proteica
Interferência de RNA
Transdução de Sinais
Serina-Treonina Quinases TOR/genética
Serina-Treonina Quinases TOR/metabolismo
Fatores de Tempo
Transfecção
Carga Tumoral
Hipóxia Tumoral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (BECN1 protein, human); 0 (Beclin-1); 0RH81L854J (Glutamine); EC 2.3.1.88 (N-Terminal Acetyltransferase A); EC 2.3.1.88 (N-Terminal Acetyltransferase E); EC 2.3.1.88 (NAA10 protein, human); EC 2.7.1.1 (MTOR protein, human); EC 2.7.1.1 (TOR Serine-Threonine Kinases); EC 2.7.1.137 (Class III Phosphatidylinositol 3-Kinases); EC 2.7.2.3 (PGK1 protein, human); EC 2.7.2.3 (Phosphoglycerate Kinase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170228
[St] Status:MEDLINE


  3 / 103 MEDLINE  
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[PMID]:27993683
[Au] Autor:Cai S; Liu X; Zhang C; Xing B; Du X
[Ad] Endereço:Department of Cell Biology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing 100191, China.
[Ti] Título:Autoacetylation of NAT10 is critical for its function in rRNA transcription activation.
[So] Source:Biochem Biophys Res Commun;483(1):624-629, 2017 Jan 29.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:NAT10, an important member of GNAT family, harbors histone acetyltransferase and participates in many cellular processes such as ribosome production and cell cycle. Here, we report that NAT10 is acetylated in vivo and autoacetylated in vitro. The lysine residue at 426 (K426) is the acetylation site of NAT10. K426R mutant of NAT10 fails to activate rRNA transcription. NAT10 K426R loses its capability of acetylating UBF though it still binds UBF, which fails to recruit PAF53 and RNA polymerase I to rDNA, eventually resulting in inhibition of pre-rRNA transcription. Therefore, acetylation of K426 in NAT10 is required for its function in activating rRNA transcription. These findings identify a new post-translational modification on NAT10 which regulates its function.
[Mh] Termos MeSH primário: Acetiltransferase N-Terminal E/metabolismo
RNA Ribossômico/metabolismo
Ativação Transcricional
[Mh] Termos MeSH secundário: Acetilação
Sítios de Ligação
Células HCT116
Células HEK293
Células HeLa
Seres Humanos
Lisina/química
Mutação
Processamento de Proteína Pós-Traducional
RNA Polimerase I/metabolismo
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Ribosomal); EC 2.3.1.88 (N-Terminal Acetyltransferase E); EC 2.3.1.88 (NAT10 protein, human); EC 2.7.7.6 (RNA Polymerase I); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170606
[Lr] Data última revisão:
170606
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161221
[St] Status:MEDLINE


  4 / 103 MEDLINE  
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[PMID]:27668839
[Au] Autor:Dörfel MJ; Fang H; Crain J; Klingener M; Weiser J; Lyon GJ
[Ad] Endereço:Stanley Institute for Cognitive Genomics, One Bungtown Road, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, USA.
[Ti] Título:Proteomic and genomic characterization of a yeast model for Ogden syndrome.
[So] Source:Yeast;34(1):19-37, 2017 Jan.
[Is] ISSN:1097-0061
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Naa10 is an N -terminal acetyltransferase that, in a complex with its auxiliary subunit Naa15, co-translationally acetylates the α-amino group of newly synthetized proteins as they emerge from the ribosome. Roughly 40-50% of the human proteome is acetylated by Naa10, rendering this an enzyme one of the most broad substrate ranges known. Recently, we reported an X-linked disorder of infancy, Ogden syndrome, in two families harbouring a c.109 T > C (p.Ser37Pro) variant in NAA10. In the present study we performed in-depth characterization of a yeast model of Ogden syndrome. Stress tests and proteomic analyses suggest that the S37P mutation disrupts Naa10 function and reduces cellular fitness during heat shock, possibly owing to dysregulation of chaperone expression and accumulation. Microarray and RNA-seq revealed a pseudo-diploid gene expression profile in ΔNaa10 cells, probably responsible for a mating defect. In conclusion, the data presented here further support the disruptive nature of the S37P/Ogden mutation and identify affected cellular processes potentially contributing to the severe phenotype seen in Ogden syndrome. Data are available via GEO under identifier GSE86482 or with ProteomeXchange under identifier PXD004923. © 2016 The Authors. Yeast published by John Wiley & Sons, Ltd.
[Mh] Termos MeSH primário: Doenças Genéticas Ligadas ao Cromossomo X/genética
Saccharomyces cerevisiae/genética
[Mh] Termos MeSH secundário: Substituição de Aminoácidos/genética
Substituição de Aminoácidos/fisiologia
Western Blotting
Genômica
Seres Humanos
Espectrometria de Massas
Modelos Biológicos
Acetiltransferase N-Terminal A/genética
Acetiltransferase N-Terminal A/fisiologia
Acetiltransferase N-Terminal E/genética
Acetiltransferase N-Terminal E/fisiologia
Análise de Sequência com Séries de Oligonucleotídeos
Proteômica
Saccharomyces cerevisiae/fisiologia
Alinhamento de Sequência
Síndrome
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.3.1.88 (N-Terminal Acetyltransferase A); EC 2.3.1.88 (N-Terminal Acetyltransferase E); EC 2.3.1.88 (NAA10 protein, human)
[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:160927
[St] Status:MEDLINE
[do] DOI:10.1002/yea.3211


