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  1 / 1045 MEDLINE  
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[PMID]:29212662
[Au] Autor:Chatterjee K; Majumder S; Wan Y; Shah V; Wu J; Huang HY; Hopper AK
[Ad] Endereço:The Ohio State University Comprehensive Cancer Research Center, The Ohio State University, Columbus, Ohio 43210, USA.
[Ti] Título:Sharing the load: Mex67-Mtr2 cofunctions with Los1 in primary tRNA nuclear export.
[So] Source:Genes Dev;31(21):2186-2198, 2017 11 01.
[Is] ISSN:1549-5477
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Eukaryotic transfer RNAs (tRNAs) are exported from the nucleus, their site of synthesis, to the cytoplasm, their site of function for protein synthesis. The evolutionarily conserved ß-importin family member Los1 (Exportin-t) has been the only exporter known to execute nuclear export of newly transcribed intron-containing pre-tRNAs. Interestingly, is unessential in all tested organisms. As tRNA nuclear export is essential, we previously interrogated the budding yeast proteome to identify candidates that function in tRNA nuclear export. Here, we provide molecular, genetic, cytological, and biochemical evidence that the Mex67-Mtr2 (TAP-p15) heterodimer, best characterized for its essential role in mRNA nuclear export, cofunctions with Los1 in tRNA nuclear export. Inactivation of Mex67 or Mtr2 leads to rapid accumulation of end-matured unspliced tRNAs in the nucleus. Remarkably, merely fivefold overexpression of Mex67-Mtr2 can substitute for Los1 in Δ cells. Moreover, in vivo coimmunoprecipitation assays with tagged Mex67 document that the Mex67 binds tRNAs. Our data also show that tRNA exporters surprisingly exhibit differential tRNA substrate preferences. The existence of multiple tRNA exporters, each with different tRNA preferences, may indicate that the proteome can be regulated by tRNA nuclear export. Thus, our data show that Mex67-Mtr2 functions in primary nuclear export for a subset of yeast tRNAs.
[Mh] Termos MeSH primário: Transporte Ativo do Núcleo Celular/genética
Proteoma/genética
RNA de Transferência/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Inativação Gênica
Proteínas de Membrana Transportadoras/genética
Proteínas de Membrana Transportadoras/metabolismo
Complexo de Proteínas Formadoras de Poros Nucleares/genética
Complexo de Proteínas Formadoras de Poros Nucleares/metabolismo
Proteínas Nucleares/genética
Proteínas Nucleares/metabolismo
Proteínas de Transporte Nucleocitoplasmático/genética
Proteínas de Transporte Nucleocitoplasmático/metabolismo
Ligação Proteica
Proteínas de Ligação a RNA/genética
Proteínas de Ligação a RNA/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Los1 protein, S cerevisiae); 0 (MEX67 protein, S cerevisiae); 0 (Membrane Transport Proteins); 0 (Mtr2 protein, S cerevisiae); 0 (Nuclear Pore Complex Proteins); 0 (Nuclear Proteins); 0 (Nucleocytoplasmic Transport Proteins); 0 (Proteome); 0 (RNA-Binding Proteins); 0 (Saccharomyces cerevisiae Proteins); 9014-25-9 (RNA, Transfer)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171208
[St] Status:MEDLINE
[do] DOI:10.1101/gad.305904.117


  2 / 1045 MEDLINE  
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[PMID]:29293652
[Au] Autor:Stockum A; Snijders AP; Maertens GN
[Ad] Endereço:Imperial College London, Department of Medicine, Division of Infectious Diseases, Norfolk Place, London, United Kingdom.
[Ti] Título:USP11 deubiquitinates RAE1 and plays a key role in bipolar spindle formation.
