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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 / 2375 MEDLINE  
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[PMID]:28747316
[Au] Autor:Suresh S; Markossian S; Osmani AH; Osmani SA
[Ad] Endereço:Department of Molecular Genetics, The Ohio State University, Columbus, OH.
[Ti] Título:Mitotic nuclear pore complex segregation involves Nup2 in .
[So] Source:J Cell Biol;216(9):2813-2826, 2017 Sep 04.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Transport through nuclear pore complexes (NPCs) during interphase is facilitated by the nucleoporin Nup2 via its importin α- and Ran-binding domains. However, and vertebrate Nup2 also locate to chromatin during mitosis, suggestive of mitotic functions. In this study, we report that Nup2 is required for mitotic NPC inheritance in Interestingly, the role of Nup2 during mitotic NPC segregation is independent of its importin α- and Ran-binding domains but relies on a central targeting domain that is necessary for localization and viability. To test whether mitotic chromatin-associated Nup2 might function to bridge NPCs with chromatin during segregation, we provided an artificial link between NPCs and chromatin via Nup133 and histone H1. Using this approach, we bypassed the requirement of Nup2 for NPC segregation. This indicates that cells ensure accurate mitotic NPC segregation to daughter nuclei by linking mitotic DNA and NPC segregation via the mitotic specific chromatin association of Nup2.
[Mh] Termos MeSH primário: Aspergillus nidulans/metabolismo
Proteínas Fúngicas/metabolismo
Mitose
Complexo de Proteínas Formadoras de Poros Nucleares/metabolismo
Poro Nuclear/metabolismo
[Mh] Termos MeSH secundário: Aspergillus nidulans/genética
Aspergillus nidulans/crescimento & desenvolvimento
Cromatina/genética
Cromatina/metabolismo
DNA Fúngico/genética
DNA Fúngico/metabolismo
Proteínas Fúngicas/genética
Histonas/metabolismo
Microscopia de Fluorescência
Mutação
Poro Nuclear/genética
Complexo de Proteínas Formadoras de Poros Nucleares/genética
Transdução de Sinais
Fatores de Tempo
Imagem com Lapso de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chromatin); 0 (DNA, Fungal); 0 (Fungal Proteins); 0 (Histones); 0 (Nuclear Pore Complex Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201610019


  3 / 2375 MEDLINE  
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[PMID]:29237697
[Au] Autor:Roucher-Boulez F; Brac de la Perriere A; Jacquez A; Chau D; Guignat L; Vial C; Morel Y; Nicolino M; Raverot G; Pugeat M
[Ad] Endereço:Laboratoire de Biochimie et Biologie Moléculaire Grand EstUM Pathologies Endocriniennes Rénales Musculaires et Mucoviscidose, Groupement Hospitalier Est, Hospices Civils de Lyon, Bron, France florence.roucher@chu-lyon.fr.
[Ti] Título:Triple-A syndrome: a wide spectrum of adrenal dysfunction.
[So] Source:Eur J Endocrinol;178(3):199-207, 2018 Mar.
[Is] ISSN:1479-683X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: Triple-A or Allgrove syndrome is an autosomal recessive disorder due to mutations in the gene, which encodes a nucleoporin named ALADIN. It is characterized by a classical clinical triad: alacrima, achalasia and adrenal insufficiency, the canonic symptoms that are associated with progressive peripheral neuropathy. Only a few cohorts have been reported. The objective of the present study was to characterize the various spectra of adrenal function in Triple-A patients. METHODS: A retrospective clinical and biological monitoring of 14 patients (10 families) was done in a single multidisciplinary French center. All had gene sequenced and adrenal function evaluation. RESULTS: Nine different mutations were found, including one new mutation: c.755G>C, p.(Trp252Ser). Regarding adrenal function, defects of the zona fasciculata and reticularis were demonstrated by increased basal ACTH levels and low DHEAS levels in all cases regardless of the degree of glucocorticoid deficiency. In contrast, mineralocorticoid function was always conserved: i.e., normal plasma renin level associated with normal aldosterone level. The main prognostic feature was exacerbation of neuropathy and cognitive disorders. CONCLUSIONS: These data suggest that, in Triple-A patients, adrenal function can be deficient, insufficient or compensated. In our cohort after the first decade of life, there does not appear to be any degradation of adrenal function over time. However, patients with compensated adrenal function should be informed and educated to manage a glucocorticoid replacement therapy in case of stressful conditions, with no need for systematic long-term treatment.
