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Pesquisa : A11.284.430.106.279.692.630 [Categoria DeCS]
Referências encontradas : 1363 [refinar]
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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


  2 / 1363 MEDLINE  
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[PMID]:29207257
[Au] Autor:Lomakin A; Nader G; Piel M
[Ad] Endereço:King's College London, Guy's Campus, Centre for Stem Cells & Regenerative Medicine, 28th Floor, Tower Wing, Great Maze Pond, London SE1 9RT, UK; Institut Curie, PSL Research University, CNRS, UMR 144, 75005 Paris, France; Institut Pierre-Gilles de Gennes, PSL Research University, 75005 Paris, France.
[Ti] Título:Forcing Entry into the Nucleus.
[So] Source:Dev Cell;43(5):547-548, 2017 Dec 04.
[Is] ISSN:1878-1551
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nuclear pore complexes tightly regulate nucleo-cytoplasmic transport, controlling the nuclear concentration of several transcription factors. In a recent issue of Cell, Elosegui-Artola et al. (2017) show that nuclear deformation modulates the nuclear entry rates of YAP/TAZ via nuclear pore stretching, clarifying how forces affect gene transcription.
[Mh] Termos MeSH primário: Transporte Ativo do Núcleo Celular/fisiologia
Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Núcleo Celular/metabolismo
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Poro Nuclear/metabolismo
Fosfoproteínas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Phosphoproteins); 0 (Transcription Factors)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180104
[Lr] Data última revisão:
180104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171206
[St] Status:MEDLINE


  3 / 1363 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


  4 / 1363 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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[PMID]:28883038
[Au] Autor:Lapetina DL; Ptak C; Roesner UK; Wozniak RW
[Ad] Endereço:Department of Cell Biology, University of Alberta, Edmonton, Alberta, Canada.
[Ti] Título:Yeast silencing factor Sir4 and a subset of nucleoporins form a complex distinct from nuclear pore complexes.
[So] Source:J Cell Biol;216(10):3145-3159, 2017 Oct 02.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Interactions occurring at the nuclear envelope (NE)-chromatin interface influence both NE structure and chromatin organization. Insights into the functions of NE-chromatin interactions have come from the study of yeast subtelomeric chromatin and its association with the NE, including the identification of various proteins necessary for tethering subtelomeric chromatin to the NE and the silencing of resident genes. Here we show that four of these proteins-the silencing factor Sir4, NE-associated Esc1, the SUMO E3 ligase Siz2, and the nuclear pore complex (NPC) protein Nup170-physically and functionally interact with one another and a subset of NPC components (nucleoporins or Nups). Importantly, this group of Nups is largely restricted to members of the inner and outer NPC rings, but it lacks numerous others including cytoplasmically and nucleoplasmically positioned Nups. We propose that this Sir4-associated Nup complex is distinct from holo-NPCs and that it plays a role in subtelomeric chromatin organization and NE tethering.
[Mh] Termos MeSH primário: Cromatina/metabolismo
Complexo de Proteínas Formadoras de Poros Nucleares/metabolismo
Poro Nuclear/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
Proteínas Reguladoras de Informação Silenciosa de Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Cromatina/genética
Poro Nuclear/genética
Complexo de Proteínas Formadoras de Poros Nucleares/genética
Proteínas Nucleares/genética
Proteínas Nucleares/metabolismo
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
Proteínas Reguladoras de Informação Silenciosa de Saccharomyces cerevisiae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chromatin); 0 (Esc1 protein, S cerevisiae); 0 (NUP170 protein, S cerevisiae); 0 (Nuclear Pore Complex Proteins); 0 (Nuclear Proteins); 0 (SIR4 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (Silent Information Regulator Proteins, Saccharomyces cerevisiae); 0 (Siz2 protein, S cerevisiae)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170909
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201609049


