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Pesquisa : D08.811.913.050.134.423.300 [Categoria DeCS]
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  1 / 18 MEDLINE  
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[PMID]:29247799
[Au] Autor:Varland S; Myklebust LM; Goksøyr SØ; Glomnes N; Torsvik J; Varhaug JE; Arnesen T
[Ad] Endereço:Department of Molecular Biology, University of Bergen, Thormøhlensgate 55, 5006 Bergen, Norway.
[Ti] Título:Identification of an alternatively spliced nuclear isoform of human N-terminal acetyltransferase Naa30.
[So] Source:Gene;644:27-37, 2018 Feb 20.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:N-terminal acetylation is a highly abundant and important protein modification in eukaryotes catalyzed by N-terminal acetyltransferases (NATs). In humans, six different NATs have been identified (NatA-NatF), each composed of individual subunits and acetylating a distinct set of substrates. Along with most NATs, NatC acts co-translationally at the ribosome. The NatC complex consists of the catalytic subunit Naa30 and the auxiliary subunits Naa35 and Naa38, and can potentially Nt-acetylate cytoplasmic proteins when the initiator methionine is followed by a bulky hydrophobic/amphipathic residue at position 2. Here, we have identified a splice variant of human NAA30, which encodes a truncated protein named Naa30 . The splice variant was abundantly present in thyroid cancer tissues and in several different human cancer cell lines. Surprisingly, Naa30 localized predominantly to the nucleus, as opposed to annotated Naa30 which has a cytoplasmic localization. Full-length Naa30 acetylated a classical NatC substrate peptide in vitro, whereas no significant NAT activity was detected for Naa30 Due to the nuclear localization, we also examined acetyltransferase activity towards lysine residues. Neither full-length Naa30 nor Naa30 displayed any lysine acetyltransferase activity. Overexpression of full-length Naa30 increased cell viability via inhibition of apoptosis. In contrast, Naa30 did not exert an anti-apoptotic effect. In sum, we identified a novel and widely expressed Naa30 isoform with a potential non-catalytic role in the nucleus.
[Mh] Termos MeSH primário: Núcleo Celular/genética
Acetiltransferase N-Terminal C/genética
Acetiltransferases N-Terminal/genética
Isoformas de Proteínas/genética
Processamento de RNA/genética
[Mh] Termos MeSH secundário: Acetilação
Sequência de Aminoácidos
Linhagem Celular
Linhagem Celular Tumoral
Sobrevivência Celular/genética
Células HEK293
Células HeLa
Seres Humanos
Lisina/genética
Células MCF-7
Processamento de Proteína Pós-Traducional/genética
Ribossomos/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protein Isoforms); EC 2.3.1.88 (N-Terminal Acetyltransferase C); EC 2.3.1.88 (N-Terminal Acetyltransferases); EC 2.3.1.88 (NAA30 protein, human); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180119
[Lr] Data última revisão:
180119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171217
[St] Status:MEDLINE


  2 / 18 MEDLINE  
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[PMID]:27694331
[Au] Autor:Van Damme P; Kalvik TV; Starheim KK; Jonckheere V; Myklebust LM; Menschaert G; Varhaug JE; Gevaert K; Arnesen T
[Ad] Endereço:From the ‡Medical Biotechnology Center, VIB, B-9000 Ghent, Belgium; petra.vandamme@vib-ugent.be.
[Ti] Título:A Role for Human N-alpha Acetyltransferase 30 (Naa30) in Maintaining Mitochondrial Integrity.
[So] Source:Mol Cell Proteomics;15(11):3361-3372, 2016 Nov.