[Mh] Termos MeSH primário: Insuficiência Adrenal/genética
Acalasia Esofágica/genética
Proteínas do Tecido Nervoso/genética
Complexo de Proteínas Formadoras de Poros Nucleares/genética
[Mh] Termos MeSH secundário: Adolescente
Insuficiência Adrenal/complicações
Insuficiência Adrenal/metabolismo
Insuficiência Adrenal/fisiopatologia
Hormônio Adrenocorticotrópico/metabolismo
Adulto
Idoso
Aldosterona/metabolismo
Criança
Transtornos Cognitivos/etiologia
Transtornos Cognitivos/fisiopatologia
Transtornos Cognitivos/psicologia
Estudos de Coortes
Sulfato de Desidroepiandrosterona/metabolismo
Progressão da Doença
Acalasia Esofágica/complicações
Acalasia Esofágica/metabolismo
Acalasia Esofágica/fisiopatologia
Feminino
França
Glucocorticoides/deficiência
Seres Humanos
Masculino
Meia-Idade
Doenças do Sistema Nervoso Periférico/etiologia
Doenças do Sistema Nervoso Periférico/fisiopatologia
Fenótipo
Prognóstico
Renina/metabolismo
Estudos Retrospectivos
Adulto Jovem
Zona Fasciculada/metabolismo
Zona Reticular/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (AAAS protein, human); 0 (Glucocorticoids); 0 (Nerve Tissue Proteins); 0 (Nuclear Pore Complex Proteins); 4964P6T9RB (Aldosterone); 57B09Q7FJR (Dehydroepiandrosterone Sulfate); 9002-60-2 (Adrenocorticotropic Hormone); EC 3.4.23.15 (Renin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171215
[St] Status:MEDLINE
[do] DOI:10.1530/EJE-17-0642


  4 / 2375 MEDLINE  
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[PMID]:29330116
[Au] Autor:Wen SH; Lin LN; Wu HJ; Yu L; Lin L; Zhu LL; Li HY; Zhang HL; Li CC
[Ad] Endereço:Department of Pediatric Pulmonology, The Second Affiliated Hospital & Yuying Children's Hospital, Wenzhou Medical University, Wenzhou 325027, PR China.
[Ti] Título:TNF-α increases Staphylococcus aureus-induced death of human alveolar epithelial cell line A549 associated with RIP3-mediated necroptosis.
[So] Source:Life Sci;195:81-86, 2018 Feb 15.
[Is] ISSN:1879-0631
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:AIM: To explore the role of tumor necrosis factor-alpha (TNF-α) on Staphylococcus aureus-induced necroptosis in alveolar epithelial cells. MAIN METHODS: The A549 alveolar epithelial cell line was pretreated with small interfering RNA (siRNA) against receptor interacting protein-3 (RIP3) and then stimulated by S. aureus, where some cells were pretreated with TNF-α or TNF-α with anti-TNF-α antibody simultaneously. A549 cell death was assessed using lactate dehydrogenase (LDH) leakage and flow cytometry analyses. The protein expressions of RIP1, RIP3, cleaved caspase-1, and cleaved caspase-8 were analyzed by western blot. KEY FINDINGS: S. aureus-induced LDH release was increased significantly by TNF-α. In addition, flow cytometry showed that TNF-α increased A549 cell apoptosis and necrosis in S. aureus-infected cell cultures. Levels of RIP3 and cleaved caspase-1 protein in A549 cells infected with S. aureus increased at 12 h post-infection, as shown by western blot. Significant additional increases in RIP3 expression were observed following the addition of TNF-α. Decreasing RIP3 levels by siRNA significantly suppressed the release of LDH induced by TNF-α and S. aureus. RIP3 siRNA also significantly suppressed A549 cell necrosis induced by S. aureus and TNF-α at 6 and 12 h post-infection as shown by flow cytometry analysis. SIGNIFICANCE: TNF-α enhances the damage of S. aureus on lung epithelial cells, and its mechanism is associated with RIP3 mediated necroptosis.