[So] Source:PLoS One;13(1):e0190513, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Correct segregation of the mitotic chromosomes into daughter cells is a highly regulated process critical to safeguard genome stability. During M phase the spindle assembly checkpoint (SAC) ensures that all kinetochores are correctly attached before its inactivation allows progression into anaphase. Upon SAC inactivation, the anaphase promoting complex/cyclosome (APC/C) E3 ligase ubiquitinates and targets cyclin B and securin for proteasomal degradation. Here, we describe the identification of Ribonucleic Acid Export protein 1 (RAE1), a protein previously shown to be involved in SAC regulation and bipolar spindle formation, as a novel substrate of the deubiquitinating enzyme (DUB) Ubiquitin Specific Protease 11 (USP11). Lentiviral knock-down of USP11 or RAE1 in U2OS cells drastically reduces cell proliferation and increases multipolar spindle formation. We show that USP11 is associated with the mitotic spindle, does not regulate SAC inactivation, but controls ubiquitination of RAE1 at the mitotic spindle, hereby functionally modulating its interaction with Nuclear Mitotic Apparatus protein (NuMA).
[Mh] Termos MeSH primário: Proteínas Associadas à Matriz Nuclear/metabolismo
Proteínas de Transporte Nucleocitoplasmático/metabolismo
Fuso Acromático
Tioléster Hidrolases/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Proliferação Celular
Técnicas de Silenciamento de Genes
Células HEK293
Seres Humanos
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Ligação Proteica
Especificidade por Substrato
Tioléster Hidrolases/genética
Ubiquitinação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Intracellular Signaling Peptides and Proteins); 0 (Nuclear Matrix-Associated Proteins); 0 (Nucleocytoplasmic Transport Proteins); 0 (RAE1 protein, human); 0 (SPRY3 protein, human); EC 3.1.2.- (Thiolester Hydrolases); EC 3.1.2.15 (USP11 protein, human)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180221
[Lr] Data última revisão:
180221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180103
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190513


  3 / 1045 MEDLINE  
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[PMID]:29374693
[Au] Autor:Ernst BP; Mikstas C; Stöver T; Stauber R; Strieth S
[Ad] Endereço:Department of Otorhinolaryngology, University Hospital Frankfurt, Frankfurt, Germany benjamin.ernst@unimedizin-mainz.de.
[Ti] Título:Association of eIF4E and SPARC Expression with Lymphangiogenesis and Lymph Node Metastasis in Hypopharyngeal Cancer.
[So] Source:Anticancer Res;38(2):699-706, 2018 02.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIM: Head and neck squamous cell carcinomas (HNSCC) are characterized by aggressiveness, early recurrence and lymph node metastasis. Therefore, there is an urgent need to identify new biomarkers and drug targets. MATERIALS AND METHODS: Neck dissection specimens from 11 patients diagnosed with hypopharyngeal cancer were analyzed for their lymphatic vessel density (LVD) by lymphatic vessel endothelial hyaluronan receptor 1 (LYVE-1) immunostaining, expression of eukaryotic initiation factor 4E (eIF4E) and levels of secreted protein acidic and rich in cysteine (SPARC) using immunoblot analysis. RESULTS: Compared to lymph node biopsies of healthy controIs, LVD was significantly increased in metastatic lymph nodes as well as in advanced primary tumors. Overexpression of eIF4E and SPARC was demonstrated in all hypopharyngeal cancer specimens. Notably, we observed that increased LVD significantly correlated with the expression of eIF4E as well as SPARC levels. CONCLUSION: eIF4E- and SPARC-associated signaling pathways may be associated with lymphangiogenesis and could be exploited to counteract the spread of hypopharyngeal cancer cells.