  5 / 103 MEDLINE  
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[PMID]:27484799
[Au] Autor:Reddi R; Saddanapu V; Chinthapalli DK; Sankoju P; Sripadi P; Addlagatta A
[Ad] Endereço:From the Centre for Chemical Biology and.
[Ti] Título:Human Naa50 Protein Displays Broad Substrate Specificity for Amino-terminal Acetylation: DETAILED STRUCTURAL AND BIOCHEMICAL ANALYSIS USING TETRAPEPTIDE LIBRARY.
[So] Source:J Biol Chem;291(39):20530-8, 2016 Sep 23.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Amino-terminal acetylation is a critical co-translational modification of the newly synthesized proteins in a eukaryotic cell carried out by six amino-terminal acetyltransferases (NATs). All NATs contain at least one catalytic subunit, and some contain one or two additional auxiliary subunits. For example, NatE is a complex of Naa10, Naa50, and Naa15 (auxiliary). In the present study, the crystal structure of human Naa50 suggested the presence of CoA and acetylated tetrapeptide (AcMMXX) that have co-purified with the protein. Biochemical and thermal stability studies on the tetrapeptide library with variations in the first and second positions confirm our results from the crystal structure that a peptide with Met-Met in the first two positions is the best substrate for this enzyme. In addition, Naa50 acetylated all MXAA peptides except for MPAA. Transcriptome analysis of 10 genes that make up six NATs in humans from eight different cell lines suggests that components of NatE are transcribed in all cell lines, whereas others are variable. Because Naa10 is reported to acetylate all amino termini that are devoid of methionine and Naa50 acetylates all other peptides that are followed by methionine, we believe that NatE complex can be a major contributor for amino-terminal acetylation at the ribosome exit tunnel.
[Mh] Termos MeSH primário: Acetiltransferase N-Terminal E/metabolismo
Oligopeptídeos/química
Biblioteca de Peptídeos
[Mh] Termos MeSH secundário: Células A549
Acetilação
Células HEK293
Seres Humanos
Complexos Multienzimáticos/genética
Complexos Multienzimáticos/metabolismo
Acetiltransferase N-Terminal A/genética
Acetiltransferase N-Terminal A/metabolismo
Acetiltransferase N-Terminal E/genética
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Multienzyme Complexes); 0 (Oligopeptides); 0 (Peptide Library); EC 2.3.1.88 (N-Terminal Acetyltransferase A); EC 2.3.1.88 (N-Terminal Acetyltransferase E); EC 2.3.1.88 (NAA10 protein, human); EC 2.3.1.88 (NAA15 protein, human); EC 2.3.1.88 (NAA50 protein, human)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170923
[Lr] Data última revisão:
170923
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160804
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.730432


