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[PMID]:28044231
[Au] Autor:Inada N
[Ad] Endereço:The Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama-cho, Ikoma-shi, Nara, 630-0192, Japan. norikoi@bs.naist.jp.
[Ti] Título:Plant actin depolymerizing factor: actin microfilament disassembly and more.
[So] Source:J Plant Res;130(2):227-238, 2017 Mar.
[Is] ISSN:1618-0860
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:ACTIN DEPOLYMERIZING FACTOR (ADF) is a conserved protein among eukaryotes. The main function of ADF is the severing and depolymerizing filamentous actin (F-actin), thus regulating F-actin organization and dynamics and contributing to growth and development of the organisms. Mammalian genomes contain only a few ADF genes, whereas angiosperm plants have acquired an expanding number of ADFs, resulting in the differentiation of physiological functions. Recent studies have revealed functions of ADFs in plant growth and development, and various abiotic and biotic stress responses. In biotic stress responses, ADFs are involved in both susceptibility and resistance, depending on the pathogens. Furthermore, recent studies have highlighted a new role of ADF in the nucleus, possibly in the regulation of gene expression. In this review, I will summarize the current status of plant ADF research and discuss future research directions.
[Mh] Termos MeSH primário: Citoesqueleto de Actina/genética
Destrina/genética
Proteínas de Plantas/genética
Plantas/genética
[Mh] Termos MeSH secundário: Citoesqueleto de Actina/metabolismo
Destrina/metabolismo
Proteínas de Plantas/metabolismo
Plantas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Destrin); 0 (Plant Proteins)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171014
[Lr] Data última revisão:
171014
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170104
[St] Status:MEDLINE
[do] DOI:10.1007/s10265-016-0899-8


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[PMID]:27922676
[Au] Autor:Huo Y; Xie X; Jiang B
[Ad] Endereço:Eye Center, Second Affiliated Hospital of Zhejiang University School of Medicine, Hangzhou, Zhejiang 310009, P.R. China.
[Ti] Título:Identification of functional pathways associated with the conditional ablation of serum response factor in Dstncorn1 mice.
[So] Source:Mol Med Rep;15(1):139-145, 2017 Jan.
[Is] ISSN:1791-3004
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:The aim of the present study was to investigate the signaling pathways associated with functional alterations in corneal tissues following the conditional ablation of serum response factor (Srf) in Dstncorn1 mice. The gene expression profiling array GSE49688, which includes 3 samples each from the wild­type (WT), Dstncorn1 mutant (corn1) and corn1 mice following the conditional ablation of Srf from the corneal epithelium [namely rescued (res)] mouse groups, was downloaded from the Gene Expression Omnibus database. The limma package was used to identify differentially expressed genes (DEGs) among the three mouse groups. DEGs were subsequently analyzed by dynamic comparison, hierarchical clustering and pathway enrichment analysis. Pathway alteration scores were also calculated in order to study the dynamic metergasis of each identified pathway. A total of 788 DEGs were identified between the corn1 and res groups, 1,365 DEGs were identified between the corn1 and WT groups, and 852 DEGs were identified between the res and WT groups. Among these DEGs, 228 genes were differentially expressed across all three groups, and were mainly enriched in signaling pathways involved in the regulation of the actin cytoskeleton, including the cofilin 1 (CFL1), the mitogen­activated protein kinase (MAPK) signaling pathway and focal adhesion. The dilated cardiomyopathy signaling pathway displayed the highest alteration score, and was enriched with integrin and integrin ß­6 (ITGB6). In conclusion, the actin cytoskeleton regulatory pathway, MAPK and dilated cardiomyopathy signaling pathways, as well as CFL1 and ITGB6 genes, may be regulated by Srf to serve important roles in the progression of corneal disease.