[Mh] Termos MeSH primário: Neoplasias Hipofaríngeas/metabolismo
Neoplasias Hipofaríngeas/patologia
Linfangiogênese/fisiologia
Proteínas de Transporte Nucleocitoplasmático/metabolismo
Osteonectina/metabolismo
[Mh] Termos MeSH secundário: Biomarcadores Tumorais/metabolismo
Carcinoma de Células Escamosas/metabolismo
Carcinoma de Células Escamosas/patologia
Feminino
Neoplasias de Cabeça e Pescoço/metabolismo
Neoplasias de Cabeça e Pescoço/patologia
Seres Humanos
Linfonodos/metabolismo
Linfonodos/patologia
Metástase Linfática/patologia
Masculino
Meia-Idade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (EIF4ENIF1 protein, human); 0 (Nucleocytoplasmic Transport Proteins); 0 (Osteonectin); 0 (SPARC protein, human)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180208
[Lr] Data última revisão:
180208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180129
[St] Status:MEDLINE


  4 / 1045 MEDLINE  
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[PMID]:28867566
[Au] Autor:Jung YD; Lee HE; Jo A; Hiroo I; Cha HJ; Kim HS
[Ad] Endereço:Biotherapeutics Translational Research Center, Korea Research Institute of Bioscience & Biotechnology, Daejeon 34141, Republic of Korea.
[Ti] Título:Activity analysis of LTR12C as an effective regulatory element of the RAE1 gene.
[So] Source:Gene;634:22-28, 2017 Nov 15.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Ribonucleic acid export 1 (RAE1) plays an important role in the export of mature mRNAs from the nucleus to the cytoplasm. Long terminal repeats (LTRs) became integrated into the human genome during primate evolution. One such repeat element, LTR12C, lies within a predicted regulatory region located upstream of the RAE1 gene. We examined the transcriptional activity of LTR12C by using the luciferase assay, and showed that the tandem repeat region (TRR) located within LTR12C was required for its regulatory function. A bioinformatics analysis revealed that the LTR12C element had multiple transcription factor binding sites specific for nuclear transcription factor Y (NF-Y), and the promoter activity of LTR12C was significantly decreased after NF-Y knockdown. Additionally, we discovered novel data indicating that LTR12C was initially inserted into the gorilla genome. Taken together, our results reveal that the TRR of LTR12C has powerful regulatory activity due to its NF-Y binding sites, and the integration of the LTR12C element into the primate genome during evolution may have affected RAE1 transcription.
[Mh] Termos MeSH primário: Fator de Ligação a CCAAT/metabolismo
Gorilla gorilla/genética
Proteínas Associadas à Matriz Nuclear/metabolismo
Proteínas de Transporte Nucleocitoplasmático/metabolismo
Sequências Repetidas Terminais
[Mh] Termos MeSH secundário: Células A549
Animais
Sítios de Ligação
Linhagem Celular
Evolução Molecular
Regulação da Expressão Gênica
Células HCT116
Células HEK293
Células Hep G2
Seres Humanos
Regiões Promotoras Genéticas
Sequências de Repetição em Tandem
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CCAAT-Binding Factor); 0 (Nuclear Matrix-Associated Proteins); 0 (Nucleocytoplasmic Transport Proteins); 0 (RAE1 protein, human); 0 (Transcription Factors); 0 (nuclear factor Y)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170905
[St] Status:MEDLINE


  5 / 1045 MEDLINE  
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[PMID]:28864412
[Au] Autor:Zheng J; Yang J; Choe YJ; Hao X; Cao X; Zhao Q; Zhang Y; Franssens V; Hartl FU; Nyström T; Winderickx J; Liu B
[Ad] Endereço:Department of Chemistry and Molecular Biology, University of Gothenburg, S-413 90, Göteborg, Sweden; Department of Biology, Functional Biology, KU Leuven, 3001, Heverlee, Belgium.
[Ti] Título:Role of the ribosomal quality control machinery in nucleocytoplasmic translocation of polyQ-expanded huntingtin exon-1.
[So] Source:Biochem Biophys Res Commun;493(1):708-717, 2017 Nov 04.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The subcellular localization of polyQ-expanded huntingtin exon1 (Httex1) modulates polyQ toxicity in models of Huntington's disease. Using genome-wide screens in a yeast model system, we report that the ribosome quality control (RQC) machinery, recently implicated in neurodegeneration, is a key determinant for the nucleocytoplasmic distribution of Httex1-103Q. Deletion of the RQC genes, LTN1 or RQC1, caused the accumulation of Httex1-103Q in the nucleus through a process that required the CAT-tail tagging activity of Rqc2 and transport via the nuclear pore complex. We provide evidence that nuclear accumulation of Httex1-103Q enhances its cytotoxicity, suggesting that the RQC machinery plays an important role in protecting cells against the adverse effects of polyQ expansion proteins.
