Base de dados : MEDLINE
Pesquisa : A11.284.149.165.630 [Categoria DeCS]
Referências encontradas : 5135 [refinar]
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  1 / 5135 MEDLINE  
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[PMID]:28452496
[Au] Autor:Wang CH; Mehta P; Elbaum M
[Ad] Endereço:Department of Physics, Boston University, Boston, Massachusetts 02215, USA.
[Ti] Título:Thermodynamic Paradigm for Solution Demixing Inspired by Nuclear Transport in Living Cells.
[So] Source:Phys Rev Lett;118(15):158101, 2017 Apr 14.
[Is] ISSN:1079-7114
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Living cells display a remarkable capacity to compartmentalize their functional biochemistry. A particularly fascinating example is the cell nucleus. Exchange of macromolecules between the nucleus and the surrounding cytoplasm does not involve traversing a lipid bilayer membrane. Instead, large protein channels known as nuclear pores cross the nuclear envelope and regulate the passage of other proteins and RNA molecules. Beyond simply gating diffusion, the system of nuclear pores and associated transport receptors is able to generate substantial concentration gradients, at the energetic expense of guanosine triphosphate hydrolysis. In contrast to conventional approaches to demixing such as reverse osmosis and dialysis, the biological system operates continuously, without application of cyclic changes in pressure or solvent exchange. Abstracting the biological paradigm, we examine this transport system as a thermodynamic machine of solution demixing. Building on the construct of free energy transduction and biochemical kinetics, we find conditions for the stable operation and optimization of the concentration gradients as a function of dissipation in the form of entropy production.
[Mh] Termos MeSH primário: Transporte Ativo do Núcleo Celular
Citoplasma/metabolismo
Membrana Nuclear/metabolismo
Proteínas/química
[Mh] Termos MeSH secundário: Núcleo Celular
Difusão
Cinética
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180209
[Lr] Data última revisão:
180209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1103/PhysRevLett.118.158101


  2 / 5135 MEDLINE  
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[PMID]:27776995
[Au] Autor:Rebl A; Rebl H; Köbis JM; Goldammer T; Seyfert HM
[Ad] Endereço:Leibniz Institute for Farm Animal Biology (FBN), Institute for Genome Biology, Wilhelm-Stahl-Allee 2, 18196, Dummerstorf, Germany.
[Ti] Título:ST2 from rainbow trout quenches TLR signalling, localises at the nuclear membrane and allows the nuclear translocation of MYD88.
[So] Source:Dev Comp Immunol;67:139-152, 2017 02.
[Is] ISSN:1879-0089
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The mammalian interleukin 1 receptor-like 1 receptor (IL1RL1), commonly known as ST2, is thought to downregulate TLR signalling by sequestering the signalling adapter MYD88 (myeloid differentiation primary response protein 88). ST2 sequences are known in several fish species, but none of them have functionally been examined. We characterised ST2 from rainbow trout (Oncorhynchus mykiss) and the structure of its encoding gene. The primary sequence of ST2 is only weakly conserved from fish to human. However, the amino acid sequences forming the interfaces for ST2 and MYD88 interaction are well conserved throughout evolution. High similarity of the gene segmentation unambiguously proves the common ancestry of fish and mammalian ST2. Trout ST2 and trout MYD88 genes were constitutively expressed in embryonic, larval and adult trout. In vivo infection with Aeromonas salmonicida did not modulate the mRNA levels of both factors. Overexpressing trout ST2 in the mammalian HEK-293 reconstitution system of TLR2 signalling quenched the Escherichia coli-induced activation of NF-κB and SAA promoters in a dose-dependent fashion. The expression of GFP-tagged trout ST2 in human HEK-293 or trout CHSE-214 cells surprisingly revealed that (i) ST2 localised abundantly at the nuclear membrane rather than at the cell membrane and (ii) the coexpression of both ST2 and MYD88 allowed the translocation of trout MYD88 from cytoplasm to nucleus, as assessed using confocal microscopy and Western blotting. Hence, we validated that trout ST2 is a dampener of TLR signalling and interacts with MYD88. The spatial distribution of these factors raises questions about how this repressive mechanism functions.
[Mh] Termos MeSH primário: Proteínas de Peixes/metabolismo
Proteína 1 Semelhante a Receptor de Interleucina-1/metabolismo
Fator 88 de Diferenciação Mieloide/metabolismo
Membrana Nuclear/metabolismo
Oncorhynchus mykiss/imunologia
[Mh] Termos MeSH secundário: Transporte Ativo do Núcleo Celular
Animais
Evolução Biológica
Proteínas de Peixes/genética
Seres Humanos
Proteína 1 Semelhante a Receptor de Interleucina-1/genética
Mamíferos
Ligação Proteica
Transporte Proteico
Transdução de Sinais
Receptores Toll-Like/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fish Proteins); 0 (IL1RL1 protein, human); 0 (Interleukin-1 Receptor-Like 1 Protein); 0 (Myeloid Differentiation Factor 88); 0 (Toll-Like Receptors)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:180210
[Lr] Data última revisão:
180210
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161026
[St] Status:MEDLINE