[Mh] Termos MeSH primário: Córnea/metabolismo
Doenças da Córnea/genética
Destrina/genética
Deleção de Genes
Perfilação da Expressão Gênica
Fator de Resposta Sérica/genética
Transdução de Sinais
[Mh] Termos MeSH secundário: Animais
Análise por Conglomerados
Doenças da Córnea/metabolismo
Destrina/metabolismo
Redes Reguladoras de Genes
Camundongos
Proteínas Quinases Ativadas por Mitógeno/metabolismo
Fator de Resposta Sérica/metabolismo
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Destrin); 0 (Dstn protein, mouse); 0 (Serum Response Factor); EC 2.7.11.24 (Mitogen-Activated Protein Kinases)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170403
[Lr] Data última revisão:
170403
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161207
[St] Status:MEDLINE
[do] DOI:10.3892/mmr.2016.5984


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[PMID]:27716047
[Au] Autor:Liu Z; Yin L; Li Y; Yuan F; Zhang X; Ma J; Liu H; Wang Y; Zheng K; Cao J
[Ad] Endereço:Department of Pathogenic Biology and Immunology, Laboratory of Infection and Immunity, Xuzhou Medical University, Xuzhou, Jiangsu, 221004, People's Republic of China.
[Ti] Título:Intranasal immunization with recombinant Toxoplasma gondii actin depolymerizing factor confers protective efficacy against toxoplasmosis in mice.
[So] Source:BMC Immunol;17(1):37, 2016 Oct 06.
[Is] ISSN:1471-2172
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Toxoplasma gondii is an opportunistic protozoan closely associated with AIDS and vertical transmission. T. gondii actin depolymerizing factor (TgADF) plays an important role in actin cytoskeleton remodeling, and it is required to invade host cells. TgADF was a promising vaccine candidate. To observe the immunological changes and protective efficacy of recombinant TgADF protein (rTgADF) against T. gondii infection, we optimized the intranasal immunization dose of rTgADF and analyzed the survival rate and tachyzoite loads in mouse tissues after oral challenge with T. gondii tachyzoites. RESULTS: rTgADF was prepared, purified, and combined with mouse anti-His antibody and rabbit anti-T. gondii serum. After intranasal immunization with 10 µg, 20 µg, 30 µg, or 40 µg of rTgADF, the 30-µg group elicited high levels of secretory IgA (sIgA) in nasal, intestinal, and vesical washes, raised IgG titres in the sera, strong proliferation of splenocytes, and increased secretion of IL-2 and IFN-γ when compared with the control group. When the mice were orally challenged with T. gondii, an increase in the survival rate (36.36 %) and a decrease in the tachyzoite loads in the liver (67.77 %) and brain (51.01 %) were observed. CONCLUSIONS: Our findings demonstrate that intranasal immunization with rTgADF can simultaneously trigger mucosal and systemic immune responses and protect the mice against T. gondii infection.
[Mh] Termos MeSH primário: Antígenos de Protozoários/uso terapêutico
Destrina/uso terapêutico
Imunidade nas Mucosas
Linfócitos/imunologia
Proteínas Recombinantes/uso terapêutico
Toxoplasma/imunologia
Toxoplasmose/terapia
[Mh] Termos MeSH secundário: Administração Intranasal
Animais
Antígenos de Protozoários/imunologia
Proliferação Celular
Células Cultivadas
Destrina/imunologia
Feminino
Seres Humanos
Soros Imunes/administração & dosagem
Imunoglobulina A/sangue
Linfócitos/parasitologia
Camundongos
Camundongos Endogâmicos BALB C
Coelhos
Toxoplasmose/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, Protozoan); 0 (Destrin); 0 (Immune Sera); 0 (Immunoglobulin A); 0 (Recombinant Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171009
[Lr] Data última revisão:
171009
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161008
[St] Status:MEDLINE


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[PMID]:27684042
[Au] Autor:Berdieva M; Bogolyubov D; Podlipaeva Y; Goodkov A
[Ad] Endereço:Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Avenue, 194064 St. Petersburg, Russia. Electronic address: maria.berd4@yandex.ru.
[Ti] Título:Nucleus-associated actin in Amoeba proteus.
[So] Source:Eur J Protistol;56:191-199, 2016 Oct.