  6 / 1363 MEDLINE  
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[PMID]:28700925
[Au] Autor:Jovanovic-Talisman T; Zilman A
[Ad] Endereço:Department of Molecular Medicine, Beckman Research Institute of the City of Hope Comprehensive Cancer Center, Duarte, California. Electronic address: ttalisman@coh.org.
[Ti] Título:Protein Transport by the Nuclear Pore Complex: Simple Biophysics of a Complex Biomachine.
[So] Source:Biophys J;113(1):6-14, 2017 Jul 11.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In eukaryotic cells, transport of molecules between the nucleus and the cytoplasm is facilitated by highly selective and efficient biomachines known as nuclear pore complexes (NPCs). The structural details of NPCs vary across species, with many of their constituent proteins exhibiting relatively low sequence conservation; yet the NPC as a whole retains its general architecture and mechanism of action in all eukaryotes from yeast to humans. This functional conservation in the absence of precise molecular conservation suggests that many aspects of the NPC transport mechanism may be understood based on general biophysical considerations. Accordingly, some aspects of NPC function have been recapitulated in artificial nanochannel mimics, even though they lack certain molecular elements of the endogenous NPC. Herein, we review biophysical aspects of NPC architecture and function and cover recent progress in the field. We also review recent advances in man-made molecular filters inspired by NPCs, and their applications in nanotechnology. We conclude the review with an outlook on outstanding questions in the field and biomedical aspects of NPC transport.
[Mh] Termos MeSH primário: Poro Nuclear/metabolismo
Proteínas/metabolismo
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Poro Nuclear/química
Transporte Proteico
Proteínas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170825
[Lr] Data última revisão:
170825
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170713
[St] Status:MEDLINE


  7 / 1363 MEDLINE  
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[PMID]:28659328
[Au] Autor:Rüthnick D; Neuner A; Dietrich F; Kirrmaier D; Engel U; Knop M; Schiebel E
[Ad] Endereço:Zentrum für Molekulare Biologie at the University of Heidelberg, German Cancer Research Center-Center for Molecular Biology Alliance, Heidelberg, Germany.
[Ti] Título:Characterization of spindle pole body duplication reveals a regulatory role for nuclear pore complexes.
[So] Source:J Cell Biol;216(8):2425-2442, 2017 Aug 07.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The spindle pole body (SPB) of budding yeast duplicates once per cell cycle. In G1, the satellite, an SPB precursor, assembles next to the mother SPB (mSPB) on the cytoplasmic side of the nuclear envelope (NE). How the growing satellite subsequently inserts into the NE is an open question. To address this, we have uncoupled satellite growth from NE insertion. We show that the bridge structure that separates the mSPB from the satellite is a distance holder that prevents deleterious fusion of both structures. Binding of the γ-tubulin receptor Spc110 to the central plaque from within the nucleus is important for NE insertion of the new SPB. Moreover, we provide evidence that a nuclear pore complex associates with the duplicating SPB and helps to insert the SPB into the NE. After SPB insertion, membrane-associated proteins including the conserved Ndc1 encircle the SPB and retain it within the NE. Thus, uncoupling SPB growth from NE insertion unmasks functions of the duplication machinery.
[Mh] Termos MeSH primário: Ciclo Celular
Membrana Nuclear/metabolismo
Poro Nuclear/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
Corpos Polares do Fuso/metabolismo
[Mh] Termos MeSH secundário: Proteínas do Citoesqueleto/genética
Proteínas do Citoesqueleto/metabolismo
Genótipo
Microscopia Eletrônica de Transmissão
Microscopia de Fluorescência
Proteínas Associadas aos Microtúbulos/genética
Proteínas Associadas aos Microtúbulos/metabolismo
Mutação
Membrana Nuclear/genética
Membrana Nuclear/ultraestrutura
Poro Nuclear/genética
Poro Nuclear/ultraestrutura
Complexo de Proteínas Formadoras de Poros Nucleares/genética
Complexo de Proteínas Formadoras de Poros Nucleares/metabolismo
Proteínas Nucleares/genética
Proteínas Nucleares/metabolismo
Fenótipo
Fosfoproteínas/genética
Fosfoproteínas/metabolismo
Transporte Proteico
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/crescimento & desenvolvimento
Saccharomyces cerevisiae/ultraestrutura
Proteínas de Saccharomyces cerevisiae/genética
Corpos Polares do Fuso/genética
Corpos Polares do Fuso/ultraestrutura
Fatores de Tempo
Tubulina (Proteína)/genética
Tubulina (Proteína)/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytoskeletal Proteins); 0 (Microtubule-Associated Proteins); 0 (NDC1 protein, S cerevisiae); 0 (Nuclear Pore Complex Proteins); 0 (Nuclear Proteins); 0 (Phosphoproteins); 0 (SPC110 protein, S cerevisiae); 0 (SPC42 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (Spc29 protein, S cerevisiae); 0 (Tubulin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170630
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201612129