  3 / 5135 MEDLINE  
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[PMID]:28449239
[Au] Autor:Bermeo S; Al-Saedi A; Kassem M; Vidal C; Duque G
[Ad] Endereço:Sydney Medical School Nepean, The University of Sydney, Penrith, NSW, Australia.
[Ti] Título:The Role of the Nuclear Envelope Protein MAN1 in Mesenchymal Stem Cell Differentiation.
[So] Source:J Cell Biochem;118(12):4425-4435, 2017 Dec.
[Is] ISSN:1097-4644
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mutations in MAN1, a protein of the nuclear envelope, cause bone phenotypes characterized by hyperostosis. The mechanism of this pro-osteogenic phenotype remains unknown. We increased and decreased MAN1 expression in mesenchymal stem cells (MSC) upon which standard osteogenic and adipogenic differentiation were performed. MAN1 knockdown increased osteogenesis and mineralization. In contrast, osteogenesis remained stable upon MAN1 overexpression. Regarding a mechanism, we found that low levels of MAN1 facilitated the nuclear accumulation of regulatory smads and smads-related complexes, with a concurrently high expression of nuclear ß-Catenin. In addition, we found adipogenesis to be decreased in both conditions, although predominantly affected by MAN1 overexpression. Finally, lamin A, a protein of the nuclear envelope that regulates MSC differentiation, was unaffected by changes in MAN1. In conclusion, our studies demonstrated that lower levels of MAN1 in differentiating MSC are associated with higher osteogenesis and lower adipogenesis. High levels of MAN1 only affected adipogenesis. These effects could have an important role in the understanding of the role of the proteins of the nuclear envelope in bone formation. J. Cell. Biochem. 118: 4425-4435, 2017. © 2017 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Adipogenia
Diferenciação Celular
Proteínas de Membrana/metabolismo
Células Mesenquimais Estromais/metabolismo
Membrana Nuclear/metabolismo
Proteínas Nucleares/metabolismo
[Mh] Termos MeSH secundário: Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MAN1 protein, human); 0 (Membrane Proteins); 0 (Nuclear Proteins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180102
[Lr] Data última revisão:
180102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE
[do] DOI:10.1002/jcb.26096