  6 / 103 MEDLINE  
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[PMID]:27422821
[Au] Autor:Rong Z; Ouyang Z; Magin RS; Marmorstein R; Yu H
[Ad] Endereço:From the Howard Hughes Medical Institute, Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas 75390 and.
[Ti] Título:Opposing Functions of the N-terminal Acetyltransferases Naa50 and NatA in Sister-chromatid Cohesion.
[So] Source:J Biol Chem;291(36):19079-91, 2016 09 02.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:During the cell cycle, sister-chromatid cohesion tethers sister chromatids together from S phase to the metaphase-anaphase transition and ensures accurate segregation of chromatids into daughter cells. N-terminal acetylation is one of the most prevalent protein covalent modifications in eukaryotes and is mediated by a family of N-terminal acetyltransferases (NAT). Naa50 (also called San) has previously been shown to play a role in sister-chromatid cohesion in metazoans. The mechanism by which Naa50 contributes to cohesion is not understood however. Here, we show that depletion of Naa50 in HeLa cells weakens the interaction between cohesin and its positive regulator sororin and causes cohesion defects in S phase, consistent with a role of Naa50 in cohesion establishment. Strikingly, co-depletion of NatA, a heterodimeric NAT complex that physically interacts with Naa50, rescues the sister-chromatid cohesion defects and the resulting mitotic arrest caused by Naa50 depletion, indicating that NatA and Naa50 play antagonistic roles in cohesion. Purified recombinant NatA and Naa50 do not affect each other's NAT activity in vitro Because NatA and Naa50 exhibit distinct substrate specificity, we propose that they modify different effectors and regulate sister-chromatid cohesion in opposing ways.
[Mh] Termos MeSH primário: Proteínas de Ciclo Celular/metabolismo
Cromátides/enzimologia
Proteínas Cromossômicas não Histona/metabolismo
Cromossomos Humanos/enzimologia
Mitose/fisiologia
Acetiltransferase N-Terminal A/metabolismo
Acetiltransferase N-Terminal E/metabolismo
Fase S/fisiologia
[Mh] Termos MeSH secundário: Proteínas de Ciclo Celular/genética
Cromátides/genética
Proteínas Cromossômicas não Histona/genética
Cromossomos Humanos/genética
Células HeLa
Seres Humanos
Acetiltransferase N-Terminal A/genética
Acetiltransferase N-Terminal E/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cell Cycle Proteins); 0 (Chromosomal Proteins, Non-Histone); 0 (cohesins); EC 2.3.1.88 (N-Terminal Acetyltransferase A); EC 2.3.1.88 (N-Terminal Acetyltransferase E); EC 2.3.1.88 (NAA50 protein, human)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171124
[Lr] Data última revisão:
171124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160717
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.737585


  7 / 103 MEDLINE  
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[PMID]:26882543
[Au] Autor:Liu X; Tan Y; Zhang C; Zhang Y; Zhang L; Ren P; Deng H; Luo J; Ke Y; Du X
[Ad] Endereço:Key Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Peking University Health Science Center, Beijing, China Department of Cell Biology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.
[Ti] Título:NAT10 regulates p53 activation through acetylating p53 at K120 and ubiquitinating Mdm2.
[So] Source:EMBO Rep;17(3):349-66, 2016 Mar.
[Is] ISSN:1469-3178
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:As a genome guardian, p53 maintains genome stability by arresting cells for damage repair or inducing cell apoptosis to eliminate the damaged cells in stress response. Several nucleolar proteins stabilize p53 by interfering Mdm2-p53 interaction upon cellular stress, while other mechanisms by which nucleolar proteins activate p53 remain to be determined. Here, we identify NAT10 as a novel regulator for p53 activation. NAT10 acetylates p53 at K120 and stabilizes p53 by counteracting Mdm2 action. In addition, NAT10 promotes Mdm2 degradation with its intrinsic E3 ligase activity. After DNA damage, NAT10 translocates to nucleoplasm and activates p53-mediated cell cycle control and apoptosis. Finally, NAT10 inhibits cell proliferation and expression of NAT10 decreases in human colorectal carcinomas. Thus, our data demonstrate that NAT10 plays a critical role in p53 activation via acetylating p53 and counteracting Mdm2 action, providing a novel pathway by which nucleolar protein activates p53 as a cellular stress sensor.
[Mh] Termos MeSH primário: Neoplasias Colorretais/metabolismo
Acetiltransferase N-Terminal E/metabolismo
Proteínas Proto-Oncogênicas c-mdm2/metabolismo
Proteína Supressora de Tumor p53/metabolismo
Ubiquitinação
[Mh] Termos MeSH secundário: Acetilação
Transporte Ativo do Núcleo Celular
Apoptose
Núcleo Celular/metabolismo
Dano ao DNA
Células HCT116
Células HEK293
Seres Humanos
Acetiltransferase N-Terminal E/genética
Ligação Proteica
Estabilidade Proteica
Proteólise
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Tumor Suppressor Protein p53); EC 2.3.1.88 (N-Terminal Acetyltransferase E); EC 2.3.1.88 (NAT10 protein, human); EC 2.3.2.27 (MDM2 protein, human); EC 2.3.2.27 (Proto-Oncogene Proteins c-mdm2)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160217
[St] Status:MEDLINE
[do] DOI:10.15252/embr.201540505