  8 / 1363 MEDLINE  
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[PMID]:28586646
[Au] Autor:Raices M; Bukata L; Sakuma S; Borlido J; Hernandez LS; Hart DO; D'Angelo MA
[Ad] Endereço:Development, Aging and Regeneration Program, Sanford Burnham Prebys Medical Discovery Institute, 10901 North Torrey Pines Road, La Jolla, 92037 CA, USA.
[Ti] Título:Nuclear Pores Regulate Muscle Development and Maintenance by Assembling a Localized Mef2C Complex.
[So] Source:Dev Cell;41(5):540-554.e7, 2017 Jun 05.
[Is] ISSN:1878-1551
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nuclear pore complexes (NPCs) are multiprotein channels connecting the nucleus with the cytoplasm. NPCs have been shown to have tissue-specific composition, suggesting that their function can be specialized. However, the physiological roles of NPC composition changes and their impacts on cellular processes remain unclear. Here we show that the addition of the Nup210 nucleoporin to NPCs during myoblast differentiation results in assembly of an Mef2C transcriptional complex required for efficient expression of muscle structural genes and microRNAs. We show that this NPC-localized complex is essential for muscle growth, myofiber maturation, and muscle cell survival and that alterations in its activity result in muscle degeneration. Our findings suggest that NPCs regulate the activity of functional gene groups by acting as scaffolds that promote the local assembly of tissue-specific transcription complexes and show how nuclear pore composition changes can be exploited to regulate gene expression at the nuclear periphery.
[Mh] Termos MeSH primário: Embrião não Mamífero/citologia
Fatores de Transcrição MEF2/metabolismo
Desenvolvimento Muscular/genética
Complexo de Proteínas Formadoras de Poros Nucleares/metabolismo
Poro Nuclear/fisiologia
Proteínas de Peixe-Zebra/metabolismo
Peixe-Zebra/metabolismo
[Mh] Termos MeSH secundário: Animais
Diferenciação Celular
Núcleo Celular/genética
Embrião não Mamífero/metabolismo
Fatores de Transcrição MEF2/genética
Membrana Nuclear/genética
Complexo de Proteínas Formadoras de Poros Nucleares/genética
Peixe-Zebra/crescimento & desenvolvimento
Proteínas de Peixe-Zebra/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MEF2 Transcription Factors); 0 (Nuclear Pore Complex Proteins); 0 (Zebrafish Proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170607
[St] Status:MEDLINE


  9 / 1363 MEDLINE  
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[PMID]:28525751
[Au] Autor:van Steensel B; Belmont AS
[Ad] Endereço:Division of Gene Regulation, Netherlands Cancer Institute, 1066 CX Amsterdam, the Netherlands; Department of Cell Biology, Erasmus University Medical Center, 3015 CE Rotterdam, the Netherlands. Electronic address: b.v.steensel@nki.nl.
[Ti] Título:Lamina-Associated Domains: Links with Chromosome Architecture, Heterochromatin, and Gene Repression.
[So] Source:Cell;169(5):780-791, 2017 May 18.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In metazoan cell nuclei, hundreds of large chromatin domains are in close contact with the nuclear lamina. Such lamina-associated domains (LADs) are thought to help organize chromosomes inside the nucleus and have been associated with gene repression. Here, we discuss the properties of LADs, the molecular mechanisms that determine their association with the nuclear lamina, their dynamic links with other nuclear compartments, and their proposed roles in gene regulation.
[Mh] Termos MeSH primário: Núcleo Celular/química
Cromatina/química
[Mh] Termos MeSH secundário: Animais
Núcleo Celular/metabolismo
Regulação da Expressão Gênica
Heterocromatina
Seres Humanos
Laminas/metabolismo
Lâmina Nuclear/química
Poro Nuclear/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Chromatin); 0 (Heterochromatin); 0 (Lamins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170730
[Lr] Data última revisão:
170730
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170520
[St] Status:MEDLINE