[Mh] Termos MeSH primário: Núcleo Celular/metabolismo
Éxons/genética
Proteína Huntingtina/genética
Proteína Huntingtina/metabolismo
Peptídeos/genética
Peptídeos/metabolismo
Ribossomos/metabolismo
[Mh] Termos MeSH secundário: Transporte Ativo do Núcleo Celular/fisiologia
Seres Humanos
Proteínas de Transporte Nucleocitoplasmático/genética
Proteínas de Transporte Nucleocitoplasmático/metabolismo
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Huntingtin Protein); 0 (Nucleocytoplasmic Transport Proteins); 0 (Peptides); 26700-71-0 (polyglutamine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170903
[St] Status:MEDLINE


  6 / 1045 MEDLINE  
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[PMID]:28771467
[Au] Autor:Chen T; van Steensel B
[Ad] Endereço:Division of Gene Regulation, Netherlands Cancer Institute, Amsterdam, The Netherlands.
[Ti] Título:Comprehensive analysis of nucleocytoplasmic dynamics of mRNA in Drosophila cells.
[So] Source:PLoS Genet;13(8):e1006929, 2017 Aug.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Eukaryotic mRNAs undergo a cycle of transcription, nuclear export, and degradation. A major challenge is to obtain a global, quantitative view of these processes. Here we measured the genome-wide nucleocytoplasmic dynamics of mRNA in Drosophila cells by metabolic labeling in combination with cellular fractionation. By mathematical modeling of these data we determined rates of transcription, export and cytoplasmic decay for 5420 genes. We characterized these kinetic rates and investigated links with mRNA features, RNA-binding proteins (RBPs) and chromatin states. We found prominent correlations between mRNA decay rate and transcript size, while nuclear export rates are linked to the size of the 3'UTR. Transcription, export and decay rates are each associated with distinct spectra of RBPs. Specific classes of genes, such as those encoding cytoplasmic ribosomal proteins, exhibit characteristic combinations of rate constants, suggesting modular control. Binding of splicing factors is associated with faster rates of export, and our data suggest coordinated regulation of nuclear export of specific functional classes of genes. Finally, correlations between rate constants suggest global coordination between the three processes. Our approach provides insights into the genome-wide nucleocytoplasmic kinetics of mRNA and should be generally applicable to other cell systems.
[Mh] Termos MeSH primário: Transporte Ativo do Núcleo Celular
Proteínas de Drosophila/genética
Drosophila/genética
Proteínas de Transporte Nucleocitoplasmático/genética
RNA Mensageiro/genética
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas
Animais
Células Cultivadas
Citoplasma/metabolismo
Drosophila/metabolismo
Proteínas de Drosophila/metabolismo
Ontologia Genética
Modelos Teóricos
Proteínas de Transporte Nucleocitoplasmático/metabolismo
RNA Mensageiro/metabolismo
Proteínas de Ligação a RNA/genética
Proteínas de Ligação a RNA/metabolismo
Análise de Sequência de RNA
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (Drosophila Proteins); 0 (Nucleocytoplasmic Transport Proteins); 0 (RNA, Messenger); 0 (RNA-Binding Proteins); 0 (Transcription Factors)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170804
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006929


  7 / 1045 MEDLINE  
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[PMID]:28760339
[Au] Autor:Koyama M; Matsuura Y
[Ad] Endereço:Division of Biological Science, Graduate School of Science, Nagoya University, Japan.
[Ti] Título:Crystal structure of importin-α3 bound to the nuclear localization signal of Ran-binding protein 3.