[Is] ISSN:1535-9484
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:N-terminal acetylation (Nt-acetylation) by N-terminal acetyltransferases (NATs) is one of the most common protein modifications in eukaryotes. The NatC complex represents one of three major NATs of which the substrate profile remains largely unexplored. Here, we defined the in vivo human NatC Nt-acetylome on a proteome-wide scale by combining knockdown of its catalytic subunit Naa30 with positional proteomics. We identified 46 human NatC substrates, expanding our current knowledge on the substrate repertoire of NatC which now includes proteins harboring Met-Leu, Met-Ile, Met-Phe, Met-Trp, Met-Val, Met-Met, Met-His and Met-Lys N termini. Upon Naa30 depletion the expression levels of several organellar proteins were found reduced, in particular mitochondrial proteins, some of which were found to be NatC substrates. Interestingly, knockdown of Naa30 induced the loss of mitochondrial membrane potential and fragmentation of mitochondria. In conclusion, NatC Nt-acetylates a large variety of proteins and is essential for mitochondrial integrity and function.
[Mh] Termos MeSH primário: Proteínas Mitocondriais/metabolismo
Acetiltransferase N-Terminal C/genética
Acetiltransferase N-Terminal C/metabolismo
Proteômica/métodos
[Mh] Termos MeSH secundário: Acetilação
Linhagem Celular Tumoral
Técnicas de Silenciamento de Genes
Células HeLa
Seres Humanos
Ligação Proteica
Mapas de Interação de Proteínas
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Mitochondrial Proteins); EC 2.3.1.88 (N-Terminal Acetyltransferase C); EC 2.3.1.88 (NAA30 protein, human)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161004
[St] Status:MEDLINE


  3 / 18 MEDLINE  
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[PMID]:27376574
[Au] Autor:Li Y; Oosting M; Deelen P; Ricaño-Ponce I; Smeekens S; Jaeger M; Matzaraki V; Swertz MA; Xavier RJ; Franke L; Wijmenga C; Joosten LA; Kumar V; Netea MG
[Ad] Endereço:University of Groningen, University Medical Center Groningen, Department of Genetics, Groningen, the Netherlands.
[Ti] Título:Inter-individual variability and genetic influences on cytokine responses to bacteria and fungi.
[So] Source:Nat Med;22(8):952-60, 2016 Aug.
[Is] ISSN:1546-170X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Little is known about the inter-individual variation of cytokine responses to different pathogens in healthy individuals. To systematically describe cytokine responses elicited by distinct pathogens and to determine the effect of genetic variation on cytokine production, we profiled cytokines produced by peripheral blood mononuclear cells from 197 individuals of European origin from the 200 Functional Genomics (200FG) cohort in the Human Functional Genomics Project (http://www.humanfunctionalgenomics.org), obtained over three different years. We compared bacteria- and fungi-induced cytokine profiles and found that most cytokine responses were organized around a physiological response to specific pathogens, rather than around a particular immune pathway or cytokine. We then correlated genome-wide single-nucleotide polymorphism (SNP) genotypes with cytokine abundance and identified six cytokine quantitative trait loci (QTLs). Among them, a cytokine QTL at the NAA35-GOLM1 locus markedly modulated interleukin (IL)-6 production in response to multiple pathogens and was associated with susceptibility to candidemia. Furthermore, the cytokine QTLs that we identified were enriched among SNPs previously associated with infectious diseases and heart diseases. These data reveal and begin to explain the variability in cytokine production by human immune cells in response to pathogens.