[Mh] Termos MeSH primário: Morte Celular/efeitos dos fármacos
Proteína Serina-Treonina Quinases de Interação com Receptores/fisiologia
Staphylococcus aureus/efeitos dos fármacos
Fator de Necrose Tumoral alfa/farmacologia
[Mh] Termos MeSH secundário: Células A549
Células Epiteliais Alveolares
Caspase 8/genética
Caspase 8/metabolismo
Seres Humanos
L-Lactato Desidrogenase/metabolismo
Necrose/induzido quimicamente
Necrose/patologia
Complexo de Proteínas Formadoras de Poros Nucleares/efeitos dos fármacos
Complexo de Proteínas Formadoras de Poros Nucleares/fisiologia
Proteínas de Ligação a RNA/efeitos dos fármacos
Proteínas de Ligação a RNA/fisiologia
Proteína Serina-Treonina Quinases de Interação com Receptores/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (AGFG1 protein, human); 0 (Nuclear Pore Complex Proteins); 0 (RNA-Binding Proteins); 0 (Tumor Necrosis Factor-alpha); EC 1.1.1.27 (L-Lactate Dehydrogenase); EC 2.7.11.1 (RIPK3 protein, human); EC 2.7.11.1 (Receptor-Interacting Protein Serine-Threonine Kinases); EC 3.4.22.- (CASP8 protein, human); EC 3.4.22.- (Caspase 8)
[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:180114
[St] Status:MEDLINE


  5 / 2375 MEDLINE  
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[PMID]:29269482
[Au] Autor:Franks TM; McCloskey A; Shokirev MN; Benner C; Rathore A; Hetzer MW
[Ad] Endereço:Laboratory of Molecular and Cellular Biology, Salk Institute for Biological Studies, La Jolla, California 92037, USA.
[Ti] Título:Nup98 recruits the Wdr82-Set1A/COMPASS complex to promoters to regulate H3K4 trimethylation in hematopoietic progenitor cells.
[So] Source:Genes Dev;31(22):2222-2234, 2017 11 15.
[Is] ISSN:1549-5477
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recent studies have shown that a subset of nucleoporins (Nups) can detach from the nuclear pore complex and move into the nuclear interior to regulate transcription. One such dynamic Nup, called Nup98, has been implicated in gene activation in healthy cells and has been shown to drive leukemogenesis when mutated in patients with acute myeloid leukemia (AML). Here we show that in hematopoietic cells, Nup98 binds predominantly to transcription start sites to recruit the Wdr82-Set1A/COMPASS (complex of proteins associated with Set1) complex, which is required for deposition of the histone 3 Lys4 trimethyl (H3K4me3)-activating mark. Depletion of Nup98 or Wdr82 abolishes Set1A recruitment to chromatin and subsequently ablates H3K4me3 at adjacent promoters. Furthermore, expression of a Nup98 fusion protein implicated in aggressive AML causes mislocalization of H3K4me3 at abnormal regions and up-regulation of associated genes. Our findings establish a function of Nup98 in hematopoietic gene activation and provide mechanistic insight into which Nup98 leukemic fusion proteins promote AML.
[Mh] Termos MeSH primário: Células-Tronco Hematopoéticas/metabolismo
Histona-Lisina N-Metiltransferase/metabolismo
Histonas/metabolismo
Complexo de Proteínas Formadoras de Poros Nucleares/metabolismo
Regiões Promotoras Genéticas
Ativação Transcricional
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Cromatina/metabolismo
Proteínas Cromossômicas não Histona/metabolismo
Regulação da Expressão Gênica no Desenvolvimento
Seres Humanos
Metilação
Camundongos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Chromatin); 0 (Chromosomal Proteins, Non-Histone); 0 (Histones); 0 (Nuclear Pore Complex Proteins); 0 (Wdr82 protein, mouse); 0 (nuclear pore complex protein 98); EC 2.1.1.43 (Histone-Lysine N-Methyltransferase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180202
[Lr] Data última revisão:
180202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171223
[St] Status:MEDLINE
[do] DOI:10.1101/gad.306753.117


  6 / 2375 MEDLINE  
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[PMID]:29284709
[Au] Autor:Sump B; Brickner JH
[Ad] Endereço:Department of Molecular Biosciences, Northwestern University, Evanston, Illinois 60208, USA.
[Ti] Título:Nup98 regulation of histone methylation promotes normal gene expression and may drive leukemogenesis.
[So] Source:Genes Dev;31(22):2201-2203, 2017 11 15.