[So] Source:Biochem Biophys Res Commun;491(3):609-613, 2017 Sep 23.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ran-binding protein 3 (RanBP3) is a primarily nuclear Ran-binding protein that functions as an accessory factor in the Ran GTPase system. RanBP3 associates with Ran-specific nucleotide exchange factor RCC1 and enhances its catalytic activity towards Ran. RanBP3 also promotes CRM1-mediated nuclear export as well as CRM1-independent nuclear export of ß-catenin, Smad2, and Smad3. Nuclear import of RanBP3 is dependent on the nuclear import adaptor protein importin-α and, RanBP3 is imported more efficiently by importin-α3 than by other members of the importin-α family. Protein kinase signaling pathways control nucleocytoplasmic transport through phosphorylation of RanBP3 at Ser58, immediately C-terminal to the nuclear localization signal (NLS) in the N-terminal region of RanBP3. Here we report the crystal structure of human importin-α3 bound to an N-terminal fragment of human RanBP3 containing the NLS sequence that is necessary and sufficient for nuclear import. The structure reveals that RanBP3 binds to importin-α3 residues that are strictly conserved in all seven isoforms of human importin-α at the major NLS-binding site, indicating that the region of importin-α outside the NLS-binding site, possibly the autoinhibotory importin-ß1-binding domain, may be the key determinant for the preferential binding of RanBP3 to importin-α3. Computational docking simulation indicates that phosphorylation of RanBP3 at Ser58 could potentially stabilize the association of RanBP3 with importin-α through interactions between the phosphate moiety of phospho-Ser58 of RanBP3 and a cluster of basic residues (Arg96 and Lys97 in importin-α3) on armadillo repeat 1 of importin-α.
[Mh] Termos MeSH primário: Proteínas de Drosophila/química
Proteínas de Drosophila/ultraestrutura
Modelos Químicos
Simulação de Acoplamento Molecular
Sinais de Localização Nuclear/química
Proteínas Nucleares/química
Proteínas Nucleares/ultraestrutura
Proteínas de Transporte Nucleocitoplasmático/química
Proteínas de Transporte Nucleocitoplasmático/ultraestrutura
alfa Carioferinas/química
alfa Carioferinas/ultraestrutura
[Mh] Termos MeSH secundário: Sítios de Ligação
Cristalografia
Ligação Proteica
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (Kap-alpha3 protein, Drosophila); 0 (Nuclear Localization Signals); 0 (Nuclear Proteins); 0 (Nucleocytoplasmic Transport Proteins); 0 (RANBP3 protein, human); 0 (alpha Karyopherins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170911
[Lr] Data última revisão:
170911
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170802
[St] Status:MEDLINE


  8 / 1045 MEDLINE  
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[PMID]:28739693
[Au] Autor:Konagai A; Yoshimura K; Hazama S; Yamamoto N; Aoki K; Ueno T; Fujioka M; Iijima H; Kato M; Uchida M; Wada T; Inoue M; Asao T; Fuse M; Wada S; Kuramasu A; Kamei R; Takeda S; Yamamoto S; Yoshino S; Oka M; Nagano H
[Ad] Endereço:Department of Gastroenterological, Breast and Endocrine Surgery, Yamaguchi University Graduate School of Medicine, Yamaguchi, Japan.
[Ti] Título:Correlation Between NKG2DL Expression and Antitumor Effect of Protein-bound Polysaccharide-K in Tumor-bearing Mouse Models.
[So] Source:Anticancer Res;37(8):4093-4101, 2017 08.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIM: We investigated the relationship between the expression of natural killer group 2, member D ligands (NKG2DLs) and the antitumor effects of protein-bound polysaccharide-K (PSK). MATERIALS AND METHODS: PSK was administered to evaluate its effectiveness against tumor growth. The expression of Rae-1 and H60 were analyzed in multiple cell lines. RESULTS: PSK showed the highest antitumor effects in mice implanted with cells expressing neither Rae-1 nor H60. PSK had little antitumor effect in mice implanted with cells expressing both Rae-1 and H60. A correlation between the expression of NKG2DLs and the antitumor effect of PSK was observed. After PSK administration, INF-γ production in CD8 T cells increased in mice with cells expressing neither Rae-1 nor H60, but did not change in mice implanted with cells expressing both Rae-1 and H60. CONCLUSION: We demonstrated that the expression of NKG2DLs affects tumor immunity and the efficacy of immuno therapy in tumor-bearing mouse model.