  4 / 5135 MEDLINE  
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[PMID]:28743001
[Au] Autor:Pae J; Cinalli RM; Marzio A; Pagano M; Lehmann R
[Ad] Endereço:HHMI and Kimmel Center for Biology and Medicine of the Skirball Institute, Department of Cell Biology, New York University School of Medicine, New York, NY 10016, USA.
[Ti] Título:GCL and CUL3 Control the Switch between Cell Lineages by Mediating Localized Degradation of an RTK.
[So] Source:Dev Cell;42(2):130-142.e7, 2017 07 24.
[Is] ISSN:1878-1551
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The separation of germline from somatic lineages is fundamental to reproduction and species preservation. Here, we show that Drosophila Germ cell-less (GCL) is a critical component in this process by acting as a switch that turns off a somatic lineage pathway. GCL, a conserved BTB (Broad-complex, Tramtrack, and Bric-a-brac) protein, is a substrate-specific adaptor for Cullin3-RING ubiquitin ligase complex (CRL3 ). We show that CRL3 promotes PGC fate by mediating degradation of Torso, a receptor tyrosine kinase (RTK) and major determinant of somatic cell fate. This mode of RTK degradation does not depend upon receptor activation but is prompted by release of GCL from the nuclear envelope during mitosis. The cell-cycle-dependent change in GCL localization provides spatiotemporal specificity for RTK degradation and sequesters CRL3 to prevent it from participating in excessive activities. This precisely orchestrated mechanism of CRL3 function and regulation defines cell fate at the single-cell level.
[Mh] Termos MeSH primário: Linhagem da Célula
Proteínas Culina/metabolismo
Proteínas de Drosophila/metabolismo
Drosophila melanogaster/citologia
Drosophila melanogaster/metabolismo
Proteínas Nucleares/metabolismo
Proteólise
Receptores Proteína Tirosina Quinases/metabolismo
[Mh] Termos MeSH secundário: Animais
Membrana Celular/metabolismo
Sequência Conservada
Proteínas de Drosophila/química
Células Germinativas/citologia
Células Germinativas/metabolismo
Células HEK293
Seres Humanos
Mitose
Membrana Nuclear/metabolismo
Sinais de Localização Nuclear/metabolismo
Proteínas Nucleares/química
Oogênese
Domínios Proteicos
Transdução de Sinais
Especificidade por Substrato
Ubiquitinação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Cullin Proteins); 0 (Drosophila Proteins); 0 (Nuclear Localization Signals); 0 (Nuclear Proteins); 0 (gcl protein, Drosophila); 0 (gft protein, Drosophila); EC 2.7.10.1 (Receptor Protein-Tyrosine Kinases); EC 2.7.10.1 (torso protein, Drosophila)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171208
[Lr] Data última revisão:
171208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE


  5 / 5135 MEDLINE  
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[PMID]:29096075
[Au] Autor:Parchure A; Munson M; Budnik V
[Ad] Endereço:Department of Neurobiology, University of Massachusetts Medical School, Worcester, MA, USA.
[Ti] Título:Getting mRNA-Containing Ribonucleoprotein Granules Out of a Nuclear Back Door.
[So] Source:Neuron;96(3):604-615, 2017 Nov 01.
[Is] ISSN:1097-4199
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A pivotal feature of long-lasting synaptic plasticity is the localization of RNAs and the protein synthesis machinery at synaptic sites. How and where ribonucleoprotein (RNP) transport granules that support this synthetic activity are formed is of fundamental importance. The prevailing model poses that the nuclear pore complex (NPC) is the sole gatekeeper for transit of cellular material in and out of the nucleus. However, insights from the nuclear assembly of large viral capsids highlight a back door route for nuclear escape, a process referred to nuclear envelope (NE) budding. Recent studies indicate that NE budding might be an endogenous cellular process for the nuclear export of very large RNPs and protein aggregates. In Drosophila, this mechanism is required for synaptic plasticity, but its role may extend beyond the nervous system, in tissues where local changes in translation are required. Here we discuss these recent findings and a potential relationship between NE budding and the NPC.
[Mh] Termos MeSH primário: Transporte Ativo do Núcleo Celular/fisiologia
Núcleo Celular/metabolismo
Grânulos Citoplasmáticos/metabolismo
RNA Mensageiro/metabolismo
Ribonucleoproteínas/metabolismo
[Mh] Termos MeSH secundário: Animais
Núcleo Celular/genética
Grânulos Citoplasmáticos/genética
Seres Humanos
Membrana Nuclear/genética
Membrana Nuclear/metabolismo
RNA Mensageiro/genética
Ribonucleoproteínas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (RNA, Messenger); 0 (Ribonucleoproteins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171103
[St] Status:MEDLINE