  10 / 1363 MEDLINE  
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[PMID]:28490590
[Au] Autor:Huffman JB; Daniel GR; Falck-Pedersen E; Huet A; Smith GA; Conway JF; Homa FL
[Ad] Endereço:Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, USA.
[Ti] Título:The C Terminus of the Herpes Simplex Virus UL25 Protein Is Required for Release of Viral Genomes from Capsids Bound to Nuclear Pores.
[So] Source:J Virol;91(15), 2017 Aug 01.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The herpes simplex virus (HSV) capsid is released into the cytoplasm after fusion of viral and host membranes, whereupon dynein-dependent trafficking along microtubules targets it to the nuclear envelope. Binding of the capsid to the nuclear pore complex (NPC) is mediated by the capsid protein pUL25 and the capsid-tethered tegument protein pUL36. Temperature-sensitive mutants in both pUL25 and pUL36 dock at the NPC but fail to release DNA. The uncoating reaction has been difficult to study due to the rapid release of the genome once the capsid interacts with the nuclear pore. In this study, we describe the isolation and characterization of a truncation mutant of pUL25. Live-cell imaging and immunofluorescence studies demonstrated that the mutant was not impaired in penetration of the host cell or in trafficking of the capsid to the nuclear membrane. However, expression of viral proteins was absent or significantly delayed in cells infected with the pUL25 mutant virus. Transmission electron microscopy revealed capsids accumulated at nuclear pores that retained the viral genome for at least 4 h postinfection. In addition, cryoelectron microscopy (cryo-EM) reconstructions of virion capsids did not detect any obvious differences in the location or structural organization for the pUL25 or pUL36 proteins on the pUL25 mutant capsids. Further, in contrast to wild-type virus, the antiviral response mediated by the viral DNA-sensing cyclic guanine adenine synthase (cGAS) was severely compromised for the pUL25 mutant. These results demonstrate that the pUL25 capsid protein has a critical role in releasing viral DNA from NPC-bound capsids. Herpes simplex virus 1 (HSV-1) is the causative agent of several pathologies ranging in severity from the common cold sore to life-threatening encephalitic infection. Early steps in infection include release of the capsid into the cytoplasm, docking of the capsid at a nuclear pore, and release of the viral genome into the nucleus. A key knowledge gap is how the capsid engages the NPC and what triggers release of the viral genome into the nucleus. Here we show that the C-terminal region of the HSV-1 pUL25 protein is required for releasing the viral genome from capsids docked at nuclear pores. The significance of our research is in identifying pUL25 as a key viral factor for genome uncoating. pUL25 is found at each of the capsid vertices as part of the capsid vertex-specific component and implicates the importance of this complex for NPC binding and genome release.
[Mh] Termos MeSH primário: Proteínas do Capsídeo/metabolismo
DNA Viral/metabolismo
Herpesvirus Humano 1/fisiologia
Poro Nuclear/metabolismo
Desenvelopamento do Vírus
[Mh] Termos MeSH secundário: Animais
Proteínas do Capsídeo/genética
Cercopithecus aethiops
Microscopia
Proteínas Mutantes/genética
Proteínas Mutantes/metabolismo
Deleção de Sequência
Células Vero
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Capsid Proteins); 0 (DNA, Viral); 0 (Mutant Proteins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170727
[Lr] Data última revisão:
170727
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170512
[St] Status:MEDLINE



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