  8 / 103 MEDLINE  
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[PMID]:26755727
[Au] Autor:Magin RS; March ZM; Marmorstein R
[Ad] Endereço:From the Department of Biochemistry and Biophysics, Abramson Family Cancer Research Institute, and Graduate Group in Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104 and.
[Ti] Título:The N-terminal Acetyltransferase Naa10/ARD1 Does Not Acetylate Lysine Residues.
[So] Source:J Biol Chem;291(10):5270-7, 2016 Mar 04.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The N-terminal acetyltransferase NatA is a heterodimeric complex consisting of a catalytic subunit (Naa10/ARD1) and an auxiliary subunit (Naa15). NatA co-translationally acetylates the N termini of a wide variety of nascent polypeptides. In addition, Naa10 can act independently to posttranslationally acetylate a distinct set of substrates, notably actin. Recent structural studies of Naa10 have also revealed the molecular basis for N-terminal acetylation specificity. Surprisingly, recent reports claim that Naa10 may also acetylate lysine residues of diverse targets, including methionine sulfoxide reductase A, myosin light chain kinase, and Runt-related transcription factor 2. Here we used recombinant proteins to reconstitute and assess lysine acetylation events catalyzed by Naa10 in vitro. We show that there is no difference in lysine acetylation of substrate proteins with or without Naa10, suggesting that the substrates may be acetylated chemically rather than enzymatically. Together, our data argue against a role for Naa10 in lysine acetylation.
[Mh] Termos MeSH primário: Lisina/metabolismo
Acetiltransferase N-Terminal A/metabolismo
Acetiltransferase N-Terminal E/metabolismo
Processamento de Proteína Pós-Traducional
[Mh] Termos MeSH secundário: Acetilação
Sequência de Aminoácidos
Animais
Subunidade alfa 1 de Fator de Ligação ao Core/metabolismo
Seres Humanos
Metionina Sulfóxido Redutases/metabolismo
Camundongos
Dados de Sequência Molecular
Quinase de Cadeia Leve de Miosina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Core Binding Factor Alpha 1 Subunit); 0 (Runx2 protein, mouse); EC 1.8.4.- (Methionine Sulfoxide Reductases); EC 1.8.4.11 (methionine sulfoxide reductase); EC 2.3.1.88 (N-Terminal Acetyltransferase A); EC 2.3.1.88 (N-Terminal Acetyltransferase E); EC 2.3.1.88 (NAA10 protein, human); EC 2.7.11.18 (Myosin-Light-Chain Kinase); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:170505
[Lr] Data última revisão:
170505
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160113
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.709428