[Is] ISSN:1549-5477
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nuclear pore proteins (Nups) interact with chromosomes to regulate gene expression and chromatin structure. A new study by Franks and colleagues (pp. 2222-2234) provides new mechanistic insight into the molecular basis by which Nup98 promotes gene activation in normal hematopoietic cells and how that process is altered by translocations to cause excess expression of developmental genes in leukemia.
[Mh] Termos MeSH primário: Histonas/genética
Proteínas de Fusão Oncogênicas/genética
[Mh] Termos MeSH secundário: Proteínas de Homeodomínio/genética
Leucemia/genética
Metilação
Complexo de Proteínas Formadoras de Poros Nucleares/genética
Translocação Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; REVIEW; COMMENT
[Nm] Nome de substância:
0 (Histones); 0 (Homeodomain Proteins); 0 (Nuclear Pore Complex Proteins); 0 (Oncogene Proteins, Fusion)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180131
[Lr] Data última revisão:
180131
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171230
[St] Status:MEDLINE
[do] DOI:10.1101/gad.310359.117


  7 / 2375 MEDLINE  
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[PMID]:29232718
[Au] Autor:Zhu Y; Wang B; Tang K; Hsu CC; Xie S; Du H; Yang Y; Tao WA; Zhu JK
[Ad] Endereço:Shanghai Center for Plant Stress Biology and CAS Center of Excellence for Molecular Plant Sciences, Chinese Academy of Sciences, Shanghai, China.
[Ti] Título:An Arabidopsis Nucleoporin NUP85 modulates plant responses to ABA and salt stress.
[So] Source:PLoS Genet;13(12):e1007124, 2017 12.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Several nucleoporins in the nuclear pore complex (NPC) have been reported to be involved in abiotic stress responses in plants. However, the molecular mechanism of how NPC regulates abiotic stress responses, especially the expression of stress responsive genes remains poorly understood. From a forward genetics screen using an abiotic stress-responsive luciferase reporter (RD29A-LUC) in the sickle-1 (sic-1) mutant background, we identified a suppressor caused by a mutation in NUCLEOPORIN 85 (NUP85), which exhibited reduced expression of RD29A-LUC in response to ABA and salt stress. Consistently, the ABA and salinity induced expression of several stress responsive genes such as RD29A, COR15A and COR47 was significantly compromised in nup85 mutants and other nucleoporin mutants such as nup160 and hos1. Subsequently, Immunoprecipitation and mass spectrometry analysis revealed that NUP85 is potentially associated with HOS1 and other nucleoporins within the nup107-160 complex, along with several mediator subunits. We further showed that there is a direct physical interaction between MED18 and NUP85. Similar to NUP85 mutations, MED18 mutation was also found to attenuate expression of stress responsive genes. Taken together, we not only revealed the involvement of NUP85 and other nucleoporins in regulating ABA and salt stress responses, but also uncovered a potential relation between NPC and mediator complex in modulating the gene expression in plants.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/genética
Arabidopsis/genética
Complexo de Proteínas Formadoras de Poros Nucleares/genética
Plantas Geneticamente Modificadas/genética
Estresse Fisiológico/genética
[Mh] Termos MeSH secundário: Ácido Abscísico/toxicidade
Arabidopsis/fisiologia
Regulação da Expressão Gênica de Plantas
Peptídeos e Proteínas de Sinalização Intracelular/genética
Complexo Mediador/genética
Mutação
Complexo de Proteínas Formadoras de Poros Nucleares/biossíntese
Proteínas Nucleares/genética
Pressão Osmótica
Salinidade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (COR15 protein, Arabidopsis); 0 (HOS1 protein, Arabidopsis); 0 (Intracellular Signaling Peptides and Proteins); 0 (MED18 protein, Arabidopsis); 0 (Mediator Complex); 0 (NUP85 protein, Arabidopsis); 0 (Nuclear Pore Complex Proteins); 0 (Nuclear Proteins); 0 (RD29a protein, Arabidopsis); 144906-14-9 (COR47 protein, Arabidopsis); 72S9A8J5GW (Abscisic Acid)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180111
[Lr] Data última revisão:
180111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171213
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1007124


  8 / 2375 MEDLINE  
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[PMID]:28455351
[Au] Autor:Chu DB; Gromova T; Newman TAC; Burgess SM
[Ad] Endereço:Department of Molecular and Cellular Biology, University of California, Davis, California 95616.
[Ti] Título:The Nucleoporin Nup2 Contains a Meiotic-Autonomous Region that Promotes the Dynamic Chromosome Events of Meiosis.