[Mh] Termos MeSH primário: Bactérias/imunologia
Citocinas/imunologia
Fungos/imunologia
Variação Genética
Imunidade Inata/imunologia
Leucócitos Mononucleares/imunologia
[Mh] Termos MeSH secundário: Adulto
Idoso
Aspergillus fumigatus/imunologia
Bacteroides fragilis/imunologia
Candida albicans/imunologia
Candidemia/imunologia
Cromossomos Humanos Par 1/genética
Cromossomos Humanos Par 7/genética
Escherichia coli/imunologia
Grupo com Ancestrais do Continente Europeu/genética
Feminino
Perfilação da Expressão Gênica
Genótipo
Seres Humanos
Fenômenos Imunogenéticos
Individualidade
Interleucina-6/imunologia
Masculino
Proteínas de Membrana/genética
Meia-Idade
Mycobacterium tuberculosis/imunologia
Acetiltransferase N-Terminal C/genética
Fenótipo
Polimorfismo de Nucleotídeo Único
Locos de Características Quantitativas
Staphylococcus aureus/imunologia
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytokines); 0 (GOLM1 protein, human); 0 (IL6 protein, human); 0 (Interleukin-6); 0 (Membrane Proteins); EC 2.3.1.88 (N-Terminal Acetyltransferase C); EC 2.3.1.88 (NAA35 protein, human)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160705
[St] Status:MEDLINE
[do] DOI:10.1038/nm.4139


  4 / 18 MEDLINE  
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[PMID]:27075776
[Au] Autor:Zhao J; Noon SE; Krantz ID; Wu Y
[Ti] Título:A de novo interstitial deletion of 7q31.2q31.31 identified in a girl with developmental delay and hearing loss.
[So] Source:Am J Med Genet C Semin Med Genet;172(2):102-8, 2016 Jun.
[Is] ISSN:1552-4876
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We report on a 4-year-old female who presented with unilateral sensorineural hearing loss and a concern for developmental delay. A genome-wide SNP array analysis was performed and revealed a de novo 3.2 Mb interstitial deletion of chromosome 7q31.2q31.31. This region contains thirteen protein-encoding genes. It is unknown whether haploinsufficiency of any of these genes is responsible for the clinical features of our patient. We reviewed, the clinical phenotype of a previously published 7q31.3 deletion patient and 18 additional patients with overlapping 7q31 deletions listed in the DECIPHER database. The most consistent feature in these patients and our proband is delayed speech and language development. Hearing loss is presented both in our proband and the published 7q31.3 patient. Our study suggests that a small region on chromosome 7q31.3 encompassing four genes, CFTR, CTTNBP2, NAA38, and ANKRD7, may represent a new locus for congenital hearing loss and/or speech development. © 2016 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Deleção Cromossômica
Deficiências do Desenvolvimento/genética
Perda Auditiva Neurossensorial/genética
[Mh] Termos MeSH secundário: Proteínas de Transporte/genética
Pré-Escolar
Cromossomos Humanos Par 7/genética
Regulador de Condutância Transmembrana em Fibrose Cística/genética
Feminino
Genoma Humano
Seres Humanos
Acetiltransferase N-Terminal C/genética
Proteínas do Tecido Nervoso/genética
Polimorfismo de Nucleotídeo Único
Proteínas/genética
Ribonucleoproteína Nuclear Pequena U4-U6/genética
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ANKRD7 protein, human); 0 (CFTR protein, human); 0 (CTTNBP2 protein, human); 0 (Carrier Proteins); 0 (NAA38 protein, human); 0 (Nerve Tissue Proteins); 0 (Proteins); 0 (Ribonucleoprotein, U4-U6 Small Nuclear); 126880-72-6 (Cystic Fibrosis Transmembrane Conductance Regulator); EC 2.3.1.88 (N-Terminal Acetyltransferase C)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171003
[Lr] Data última revisão:
171003
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160415
[St] Status:MEDLINE
[do] DOI:10.1002/ajmg.c.31488


  5 / 18 MEDLINE  
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[PMID]:26292663
[Au] Autor:Mughal AA; Grieg Z; Skjellegrind H; Fayzullin A; Lamkhannat M; Joel M; Ahmed MS; Murrell W; Vik-Mo EO; Langmoen IA; Stangeland B
[Ad] Endereço:Vilhelm Magnus Laboratory for Neurosurgical Research, Institute for Surgical Research and Department of Neurosurgery, Oslo University Hospital, Oslo, Norway. awaisam@gmail.com.
[Ti] Título:Knockdown of NAT12/NAA30 reduces tumorigenic features of glioblastoma-initiating cells.