  9 / 103 MEDLINE  
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[PMID]:26662107
[Au] Autor:Zeng Y; Zheng J; Zhao J; Jia PR; Yang Y; Yang GJ; Ma JF; Gu YQ; Xu J
[Ad] Endereço:Department of Biochemistry and Key Laboratory of Xinjiang Endemic and Ethnic Diseases, Shihezi University School of Medicine, Shihezi, Xinjiang, 832002, China.
[Ti] Título:High expression of Naa10p associates with lymph node metastasis and predicts favorable prognosis of oral squamous cell carcinoma.
[So] Source:Tumour Biol;37(5):6719-28, 2016 May.
[Is] ISSN:1423-0380
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:N-a-Acetyltransferase 10 protein (Naa10p) is a potential prognostic biomarker and a modulator of several types of cancer. Despite the efforts to elucidate the relationship between Naa10p expression and clinical prognosis, little is known about its expression and role in human oral squamous cell carcinoma (OSCC). In this study, we firstly detected the mRNA and protein levels of Naa10p in 10 paired OSCC tissue samples and found Naa10p was frequently overexpressed in the tumor tissues of patients with OSCC. Further detection by immunohistochemistry was used to examine Naa10p expression in 124 OSCC tumor specimens by tissue microarray (TMA), and a relative high level of Naa10p protein expression was found in 98 out of 124 cases (79.03 %). Additional analyses illustrated that Naa10p expression inversely correlated with clinical stage (p = 0.047), degree of lymph node status (p = 0.020), differentiation (p = 0.022), and recurrence (p = 0.016) of patients with OSCC. The survival analysis showed that patients with Naa10p-positive expression had a better prognosis for disease-free survival (DFS) or overall survival (OS) than those with Naa10p-negative expression (p = 0.003 for both). Furthermore, we assessed the effect of Naa10p knockdown on motility of oral cancer cells in vitro, and the results showed that Naa10p inhibit cell wound healing, migration, and invasion. In summary, our study illustrated that the expression of Naa10p had a potential value for predicting the progression of OSCC and prognosis of OSCC patients.
[Mh] Termos MeSH primário: Carcinoma de Células Escamosas/genética
Carcinoma de Células Escamosas/patologia
Expressão Gênica
Neoplasias Bucais/genética
Neoplasias Bucais/patologia
Acetiltransferase N-Terminal A/genética
Acetiltransferase N-Terminal E/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
Biomarcadores Tumorais
Carcinoma de Células Escamosas/mortalidade
Carcinoma de Células Escamosas/terapia
Linhagem Celular Tumoral
Movimento Celular
Terapia Combinada
Feminino
Seres Humanos
Estimativa de Kaplan-Meier
Linfonodos/patologia
Metástase Linfática
Masculino
Meia-Idade
Neoplasias Bucais/mortalidade
Neoplasias Bucais/terapia
Gradação de Tumores
Estadiamento de Neoplasias
Prognóstico
Modelos de Riscos Proporcionais
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Recidiva
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (RNA, Messenger); EC 2.3.1.88 (N-Terminal Acetyltransferase A); EC 2.3.1.88 (N-Terminal Acetyltransferase E); EC 2.3.1.88 (NAA10 protein, human)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:171111
[Lr] Data última revisão:
171111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151215
[St] Status:MEDLINE
[do] DOI:10.1007/s13277-015-4563-z


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[PMID]:26646451
[Au] Autor:Yang H; Li Q; Niu J; Li B; Jiang D; Wan Z; Yang Q; Jiang F; Wei P; Bai S
[Ad] Endereço:The First Affiliated Hospital of Kunming Medical University, Kunming, Yunnan, China.
[Ti] Título:microRNA-342-5p and miR-608 inhibit colon cancer tumorigenesis by targeting NAA10.
[So] Source:Oncotarget;7(3):2709-20, 2016 Jan 19.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:miRNAs have been shown to play pivotal roles in the establishment and progression of colon cancer, but their underlying mechanisms are not fully understood. N-acetyltransferase NAA10 participates in many cellular processes, including tumorigenesis. Here we showed that miR-342-5p and miR-608 suppressed the tumorigenesis of colon cancer cells in vitro and in vivo by targeting NAA10 mRNA for degradation. Overexpression of miR-342-5p or miR-608 decreased NAA10 mRNA and protein levels and thereby suppressed cell proliferation, migration, and cell-cycle progression, as well as promoted apoptosis in SW480 and SW620 cells. More importantly, miR-342-5p and miR-608 significantly decreased the tumorigenic capacity of SW480 and SW620 cells in a mouse xenograft model. We also observed an inverse correlation between the expression of NAA10 and that of both miRNAs. Our results implicate miR-342-5p and miR-608 in colon cancer development and unveil the underlying mechanism of this phenomenon, which involves NAA10.
[Mh] Termos MeSH primário: Transformação Celular Neoplásica/genética
Neoplasias do Colo/genética
Regulação Neoplásica da Expressão Gênica
MicroRNAs/genética
Acetiltransferase N-Terminal A/genética
Acetiltransferase N-Terminal E/genética
[Mh] Termos MeSH secundário: Animais
Apoptose/genética
Linhagem Celular Tumoral
Proliferação Celular/genética
Neoplasias do Colo/patologia
Seres Humanos
Camundongos
Camundongos SCID
Acetiltransferase N-Terminal A/metabolismo
Acetiltransferase N-Terminal E/metabolismo
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (MIRN342 microRNA, human); 0 (MIRN608 microRNA, human); 0 (MicroRNAs); EC 2.3.1.88 (N-Terminal Acetyltransferase A); EC 2.3.1.88 (N-Terminal Acetyltransferase E); EC 2.3.1.88 (NAA10 protein, human)
[Em] Mês de entrada:1611
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151210
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.6458



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