[Is] ISSN:1618-0429
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The presence, spatial distribution and forms of intranuclear and nucleus-associated cytoplasmic actin were studied in Amoeba proteus with immunocytochemical approaches. Labeling with different anti-actin antibodies and staining with TRITC-phalloidin and fluorescent deoxyribonuclease I were used. We showed that actin is abundant within the nucleus as well as in the cytoplasm of A. proteus cells. According to DNase I experiments, the predominant form of intranuclear actin is G-actin which is associated with chromatin strands. Besides, unpolymerized actin was shown to participate in organization of a prominent actin layer adjacent to the outer surface of nuclear envelope. No significant amount of F-actin was found in the nucleus. At the same time, the amoeba nucleus is enclosed in a basket-like structure formed by circumnuclear actin filaments and bundles connected with global cytoplasmic actin cytoskeleton. A supposed architectural function of actin filaments was studied by treatment with actin-depolymerizing agent latrunculin A. It disassembled the circumnuclear actin system, but did not affect the intranuclear chromatin structure. The results obtained for amoeba cells support the modern concept that actin is involved in fundamental nuclear processes that have evolved in the cells of multicellular organisms.
[Mh] Termos MeSH primário: Actinas/metabolismo
Amoeba/fisiologia
Núcleo Celular/metabolismo
[Mh] Termos MeSH secundário: Amoeba/efeitos dos fármacos
Compostos Bicíclicos Heterocíclicos com Pontes/farmacologia
Núcleo Celular/efeitos dos fármacos
Cromatina/química
Destrina/farmacologia
Imuno-Histoquímica
Polimerização/efeitos dos fármacos
Tiazolidinas/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Bridged Bicyclo Compounds, Heterocyclic); 0 (Chromatin); 0 (Destrin); 0 (Thiazolidines); SRQ9WWM084 (latrunculin A)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160930
[St] Status:MEDLINE


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[PMID]:27505888
[Au] Autor:Kanellos G; Frame MC
[Ad] Endereço:Edinburgh Cancer Research UK Centre, Institute of Genetics and Molecular Medicine, University of Edinburgh, Western General Hospital, Crewe Road South, Edinburgh EH4 2XR, UK georgios.kanellos@igmm.ed.ac.uk.
[Ti] Título:Cellular functions of the ADF/cofilin family at a glance.
[So] Source:J Cell Sci;129(17):3211-8, 2016 Sep 01.
[Is] ISSN:1477-9137
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The actin depolymerizing factor (ADF)/cofilin family comprises small actin-binding proteins with crucial roles in development, tissue homeostasis and disease. They are best known for their roles in regulating actin dynamics by promoting actin treadmilling and thereby driving membrane protrusion and cell motility. However, recent discoveries have increased our understanding of the functions of these proteins beyond their well-characterized roles. This Cell Science at a Glance article and the accompanying poster serve as an introduction to the diverse roles of the ADF/cofilin family in cells. The first part of the article summarizes their actions in actin treadmilling and the main mechanisms for their intracellular regulation; the second part aims to provide an outline of the emerging cellular roles attributed to the ADF/cofilin family, besides their actions in actin turnover. The latter part discusses an array of diverse processes, which include regulation of intracellular contractility, maintenance of nuclear integrity, transcriptional regulation, nuclear actin monomer transfer, apoptosis and lipid metabolism. Some of these could, of course, be indirect consequences of actin treadmilling functions, and this is discussed.
[Mh] Termos MeSH primário: Fatores de Despolimerização de Actina/metabolismo
Destrina/metabolismo
[Mh] Termos MeSH secundário: Animais
Apoptose
Núcleo Celular/metabolismo
Seres Humanos
Metabolismo dos Lipídeos
Estresse Fisiológico
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Actin Depolymerizing Factors); 0 (Destrin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160810
[St] Status:MEDLINE
[do] DOI:10.1242/jcs.187849


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[PMID]:27454820
[Au] Autor:Grintsevich EE; Yesilyurt HG; Rich SK; Hung RJ; Terman JR; Reisler E
[Ad] Endereço:Department of Chemistry and Biochemistry, University of California-Los Angeles, Los Angeles, California 90095, USA.
[Ti] Título:F-actin dismantling through a redox-driven synergy between Mical and cofilin.
[So] Source:Nat Cell Biol;18(8):876-85, 2016 Aug.