[So] Source:Mol Cancer;14:160, 2015 Aug 21.
[Is] ISSN:1476-4598
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Glioblastoma (GBM) is the most common primary brain malignancy and confers a dismal prognosis. GBMs harbor glioblastoma-initiating cells (GICs) that drive tumorigenesis and contribute to therapeutic resistance and tumor recurrence. Consequently, there is a strong rationale to target this cell population in order to develop new molecular therapies against GBM. Accumulating evidence indicates that Nα-terminal acetyltransferases (NATs), that are dysregulated in numerous human cancers, can serve as therapeutic targets. METHODS: Microarrays were used to study the expression of several NATs including NAT12/NAA30 in clinical samples and stem cell cultures. The expression of NAT12/NAA30 was analyzed using qPCR, immunolabeling and western blot. We conducted shRNA-mediated knockdown of NAT12/NAA30 gene in GICs and studied the effects on cell viability, sphere-formation and hypoxia sensitivity. Intracranial transplantation to SCID mice enabled us to investigate the effects of NAT12/NAA30 depletion in vivo. Using microarrays we identified genes and biochemical pathways whose expression was altered upon NAT12/NAA30 down-regulation. RESULTS: While decreased expression of the distal 3'UTR of NAT12/NAA30 was generally observed in GICs and GBMs, this gene was strongly up-regulated at the protein level in GBM and GICs. The increased protein levels were not caused by increased levels of the steady state mRNA but rather by other mechanisms. Also, shorter 3'UTR of NAT12/NAA30 correlated with poor survival in glioma patients. As well, we observed previously not described nuclear localization of this typically cytoplasmic protein. When compared to non-silencing controls, cells featuring NAT12/NAA30 knockdown exhibited reduced cell viability, sphere-forming ability, and mitochondrial hypoxia tolerance. Intracranial transplantation showed that knockdown of NAT12/NAA30 resulted in prolonged animal survival. Microarray analysis of the knockdown cultures showed reduced levels of HIF1α and altered expression of several other genes involved in the hypoxia response. Furthermore, NAT12/NAA30 knockdown correlated with expressional dysregulation of genes involved in the p53 pathway, ribosomal assembly and cell proliferation. Western blot analysis revealed reduction of HIF1α, phospho-MTOR(Ser2448) and higher levels of p53 and GFAP in these cultures. CONCLUSION: NAT12/NAA30 plays an important role in growth and survival of GICs possibly by regulating hypoxia response (HIF1α), levels of p-MTOR (Ser2448) and the p53 pathway.
[Mh] Termos MeSH primário: Glioblastoma/genética
Subunidade alfa do Fator 1 Induzível por Hipóxia/genética
Acetiltransferase N-Terminal C/biossíntese
Proteínas de Neoplasias/biossíntese
Serina-Treonina Quinases TOR/genética
Proteína Supressora de Tumor p53/genética
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Proliferação Celular/genética
Feminino
Regulação Neoplásica da Expressão Gênica
Técnicas de Silenciamento de Genes
Glioblastoma/patologia
Seres Humanos
Subunidade alfa do Fator 1 Induzível por Hipóxia/biossíntese
Masculino
Camundongos
Acetiltransferase N-Terminal C/genética
Células-Tronco Neurais/metabolismo
Células-Tronco Neurais/patologia
Prognóstico
RNA Mensageiro/biossíntese
Proteína Supressora de Tumor p53/biossíntese
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (HIF1A protein, human); 0 (Hypoxia-Inducible Factor 1, alpha Subunit); 0 (Neoplasm Proteins); 0 (RNA, Messenger); 0 (TP53 protein, human); 0 (Tumor Suppressor Protein p53); EC 2.3.1.88 (N-Terminal Acetyltransferase C); EC 2.3.1.88 (NAA30 protein, human); EC 2.7.1.1 (MTOR protein, human); EC 2.7.1.1 (TOR Serine-Threonine Kinases)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150822
[St] Status:MEDLINE
[do] DOI:10.1186/s12943-015-0432-z


  6 / 18 MEDLINE  
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[PMID]:25330323
[Au] Autor:Warnhoff K; Murphy JT; Kumar S; Schneider DL; Peterson M; Hsu S; Guthrie J; Robertson JD; Kornfeld K
[Ad] Endereço:Department of Developmental Biology, Washington University School of Medicine, St. Louis, Missouri, United States of America.