[Mh] Termos MeSH primário: Proteínas Fúngicas/administração & dosagem
Antígenos de Histocompatibilidade Menor/genética
Subfamília K de Receptores Semelhantes a Lectina de Células NK/genética
Neoplasias/tratamento farmacológico
Proteínas Associadas à Matriz Nuclear/genética
Proteínas de Transporte Nucleocitoplasmático/genética
Polissacarídeos/administração & dosagem
[Mh] Termos MeSH secundário: Animais
Linfócitos T CD8-Positivos/efeitos dos fármacos
Linhagem Celular Tumoral
Regulação Neoplásica da Expressão Gênica/efeitos dos fármacos
Seres Humanos
Ligantes
Camundongos
Antígenos de Histocompatibilidade Menor/biossíntese
Subfamília K de Receptores Semelhantes a Lectina de Células NK/biossíntese
Neoplasias/genética
Neoplasias/patologia
Proteínas Associadas à Matriz Nuclear/biossíntese
Proteínas de Transporte Nucleocitoplasmático/biossíntese
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins); 0 (KLRK1 protein, human); 0 (Ligands); 0 (Minor Histocompatibility Antigens); 0 (NK Cell Lectin-Like Receptor Subfamily K); 0 (Nuclear Matrix-Associated Proteins); 0 (Nucleocytoplasmic Transport Proteins); 0 (Polysaccharides); 0 (RAE1 protein, human); 0 (minor H antigen H60); 0 (protein-bound polysaccharide K, Basidiomycetes)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE


  9 / 1045 MEDLINE  
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[PMID]:28597296
[Au] Autor:Olsen JG; Teilum K; Kragelund BB
[Ad] Endereço:Structural Biology and NMR Laboratory (SBiNLab) and the Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, 2200, Copenhagen, Denmark.
[Ti] Título:Behaviour of intrinsically disordered proteins in protein-protein complexes with an emphasis on fuzziness.
[So] Source:Cell Mol Life Sci;74(17):3175-3183, 2017 Sep.
[Is] ISSN:1420-9071
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Intrinsically disordered proteins (IDPs) do not, by themselves, fold into a compact globular structure. They are extremely dynamic and flexible, and are typically involved in signalling and transduction of information through binding to other macromolecules. The reason for their existence may lie in their malleability, which enables them to bind several different partners with high specificity. In addition, their interactions with other macromolecules can be regulated by a variable amount of chemically diverse post-translational modifications. Four kinetically and energetically different types of complexes between an IDP and another macromolecule are reviewed: (1) simple two-state binding involving a single binding site, (2) avidity, (3) allovalency and (4) fuzzy binding; the last three involving more than one site. Finally, a qualitative definition of fuzzy binding is suggested, examples are provided, and its distinction to allovalency and avidity is highlighted and discussed.