[So] Source:Genetics;206(3):1319-1337, 2017 07.
[Is] ISSN:1943-2631
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Meiosis is a specialized cellular program required to create haploid gametes from diploid parent cells. Homologous chromosomes pair, synapse, and recombine in a dynamic environment that accommodates gross chromosome reorganization and significant chromosome motion, which are critical for normal chromosome segregation. In , Ndj1 is a meiotic telomere-associated protein required for physically attaching telomeres to proteins embedded in the nuclear envelope. In this study, we identified additional proteins that act at the nuclear periphery from meiotic cell extracts, including Nup2, a nonessential nucleoporin with a known role in tethering interstitial chromosomal loci to the nuclear pore complex. We found that deleting affects meiotic progression and spore viability, and gives increased levels of recombination intermediates and products. We identified a previously uncharacterized 125 aa region of Nup2 that is necessary and sufficient for its meiotic function, thus behaving as a meiotic autonomous region (MAR). Nup2-MAR forms distinct foci on spread meiotic chromosomes, with a subset overlapping with Ndj1 foci. Localization of Nup2-MAR to meiotic chromosomes does not require Ndj1, nor does Ndj1 localization require Nup2, suggesting these proteins function in different pathways, and their interaction is weak or indirect. Instead, several severe synthetic phenotypes are associated with the Δ Δ double mutant, including delayed turnover of recombination joint molecules, and a failure to undergo nuclear divisions without also arresting the meiotic program. These data suggest Nup2 and Ndj1 support partially overlapping functions that promote two different levels of meiotic chromosome organization necessary to withstand a dynamic stage of the eukaryotic life cycle.
[Mh] Termos MeSH primário: Meiose
Complexo de Proteínas Formadoras de Poros Nucleares/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Proteínas de Ciclo Celular/genética
Proteínas de Ciclo Celular/metabolismo
Cromossomos Fúngicos/genética
Cromossomos Fúngicos/metabolismo
Recombinação Homóloga
Complexo de Proteínas Formadoras de Poros Nucleares/química
Complexo de Proteínas Formadoras de Poros Nucleares/genética
Domínios Proteicos
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Cell Cycle Proteins); 0 (NUP2 protein, S cerevisiae); 0 (Ndj1 protein, S cerevisiae); 0 (Nuclear Pore Complex Proteins); 0 (Saccharomyces cerevisiae Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171213
[Lr] Data última revisão:
171213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE
[do] DOI:10.1534/genetics.116.194555


  9 / 2375 MEDLINE  
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[PMID]:29065307
[Au] Autor:Martino L; Morchoisne-Bolhy S; Cheerambathur DK; Van Hove L; Dumont J; Joly N; Desai A; Doye V; Pintard L
[Ad] Endereço:Cell Cycle and Development, Institut Jacques Monod, UMR7592 CNRS - Université Paris Diderot, Sorbonne Paris Cité, Paris, France.
[Ti] Título:Channel Nucleoporins Recruit PLK-1 to Nuclear Pore Complexes to Direct Nuclear Envelope Breakdown in C. elegans.
[So] Source:Dev Cell;43(2):157-171.e7, 2017 Oct 23.
[Is] ISSN:1878-1551
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In animal cells, nuclear envelope breakdown (NEBD) is required for proper chromosome segregation. Whereas mitotic kinases have been implicated in NEBD, how they coordinate their activity to trigger this event is unclear. Here, we show that both in human cells and Caenorhabditis elegans, the Polo-like kinase 1 (PLK-1) is recruited to the nuclear pore complexes, just prior to NEBD, through its Polo-box domain (PBD). We provide evidence that PLK-1 localization to the nuclear envelope (NE) is required for efficient NEBD. We identify the central channel nucleoporins NPP-1/Nup58, NPP-4/Nup54, and NPP-11/Nup62 as the critical factors anchoring PLK-1 to the NE in C. elegans. In particular, NPP-1, NPP-4, and NPP-11 primed at multiple Polo-docking sites by Cdk1 and PLK-1 itself physically interact with the PLK-1 PBD. We conclude that nucleoporins play an unanticipated regulatory role in NEBD, by recruiting PLK-1 to the NE thereby facilitating phosphorylation of critical downstream targets.