[Ti] Título:The DAF-16 FOXO transcription factor regulates natc-1 to modulate stress resistance in Caenorhabditis elegans, linking insulin/IGF-1 signaling to protein N-terminal acetylation.
[So] Source:PLoS Genet;10(10):e1004703, 2014 Oct.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The insulin/IGF-1 signaling pathway plays a critical role in stress resistance and longevity, but the mechanisms are not fully characterized. To identify genes that mediate stress resistance, we screened for C. elegans mutants that can tolerate high levels of dietary zinc. We identified natc-1, which encodes an evolutionarily conserved subunit of the N-terminal acetyltransferase C (NAT) complex. N-terminal acetylation is a widespread modification of eukaryotic proteins; however, relatively little is known about the biological functions of NATs. We demonstrated that loss-of-function mutations in natc-1 cause resistance to a broad-spectrum of physiologic stressors, including multiple metals, heat, and oxidation. The C. elegans FOXO transcription factor DAF-16 is a critical target of the insulin/IGF-1 signaling pathway that mediates stress resistance, and DAF-16 is predicted to directly bind the natc-1 promoter. To characterize the regulation of natc-1 by DAF-16 and the function of natc-1 in insulin/IGF-1 signaling, we analyzed molecular and genetic interactions with key components of the insulin/IGF-1 pathway. natc-1 mRNA levels were repressed by DAF-16 activity, indicating natc-1 is a physiological target of DAF-16. Genetic studies suggested that natc-1 functions downstream of daf-16 to mediate stress resistance and dauer formation. Based on these findings, we hypothesize that natc-1 is directly regulated by the DAF-16 transcription factor, and natc-1 is a physiologically significant effector of the insulin/IGF-1 signaling pathway that mediates stress resistance and dauer formation. These studies identify a novel biological function for natc-1 as a modulator of stress resistance and dauer formation and define a functionally significant downstream effector of the insulin/IGF-1 signaling pathway. Protein N-terminal acetylation mediated by the NatC complex may play an evolutionarily conserved role in regulating stress resistance.
[Mh] Termos MeSH primário: Proteínas de Caenorhabditis elegans/metabolismo
Caenorhabditis elegans/fisiologia
Fatores de Transcrição Forkhead/metabolismo
Insulina/metabolismo
Acetiltransferase N-Terminal C/metabolismo
Estresse Fisiológico
[Mh] Termos MeSH secundário: Acetilação
Acetiltransferases
Sequência de Aminoácidos
Animais
Animais Geneticamente Modificados
Caenorhabditis elegans/efeitos dos fármacos
Caenorhabditis elegans/genética
Caenorhabditis elegans/metabolismo
Proteínas de Caenorhabditis elegans/genética
Fatores de Transcrição Forkhead/genética
Regulação da Expressão Gênica no Desenvolvimento
Fator de Crescimento Insulin-Like I/metabolismo
Dados de Sequência Molecular
Mutação
Acetiltransferase N-Terminal C/genética
Transdução de Sinais
Zinco/metabolismo
Zinco/toxicidade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (Forkhead Transcription Factors); 0 (Insulin); 0 (daf-16 protein, C elegans); 67763-96-6 (Insulin-Like Growth Factor I); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.88 (N-Terminal Acetyltransferase C); EC 2.3.1.88 (NATC-1 protein, C elegans); J41CSQ7QDS (Zinc)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141021
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1004703


  7 / 18 MEDLINE  
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[PMID]:24243830
[Au] Autor:Zhang H; Lin W; Kannan K; Luo L; Li J; Chao PW; Wang Y; Chen YP; Gu J; Yen L
[Ad] Endereço:Department of Integrative Oncology, Affiliated Cancer Hospital, Shantou University Medical College, Shantou, Guangdong, China.