[Mh] Termos MeSH primário: Proteínas Intrinsicamente Desordenadas/metabolismo
[Mh] Termos MeSH secundário: Animais
Clatrina/química
Clatrina/metabolismo
Seres Humanos
Proteínas Intrinsicamente Desordenadas/química
Cinética
Modelos Moleculares
Proteínas Monoméricas de Montagem de Clatrina/química
Proteínas Monoméricas de Montagem de Clatrina/metabolismo
Complexo de Proteínas Formadoras de Poros Nucleares/química
Complexo de Proteínas Formadoras de Poros Nucleares/metabolismo
Proteínas de Transporte Nucleocitoplasmático/química
Proteínas de Transporte Nucleocitoplasmático/metabolismo
Ligação Proteica
Processamento de Proteína Pós-Traducional
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Clathrin); 0 (Intrinsically Disordered Proteins); 0 (Monomeric Clathrin Assembly Proteins); 0 (Nuclear Pore Complex Proteins); 0 (Nucleocytoplasmic Transport Proteins); 0 (clathrin assembly protein AP180)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170830
[Lr] Data última revisão:
170830
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170610
[St] Status:MEDLINE
[do] DOI:10.1007/s00018-017-2560-7


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[PMID]:28581441
[Au] Autor:Putz EM; Mayfosh AJ; Kos K; Barkauskas DS; Nakamura K; Town L; Goodall KJ; Yee DY; Poon IK; Baschuk N; Souza-Fonseca-Guimaraes F; Hulett MD; Smyth MJ
[Ad] Endereço:Immunology in Cancer and Infection Laboratory, QIMR Berghofer Medical Research Institute, Herston, Queensland, Australia.
[Ti] Título:NK cell heparanase controls tumor invasion and immune surveillance.
[So] Source:J Clin Invest;127(7):2777-2788, 2017 Jun 30.
[Is] ISSN:1558-8238
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:NK cells are highly efficient at preventing cancer metastasis but are infrequently found in the core of primary tumors. Here, have we demonstrated that freshly isolated mouse and human NK cells express low levels of the endo-ß-D-glucuronidase heparanase that increase upon NK cell activation. Heparanase deficiency did not affect development, differentiation, or tissue localization of NK cells under steady-state conditions. However, mice lacking heparanase specifically in NK cells (Hpsefl/fl NKp46-iCre mice) were highly tumor prone when challenged with the carcinogen methylcholanthrene (MCA). Hpsefl/fl NKp46-iCre mice were also more susceptible to tumor growth than were their littermate controls when challenged with the established mouse lymphoma cell line RMA-S-RAE-1ß, which overexpresses the NK cell group 2D (NKG2D) ligand RAE-1ß, or when inoculated with metastatic melanoma, prostate carcinoma, or mammary carcinoma cell lines. NK cell invasion of primary tumors and recruitment to the site of metastasis were strictly dependent on the presence of heparanase. Cytokine and immune checkpoint blockade immunotherapy for metastases was compromised when NK cells lacked heparanase. Our data suggest that heparanase plays a critical role in NK cell invasion into tumors and thereby tumor progression and metastases. This should be considered when systemically treating cancer patients with heparanase inhibitors, since the potential adverse effect on NK cell infiltration might limit the antitumor activity of the inhibitors.
[Mh] Termos MeSH primário: Heparina Liase/imunologia
Vigilância Imunológica
Células Matadoras Naturais/imunologia
Neoplasias Experimentais/imunologia
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Citocinas/genética
Citocinas/imunologia
Feminino
Heparina Liase/genética
Seres Humanos
Células Matadoras Naturais/patologia
Masculino
Camundongos
Camundongos Knockout
Subfamília K de Receptores Semelhantes a Lectina de Células NK/genética
Subfamília K de Receptores Semelhantes a Lectina de Células NK/imunologia
Invasividade Neoplásica/genética
Invasividade Neoplásica/imunologia
Metástase Neoplásica
Neoplasias Experimentais/genética
Neoplasias Experimentais/patologia
Proteínas Associadas à Matriz Nuclear/genética
Proteínas Associadas à Matriz Nuclear/imunologia
Proteínas de Transporte Nucleocitoplasmático/genética
Proteínas de Transporte Nucleocitoplasmático/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytokines); 0 (KLRK1 protein, human); 0 (NK Cell Lectin-Like Receptor Subfamily K); 0 (Nuclear Matrix-Associated Proteins); 0 (Nucleocytoplasmic Transport Proteins); 0 (RAE1 protein, human); EC 4.2.2.7 (Heparin Lyase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170930
[Lr] Data última revisão:
170930
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170606
[St] Status:MEDLINE



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