[Mh] Termos MeSH primário: Proteínas de Caenorhabditis elegans/metabolismo
Caenorhabditis elegans/metabolismo
Proteínas de Ciclo Celular/metabolismo
Mitose/fisiologia
Membrana Nuclear/metabolismo
Complexo de Proteínas Formadoras de Poros Nucleares/metabolismo
Poro Nuclear/metabolismo
Proteínas Serina-Treonina Quinases/metabolismo
Proteínas Proto-Oncogênicas/metabolismo
[Mh] Termos MeSH secundário: Animais
Caenorhabditis elegans/genética
Caenorhabditis elegans/crescimento & desenvolvimento
Proteínas de Caenorhabditis elegans/genética
Proteínas de Ciclo Celular/genética
Núcleo Celular/genética
Núcleo Celular/metabolismo
Embrião não Mamífero/citologia
Embrião não Mamífero/metabolismo
Células HeLa
Seres Humanos
Membrana Nuclear/genética
Poro Nuclear/genética
Complexo de Proteínas Formadoras de Poros Nucleares/genética
Fosforilação
Proteínas Serina-Treonina Quinases/genética
Proteínas Proto-Oncogênicas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (Cell Cycle Proteins); 0 (Nuclear Pore Complex Proteins); 0 (Proto-Oncogene Proteins); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.1 (polo-like kinase 1)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171025
[St] Status:MEDLINE


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[PMID]:29065306
[Au] Autor:Linder MI; Köhler M; Boersema P; Weberruss M; Wandke C; Marino J; Ashiono C; Picotti P; Antonin W; Kutay U
[Ad] Endereço:Institute of Biochemistry, Department of Biology, ETH Zurich, 8093 Zurich, Switzerland.
[Ti] Título:Mitotic Disassembly of Nuclear Pore Complexes Involves CDK1- and PLK1-Mediated Phosphorylation of Key Interconnecting Nucleoporins.
[So] Source:Dev Cell;43(2):141-156.e7, 2017 Oct 23.
[Is] ISSN:1878-1551
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:During interphase, the nuclear envelope (NE) serves as a selective barrier between cytosol and nucleoplasm. When vertebrate cells enter mitosis, the NE is dismantled in the process of nuclear envelope breakdown (NEBD). Disassembly of nuclear pore complexes (NPCs) is a key aspect of NEBD, required for NE permeabilization and formation of a cytoplasmic mitotic spindle. Here, we show that both CDK1 and polo-like kinase 1 (PLK1) support mitotic NPC disintegration by hyperphosphorylation of Nup98, the gatekeeper nucleoporin, and Nup53, a central nucleoporin linking the inner NPC scaffold to the pore membrane. Multisite phosphorylation of Nup53 critically contributes to its liberation from its partner nucleoporins, including the pore membrane protein NDC1. Initial steps of NPC disassembly in semi-permeabilized cells can be reconstituted by a cocktail of mitotic kinases including cyclinB-CDK1, NIMA, and PLK1, suggesting that the unzipping of nucleoporin interactions by protein phosphorylation is an important principle underlying mitotic NE permeabilization.
[Mh] Termos MeSH primário: Proteínas de Ciclo Celular/metabolismo
Quinases Ciclina-Dependentes/metabolismo
Mitose/fisiologia
Complexo de Proteínas Formadoras de Poros Nucleares/metabolismo
Poro Nuclear/metabolismo
Proteínas Serina-Treonina Quinases/metabolismo
Proteínas Proto-Oncogênicas/metabolismo
[Mh] Termos MeSH secundário: Proteína Quinase CDC2
Proteínas de Ciclo Celular/genética
Núcleo Celular/genética
Núcleo Celular/metabolismo
Quinases Ciclina-Dependentes/genética
Células HeLa
Seres Humanos
Membrana Nuclear/genética
Membrana Nuclear/metabolismo
Poro Nuclear/genética
Complexo de Proteínas Formadoras de Poros Nucleares/genética
Fosforilação
Proteínas Serina-Treonina Quinases/genética
Proteínas Proto-Oncogênicas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Cycle Proteins); 0 (Nuclear Pore Complex Proteins); 0 (Nup98 protein, human); 0 (Proto-Oncogene Proteins); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.1 (polo-like kinase 1); EC 2.7.11.22 (CDC2 Protein Kinase); EC 2.7.11.22 (CDK1 protein, human); EC 2.7.11.22 (Cyclin-Dependent Kinases)
[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:171025
[St] Status:MEDLINE



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