[Ti] Título:Aberrant chimeric RNA GOLM1-MAK10 encoding a secreted fusion protein as a molecular signature for human esophageal squamous cell carcinoma.
[So] Source:Oncotarget;4(11):2135-43, 2013 Nov.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:It is increasingly recognized that chimeric RNAs may exert a novel layer of cellular complexity that contributes to oncogenesis and cancer progression, and could be utilized as molecular biomarkers and therapeutic targets. To date yet no fusion chimeric RNAs have been identified in esophageal cancer, the 6th most frequent cause of cancer death in the world. While analyzing the expression of 32 recurrent cancer chimeric RNAs in esophageal squamous cell carcinoma (ESCC) from patients and cancer cell lines, we identified GOLM1-MAK10, as a highly cancer-enriched chimeric RNA in ESCC. In situ hybridization revealed that the expression of the chimera is largely restricted to cancer cells in patient tumors, and nearly undetectable in non-neoplastic esophageal tissue from normal subjects. The aberrant chimera closely correlated with histologic differentiation and lymph node metastasis. Furthermore, we demonstrate that chimera GOLM1-MAK10 encodes a secreted fusion protein. Mechanistic studies reveal that GOLM1-MAK10 is likely derived from transcription read-through/splicing rather than being generated from a fusion gene. Collectively, these findings provide novel insights into the molecular mechanism involved in ESCC and provide a novel potential target for future therapies. The secreted fusion protein translated from GOLM1-MAK10 could also serve as a unique protein signature detectable by standard non-invasive assays. These observations are critical as there is no clinically useful molecular signature available for detecting this deadly disease or monitoring the treatment response.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/genética
Carcinoma de Células Escamosas/genética
Neoplasias Esofágicas/genética
Proteínas de Membrana/genética
Acetiltransferase N-Terminal C/genética
Proteínas de Fusão Oncogênicas/genética
RNA/genética
[Mh] Termos MeSH secundário: Idoso
Sequência de Bases
Quimerismo
Estudos de Coortes
Feminino
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Hibridização In Situ
Masculino
Proteínas de Membrana/metabolismo
Meia-Idade
Acetiltransferase N-Terminal C/metabolismo
Proteínas de Fusão Oncogênicas/metabolismo
Prognóstico
Transcriptoma
Transfecção
[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 (Biomarkers, Tumor); 0 (GOLM1 protein, human); 0 (Membrane Proteins); 0 (Oncogene Proteins, Fusion); 63231-63-0 (RNA); EC 2.3.1.88 (N-Terminal Acetyltransferase C)
[Em] Mês de entrada:1409
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131119
[St] Status:MEDLINE


  8 / 18 MEDLINE  
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[PMID]:23613772
[Au] Autor:Aksnes H; Osberg C; Arnesen T
[Ad] Endereço:Department of Molecular Biology, University of Bergen, Bergen, Norway.
[Ti] Título:N-terminal acetylation by NatC is not a general determinant for substrate subcellular localization in Saccharomyces cerevisiae.
[So] Source:PLoS One;8(4):e61012, 2013.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:N-terminal acetylation has been suggested to play a role in the subcellular targeting of proteins, in particular those acetylated by the N-terminal acetyltransferase complex NatC. Based on previous positional proteomics data revealing N-terminal acetylation status and the predicted NAT substrate classes, we selected 13 suitable NatC substrates for subcellular localization studies in Saccharomyces cerevisiae. Fluorescence microscopy analysis of GFP-tagged candidates in the presence or absence of the NatC catalytic subunit Naa30 (Mak3) revealed unaltered localization patterns for all 13 candidates, thus arguing against a general role for the N-terminal acetyl group as a localization determinant. Furthermore, all organelle-localized substrates indicated undisrupted structures, thus suggesting that absence of NatC acetylation does not have a vast effect on organelle morphology in yeast.