[Is] ISSN:1476-4679
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Numerous cellular functions depend on actin filament (F-actin) disassembly. The best-characterized disassembly proteins, the ADF (actin-depolymerizing factor)/cofilins (encoded by the twinstar gene in Drosophila), sever filaments and recycle monomers to promote actin assembly. Cofilin is also a relatively weak actin disassembler, posing questions about mechanisms of cellular F-actin destabilization. Here we uncover a key link to targeted F-actin disassembly by finding that F-actin is efficiently dismantled through a post-translational-mediated synergism between cofilin and the actin-oxidizing enzyme Mical. We find that Mical-mediated oxidation of actin improves cofilin binding to filaments, where their combined effect dramatically accelerates F-actin disassembly compared with either effector alone. This synergism is also necessary and sufficient for F-actin disassembly in vivo, magnifying the effects of both Mical and cofilin on cellular remodelling, axon guidance and Semaphorin-Plexin repulsion. Mical and cofilin, therefore, form a redox-dependent synergistic pair that promotes F-actin instability by rapidly dismantling F-actin and generating post-translationally modified actin that has altered assembly properties.
[Mh] Termos MeSH primário: Citoesqueleto de Actina/metabolismo
Actinas/metabolismo
Cofilina 1/metabolismo
Proteínas de Ligação a DNA/metabolismo
Drosophila melanogaster/metabolismo
[Mh] Termos MeSH secundário: Animais
Destrina/metabolismo
Oxirredução
Ligação Proteica/genética
Coelhos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Cofilin 1); 0 (DNA-Binding Proteins); 0 (Destrin); 0 (MICAL protein, Drosophila)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170606
[Lr] Data última revisão:
170606
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160726
[St] Status:MEDLINE
[do] DOI:10.1038/ncb3390


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[PMID]:26996939
[Au] Autor:Chin SM; Jansen S; Goode BL
[Ad] Endereço:Department of Biology, Rosenstiel Basic Medical Science Research Center, Brandeis University, Waltham, MA 02454, USA.
[Ti] Título:TIRF microscopy analysis of human Cof1, Cof2, and ADF effects on actin filament severing and turnover.
[So] Source:J Mol Biol;428(8):1604-16, 2016 Apr 24.
[Is] ISSN:1089-8638
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Dynamic remodeling and turnover of cellular actin networks requires actin filament severing by actin-depolymerizing factor (ADF)/Cofilin proteins. Mammals express three different ADF/Cofilins (Cof1, Cof2, and ADF), and genetic studies suggest that in vivo they perform both overlapping and unique functions. To gain mechanistic insights into their different roles, we directly compared their G-actin and F-actin binding affinities, and quantified the actin filament severing activities of human Cof1, Cof2, and ADF using in vitro total internal reflection fluorescence microscopy. All three ADF/Cofilins had similar affinities for G-actin and F-actin. However, Cof2 and ADF severed filaments much more efficiently than Cof1 at both lower and higher concentrations and using either muscle or platelet actin. Furthermore, Cof2 and ADF were more effective than Cof1 in promoting "enhanced disassembly" when combined with actin disassembly co-factors Coronin-1B and actin-interacting protein 1 (AIP1), and these differences were observed on both preformed and actively growing filaments. To probe the mechanism underlying these differences, we used multi-wavelength total internal reflection fluorescence microscopy to directly observe Cy3-Cof1 and Cy3-Cof2 interacting with actin filaments in real time during severing. Cof1 and Cof2 each bound to filaments with similar kinetics, yet Cof2 induced severing much more rapidly than Cof1, decreasing the time interval between initial binding on a filament and severing at the same location. These differences in ADF/Cofilin activities and mechanisms may be used in cells to tune filament turnover rates, which can vary widely for different actin structures.
[Mh] Termos MeSH primário: Citoesqueleto de Actina/química
Cofilina 1/química
Cofilina 2/química
Destrina/química
Microscopia/métodos
[Mh] Termos MeSH secundário: Fatores de Despolimerização de Actina/metabolismo
Actinas/química
Animais
Relação Dose-Resposta a Droga
Escherichia coli/metabolismo
Seres Humanos
Nucleotídeos/química
Plasmídeos/metabolismo
Ligação Proteica
Coelhos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Actin Depolymerizing Factors); 0 (Actins); 0 (CFL1 protein, human); 0 (CFL2 protein, human); 0 (Cofilin 1); 0 (Cofilin 2); 0 (DSTN protein, human); 0 (Destrin); 0 (Nucleotides)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:170424
[Lr] Data última revisão:
170424
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160322
[St] Status:MEDLINE


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[PMID]:26878213
[Au] Autor:Wang D; Naydenov NG; Feygin A; Baranwal S; Kuemmerle JF; Ivanov AI
[Ad] Endereço:Department of Human and Molecular Genetics, Virginia Commonwealth University, Richmond, Virginia.