  6 / 5135 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


  7 / 5135 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


  8 / 5135 MEDLINE  
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[PMID]:28968422
[Au] Autor:Guo YJ; Fu SH; Li LL
[Ad] Endereço:Hubei Key Laboratory of Genetic Regulation and Integrative Biology, College of Life Sciences, Central China Normal University, Wuhan, China.
[Ti] Título:Autographa californica multiple nucleopolyhedrovirus ac75 is required for egress of nucleocapsids from the nucleus and formation of de novo intranuclear membrane microvesicles.
[So] Source:PLoS One;12(10):e0185630, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this study, Autographa californica multiple nucleopolyhedrovirus ac75 was functionally characterized. Ac75 has homologs in all sequenced genomes of alphabaculoviruses, betabaculoviruses, and gammabaculoviruses. It was determined to encode a protein that is associated with the nucleocapsid of budded virus and with both envelope and nucleocapsids of occlusion-derived virus. Sf9 cells transfected by an ac75-knockout bacmid resulted in the infection being restricted to single cells. No budded virus were detected although viral DNA replication and late gene expression were unaffected. Electron microscopy revealed that the virogenic stroma, nucleocapsids and occlusion bodies appeared normal in the cells transfected by an ac75-knockout bacmid. However, the nucleocapsids were unenveloped, the occlusion bodies did not contain any virions or nucleocapsids, and no nucleocapsids were found outside the nucleus or spanning the nuclear membrane. In addition, de novo intranuclear membrane microvesicles that are the precursor of occlusion-derived virus envelopes were absent in the nuclei of transfected cells. Confocal microscopy showed that AC75 protein appeared in the cytoplasm as early as 6 hours post infection. It localized to the ring zone at the periphery of the nucleus from 15 to 24 hours post infection and demonstrated light blocky cloud-like distribution in the center of the nucleus. AC75 was found to co-immunoprecipitate with BV and ODV associated envelope protein ODV-E25. The data from this study suggest that ac75 is essential for induction of the intranuclear membrane microvesicles, it appears to be required for the intranuclear envelopment of nucleocapsids, and is also essential for egress of nucleocapsids from the nuclei, in infected cells.
[Mh] Termos MeSH primário: Núcleo Celular/metabolismo
Genes Virais
Membrana Nuclear/metabolismo
Nucleocapsídeo/metabolismo
Nucleopolyhedrovirus/genética
[Mh] Termos MeSH secundário: Animais
Transporte Biológico
Western Blotting
DNA Viral/biossíntese
Técnicas de Silenciamento de Genes
Microscopia Confocal
Microscopia Eletrônica de Transmissão
Plasmídeos
Reação em Cadeia da Polimerase em Tempo Real
Células Sf9
Replicação Viral/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Viral)
[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:171003
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185630