[Mh] Termos MeSH primário: Espaço Intracelular/metabolismo
Acetiltransferase N-Terminal C/metabolismo
Saccharomyces cerevisiae/citologia
Saccharomyces cerevisiae/enzimologia
[Mh] Termos MeSH secundário: Acetilação
Sequência de Aminoácidos
Genômica
Proteínas de Fluorescência Verde/metabolismo
Transporte Proteico
Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
147336-22-9 (Green Fluorescent Proteins); EC 2.3.1.88 (N-Terminal Acetyltransferase C)
[Em] Mês de entrada:1311
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130425
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0061012


  9 / 18 MEDLINE  
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[PMID]:22875987
[Au] Autor:Novotny I; Podolská K; Blazíková M; Valásek LS; Svoboda P; Stanek D
[Ad] Endereço:Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Prague, Czech Republic.
[Ti] Título:Nuclear LSm8 affects number of cytoplasmic processing bodies via controlling cellular distribution of Like-Sm proteins.
[So] Source:Mol Biol Cell;23(19):3776-85, 2012 Oct.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Processing bodies (P-bodies) are dynamic cytoplasmic structures involved in mRNA degradation, but the mechanism that governs their formation is poorly understood. In this paper, we address a role of Like-Sm (LSm) proteins in formation of P-bodies and provide evidence that depletion of nuclear LSm8 increases the number of P-bodies, while LSm8 overexpression leads to P-body loss. We show that LSm8 knockdown causes relocalization of LSm4 and LSm6 proteins to the cytoplasm and suggest that LSm8 controls nuclear accumulation of all LSm2-7 proteins. We propose a model in which redistribution of LSm2-7 to the cytoplasm creates new binding sites for other P-body components and nucleates new, microscopically visible structures. The model is supported by prolonged residence of two P-body proteins, DDX6 and Ago2, in P-bodies after LSm8 depletion, which indicates stronger interactions between these proteins and P-bodies. Finally, an increased number of P-bodies has negligible effects on microRNA-mediated translation repression and nonsense mediated decay, further supporting the view that the function of proteins localized in P-bodies is independent of visible P-bodies.
[Mh] Termos MeSH primário: Núcleo Celular/metabolismo
Grânulos Citoplasmáticos/metabolismo
Acetiltransferase N-Terminal C/fisiologia
Processamento Pós-Transcricional do RNA
Ribonucleoproteína Nuclear Pequena U4-U6/fisiologia
[Mh] Termos MeSH secundário: Autoantígenos/metabolismo
RNA Helicases DEAD-box/metabolismo
Seres Humanos
Microscopia de Fluorescência
Acetiltransferase N-Terminal C/metabolismo
Transporte Proteico
Proteínas Proto-Oncogênicas/metabolismo
Proteínas de Ligação a RNA/metabolismo
Proteínas Recombinantes de Fusão/metabolismo
Ribonucleoproteína Nuclear Pequena U4-U6/metabolismo
Ribonucleoproteínas Nucleares Pequenas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Autoantigens); 0 (NAA38 protein, human); 0 (Proto-Oncogene Proteins); 0 (RNA-Binding Proteins); 0 (Recombinant Fusion Proteins); 0 (Ribonucleoprotein, U4-U6 Small Nuclear); 0 (Ribonucleoproteins, Small Nuclear); 0 (autoantigen GW182, human); EC 2.3.1.88 (N-Terminal Acetyltransferase C); EC 3.6.1.- (DDX6 protein, human); EC 3.6.4.13 (DEAD-box RNA Helicases)
[Em] Mês de entrada:1302
[Cu] Atualização por classe:150224
[Lr] Data última revisão:
150224
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120810
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E12-02-0085


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[PMID]:21562219
[Au] Autor:Benjamin JJ; Poon PP; Drysdale JD; Wang X; Singer RA; Johnston GC
[Ad] Endereço:Department of Microbiology & Immunology, Dalhousie University, Halifax, Nova Scotia, Canada B3H 1X5.