[Ti] Título:Actin-Depolymerizing Factor and Cofilin-1 Have Unique and Overlapping Functions in Regulating Intestinal Epithelial Junctions and Mucosal Inflammation.
[So] Source:Am J Pathol;186(4):844-58, 2016 Apr.
[Is] ISSN:1525-2191
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The actin cytoskeleton is a crucial regulator of the intestinal mucosal barrier, controlling the assembly and function of epithelial adherens and tight junctions (AJs and TJs). Junction-associated actin filaments are dynamic structures that undergo constant turnover. Members of the actin-depolymerizing factor (ADF) and cofilin protein family play key roles in actin dynamics by mediating filament severing and polymerization. We examined the roles of ADF and cofilin-1 in regulating the structure and functions of AJs and TJs in the intestinal epithelium. Knockdown of either ADF or cofilin-1 by RNA interference increased the paracellular permeability of human colonic epithelial cell monolayers to small ions. Additionally, cofilin-1, but not ADF, depletion increased epithelial permeability to large molecules. Loss of either ADF or cofilin-1 did not affect the steady-state morphology of AJs and TJs but attenuated de novo junctional assembly. The observed defects in AJ and TJ formation were accompanied by delayed assembly of the perijunctional filamentous actin belt. A total loss of ADF expression in mice did not result in a defective mucosal barrier or in spontaneous gut inflammation. However, ADF-null mice demonstrated increased intestinal permeability and exaggerated inflammation during dextran sodium sulfate-induced colitis. Our findings demonstrate novel roles for ADF and cofilin-1 in regulating the remodeling and permeability of epithelial junctions, as well as the role of ADF in limiting the severity of intestinal inflammation.
[Mh] Termos MeSH primário: Cofilina 1/metabolismo
Destrina/metabolismo
Células Epiteliais/metabolismo
Inflamação/metabolismo
Mucosa Intestinal/metabolismo
Junções Íntimas/metabolismo
[Mh] Termos MeSH secundário: Citoesqueleto de Actina/metabolismo
Actinas/metabolismo
Animais
Citoesqueleto/metabolismo
Destrina/genética
Seres Humanos
Camundongos
Proteínas dos Microfilamentos/metabolismo
Permeabilidade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Actins); 0 (Cofilin 1); 0 (Destrin); 0 (Dstn protein, mouse); 0 (Microfilament Proteins)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:160325
[Lr] Data última revisão:
160325
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:160216
[St] Status:MEDLINE


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[PMID]:26863541
[Au] Autor:Nawaz-ul-Rehman MS; Prasanth KR; Xu K; Sasvari Z; Kovalev N; de Castro Martín IF; Barajas D; Risco C; Nagy PD
[Ad] Endereço:Department of Plant Pathology, University of Kentucky, Lexington, Kentucky, United States of America.
[Ti] Título:Viral Replication Protein Inhibits Cellular Cofilin Actin Depolymerization Factor to Regulate the Actin Network and Promote Viral Replicase Assembly.