  9 / 5135 MEDLINE  
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[PMID]:28934222
[Au] Autor:Branch MR; Hepler JR
[Ad] Endereço:Department of Pharmacology, Emory University School of Medicine, Atlanta, Georgia, United States of America.
[Ti] Título:Endogenous RGS14 is a cytoplasmic-nuclear shuttling protein that localizes to juxtanuclear membranes and chromatin-rich regions of the nucleus.
[So] Source:PLoS One;12(9):e0184497, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Regulator of G protein signaling 14 (RGS14) is a multifunctional scaffolding protein that integrates G protein and H-Ras/MAPkinase signaling pathways to regulate synaptic plasticity important for hippocampal learning and memory. However, to date, little is known about the subcellular distribution and roles of endogenous RGS14 in a neuronal cell line. Most of what is known about RGS14 cellular behavior is based on studies of tagged, recombinant RGS14 ectopically overexpressed in unnatural host cells. Here, we report for the first time a comprehensive assessment of the subcellular distribution and dynamic localization of endogenous RGS14 in rat B35 neuroblastoma cells. Using confocal imaging and 3D-structured illumination microscopy, we find that endogenous RGS14 localizes to subcellular compartments not previously recognized in studies of recombinant RGS14. RGS14 localization was observed most notably at juxtanuclear membranes encircling the nucleus, at nuclear pore complexes (NPC) on both sides of the nuclear envelope and within intranuclear membrane channels, and within both chromatin-poor and chromatin-rich regions of the nucleus in a cell cycle-dependent manner. In addition, a subset of nuclear RGS14 localized adjacent to active RNA polymerase II. Endogenous RGS14 was absent from the plasma membrane in resting cells; however, the protein could be trafficked to the plasma membrane from juxtanuclear membranes in endosomes derived from ER/Golgi, following constitutive activation of endogenous RGS14 G protein binding partners using AlF4¯. Finally, our findings show that endogenous RGS14 behaves as a cytoplasmic-nuclear shuttling protein confirming what has been shown previously for recombinant RGS14. Taken together, the findings highlight possible cellular roles for RGS14 not previously recognized that are distinct from the regulation of conventional GPCR-G protein signaling, in particular undefined roles for RGS14 in the nucleus.
[Mh] Termos MeSH primário: Núcleo Celular/metabolismo
Cromatina/metabolismo
Citoplasma/metabolismo
Membrana Nuclear/metabolismo
Proteínas RGS/metabolismo
[Mh] Termos MeSH secundário: Animais
Transporte Biológico/fisiologia
Encéfalo/citologia
Encéfalo/metabolismo
Células COS
Ciclo Celular/fisiologia
Linhagem Celular Tumoral
Cercopithecus aethiops
Células HEK293
Seres Humanos
Imagem Tridimensional
Camundongos
Microscopia Confocal
Neurônios/citologia
Neurônios/metabolismo
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chromatin); 0 (RGS Proteins); 0 (Rgs14 protein, rat)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170922
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184497


  10 / 5135 MEDLINE  
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[PMID]:28910710
[Au] Autor:Wang W; Yang L; Huang X; Fu W; Pan D; Cai L; Ye J; Liu J; Xia N; Cheng T; Zhu H
[Ad] Endereço:State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, National Institute of Diagnostics and Vaccine Development in Infectious Diseases, School of Public Health, Xiamen University, Xiamen 361102, PR China.
[Ti] Título:Outer nuclear membrane fusion of adjacent nuclei in varicella-zoster virus-induced syncytia.
[So] Source:Virology;512:34-38, 2017 Dec.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Syncytia formation has been considered important for cell-to-cell spread and pathogenesis of many viruses. As a syncytium forms, individual nuclei often congregate together, allowing close contact of nuclear membranes and possibly fusion to occur. However, there is currently no reported evidence of nuclear membrane fusion between adjacent nuclei in wild-type virus-induced syncytia. Varicella-zoster virus (VZV) is one typical syncytia-inducing virus that causes chickenpox and shingles in humans. Here, we report, for the first time, an interesting observation of apparent fusion of the outer nuclear membranes from juxtaposed nuclei that comprise VZV syncytia both in ARPE-19 human epithelial cells in vitro and in human skin xenografts in the SCID-hu mouse model in vivo. This work reveals a novel aspect of VZV-related cytopathic effect in the context of multinucleated syncytia. Additionally, the information provided by this study could be helpful for future studies on interactions of viruses with host cell nuclei.
[Mh] Termos MeSH primário: Células Epiteliais/patologia
Células Epiteliais/virologia
Células Gigantes/virologia
Herpesvirus Humano 3/fisiologia
Membrana Nuclear/patologia
[Mh] Termos MeSH secundário: Fusão Celular
Linhagem Celular
Seres Humanos
Membrana Nuclear/virologia
Pele/citologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170915
[St] Status:MEDLINE



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