[Ti] Título:Dysregulated Arl1, a regulator of post-Golgi vesicle tethering, can inhibit endosomal transport and cell proliferation in yeast.
[So] Source:Mol Biol Cell;22(13):2337-47, 2011 Jul 01.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Small monomeric G proteins regulated in part by GTPase-activating proteins (GAPs) are molecular switches for several aspects of vesicular transport. The yeast Gcs1 protein is a dual-specificity GAP for ADP-ribosylation factor (Arf) and Arf-like (Arl)1 G proteins, and also has GAP-independent activities. The absence of Gcs1 imposes cold sensitivity for growth and endosomal transport; here we present evidence that dysregulated Arl1 may cause these impairments. We show that gene deletions affecting the Arl1 or Ypt6 vesicle-tethering pathways prevent Arl1 activation and membrane localization, and restore growth and trafficking in the absence of Gcs1. A mutant version of Gcs1 deficient for both ArfGAP and Arl1GAP activity in vitro still allows growth and endosomal transport, suggesting that the function of Gcs1 that is required for these processes is independent of GAP activity. We propose that, in the absence of this GAP-independent regulation by Gcs1, the resulting dysregulated Arl1 prevents growth and impairs endosomal transport at low temperatures. In cells with dysregulated Arl1, an increased abundance of the Arl1 effector Imh1 restores growth and trafficking, and does so through Arl1 binding. Protein sequestration at the trans-Golgi membrane by dysregulated, active Arl1 may therefore be the mechanism of inhibition.
[Mh] Termos MeSH primário: Complexo de Golgi/metabolismo
Proteínas Monoméricas de Ligação ao GTP/metabolismo
Corpos Multivesiculares/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Proteínas de Transporte Vesicular/metabolismo
Rede trans-Golgi/metabolismo
[Mh] Termos MeSH secundário: Fatores de Ribosilação do ADP/metabolismo
Aminoácido N-Acetiltransferase/metabolismo
Temperatura Baixa
Proteínas de Ligação a DNA/genética
Proteínas de Ligação a DNA/metabolismo
Endocitose/fisiologia
Proteínas de Ligação ao GTP/metabolismo
Proteínas Ativadoras de GTPase/genética
Proteínas Ativadoras de GTPase/metabolismo
Complexo de Golgi/genética
Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
Proteínas Monoméricas de Ligação ao GTP/genética
Acetiltransferase N-Terminal C
Ligação Proteica
Transporte Proteico
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/crescimento & desenvolvimento
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Transporte Vesicular/genética
Rede trans-Golgi/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (GCS1 protein, S cerevisiae); 0 (GTPase-Activating Proteins); 0 (IMH1 protein, S cerevisiae); 0 (Membrane Proteins); 0 (Saccharomyces cerevisiae Proteins); 0 (Vesicular Transport Proteins); EC 2.3.1.1 (Amino-Acid N-Acetyltransferase); EC 2.3.1.1 (MAK31 protein, S cerevisiae); EC 2.3.1.88 (N-Terminal Acetyltransferase C); EC 3.6.1.- (ARL1 protein, S cerevisiae); EC 3.6.1.- (GTP-Binding Proteins); EC 3.6.5.2 (ADP-Ribosylation Factors); EC 3.6.5.2 (Monomeric GTP-Binding Proteins); EC 3.6.5.2 (YPT6 protein, S cerevisiae)
[Em] Mês de entrada:1112
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110513
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E10-09-0765



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