[So] Source:PLoS Pathog;12(2):e1005440, 2016 Feb.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:RNA viruses exploit host cells by co-opting host factors and lipids and escaping host antiviral responses. Previous genome-wide screens with Tomato bushy stunt virus (TBSV) in the model host yeast have identified 18 cellular genes that are part of the actin network. In this paper, we show that the p33 viral replication factor interacts with the cellular cofilin (Cof1p), which is an actin depolymerization factor. Using temperature-sensitive (ts) Cof1p or actin (Act1p) mutants at a semi-permissive temperature, we find an increased level of TBSV RNA accumulation in yeast cells and elevated in vitro activity of the tombusvirus replicase. We show that the large p33 containing replication organelle-like structures are located in the close vicinity of actin patches in yeast cells or around actin cable hubs in infected plant cells. Therefore, the actin filaments could be involved in VRC assembly and the formation of large viral replication compartments containing many individual VRCs. Moreover, we show that the actin network affects the recruitment of viral and cellular components, including oxysterol binding proteins and VAP proteins to form membrane contact sites for efficient transfer of sterols to the sites of replication. Altogether, the emerging picture is that TBSV, via direct interaction between the p33 replication protein and Cof1p, controls cofilin activities to obstruct the dynamic actin network that leads to efficient subversion of cellular factors for pro-viral functions. In summary, the discovery that TBSV interacts with cellular cofilin and blocks the severing of existing filaments and the formation of new actin filaments in infected cells opens a new window to unravel the way by which viruses could subvert/co-opt cellular proteins and lipids. By regulating the functions of cofilin and the actin network, which are central nodes in cellular pathways, viruses could gain supremacy in subversion of cellular factors for pro-viral functions.
[Mh] Termos MeSH primário: Actinas/metabolismo
Replicação do DNA/genética
Destrina/metabolismo
Replicação Viral
[Mh] Termos MeSH secundário: Interações Hospedeiro-Patógeno
RNA Viral/genética
Tombusvirus/genética
Proteínas Virais/genética
Montagem de Vírus/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Actins); 0 (Destrin); 0 (RNA, Viral); 0 (Viral Proteins)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160211
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1005440


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[PMID]:26264370
[Au] Autor:Agricola ZN; Jagpal AK; Allbee AW; Prewitt AR; Shifley ET; Rankin SA; Zorn AM; Kenny AP
[Ad] Endereço:Perinatal Institute, Cincinnati Children's Hospital Research Foundation and Department of Pediatrics College of Medicine, University of Cincinnati, Cincinnati, Ohio.
[Ti] Título:Identification of genes expressed in the migrating primitive myeloid lineage of Xenopus laevis.
[So] Source:Dev Dyn;245(1):47-55, 2016 Jan.
[Is] ISSN:1097-0177
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: During primitive hematopoiesis in Xenopus, cebpa and spib expressing myeloid cells emerge from the anterior ventral blood island. Primitive myeloid cells migrate throughout the embryo and are critical for immunity, healing, and development. Although definitive hematopoiesis has been studied extensively, molecular mechanisms leading to the migration of primitive myelocytes remain poorly understood. We hypothesized these cells have specific extracellular matrix modifying and cell motility gene expression. RESULTS: In situ hybridization screens of transcripts expressed in Xenopus foregut mesendoderm at stage 23 identified seven genes with restricted expression in primitive myeloid cells: destrin; coronin actin binding protein, 1a; formin-like 1; ADAM metallopeptidase domain 28; cathepsin S; tissue inhibitor of metalloproteinase-1; and protein tyrosine phosphatase nonreceptor 6. A detailed in situ hybridization analysis revealed these genes are initially expressed in the aVBI but become dispersed throughout the embryo as the primitive myeloid cells become migratory, similar to known myeloid markers. Morpholino-mediated loss-of-function and mRNA-mediated gain-of-function studies revealed the identified genes are downstream of Spib.a and Cebpa, key transcriptional regulators of the myeloid lineage. CONCLUSIONS: We have identified genes specifically expressed in migratory primitive myeloid progenitors, providing tools to study how different gene networks operate in these primitive myelocytes during development and immunity.
[Mh] Termos MeSH primário: Linhagem da Célula/genética
Movimento Celular/genética
Células Mieloides/citologia
Xenopus laevis/genética
[Mh] Termos MeSH secundário: Animais
Destrina/genética
Destrina/metabolismo
Regulação da Expressão Gênica
Redes Reguladoras de Genes
Proteínas dos Microfilamentos/genética
Proteínas dos Microfilamentos/metabolismo
Células Mieloides/metabolismo
Inibidor Tecidual de Metaloproteinase-1/genética
Inibidor Tecidual de Metaloproteinase-1/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Destrin); 0 (Microfilament Proteins); 0 (Tissue Inhibitor of Metalloproteinase-1)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:170413
[Lr] Data última revisão:
170413
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150813
[St] Status:MEDLINE
[do] DOI:10.1002/dvdy.24314



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