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[PMID]: 28706108 [Au] Autor: Farrell KB; McDonald S; Lamb AK; Worcester C; Peersen OB; Di Pietro SM [Ad] Endereço: Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO. [Ti] Título: Novel function of a dynein light chain in actin assembly during clathrin-mediated endocytosis. [So] Source: J Cell Biol;216(8):2565-2580, 2017 Aug 07. [Is] ISSN: 1540-8140 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Clathrin- and actin-mediated endocytosis is essential in eukaryotic cells. In this study, we demonstrate that Tda2 is a novel protein of the endocytic machinery necessary for normal internalization of native cargo in yeast. Tda2 has not been classified in any protein family. Unexpectedly, solving the crystal structure of Tda2 revealed it belongs to the dynein light chain family. However, Tda2 works independently of the dynein motor complex and microtubules. Tda2 forms a tight complex with the polyproline motif-rich protein Aim21, which interacts physically with the SH3 domain of the Arp2/3 complex regulator Bbc1. The Tda2-Aim21 complex localizes to endocytic sites in a Bbc1- and filamentous actin-dependent manner. Importantly, the Tda2-Aim21 complex interacts directly with and facilitates the recruitment of actin-capping protein, revealing barbed-end filament capping at endocytic sites to be a regulated event. Thus, we have uncovered a new layer of regulation of the actin cytoskeleton by a member of a conserved protein family that has not been previously associated with a function in endocytosis. [Mh] Termos MeSH primário: Citoesqueleto de Actina/metabolismo Actinas/metabolismo Vesículas Revestidas por Clatrina/metabolismo Dineínas/metabolismo Endocitose Proteínas de Saccharomyces cerevisiae/metabolismo Saccharomyces cerevisiae/metabolismo [Mh] Termos MeSH secundário: Proteínas de Capeamento de Actina/metabolismo Complexo 2-3 de Proteínas Relacionadas à Actina/genética Complexo 2-3 de Proteínas Relacionadas à Actina/metabolismo Proteínas do Citoesqueleto/genética Proteínas do Citoesqueleto/metabolismo Dineínas/química Complexo de Proteínas da Cadeia de Transporte de Elétrons/genética Complexo de Proteínas da Cadeia de Transporte de Elétrons/metabolismo Genótipo Cinética Microscopia de Fluorescência Microscopia de Vídeo Modelos Moleculares Mutação Fenótipo Ligação Proteica Conformação Proteica Saccharomyces cerevisiae/genética Proteínas de Saccharomyces cerevisiae/química Proteínas de Saccharomyces cerevisiae/genética Transdução de Sinais Relação Estrutura-Atividade [Pt] Tipo de publicação: JOURNAL ARTICLE; VIDEO-AUDIO MEDIA [Nm] Nome de substância: 0 (Actin Capping Proteins); 0 (Actin-Related Protein 2-3 Complex); 0 (Actins); 0 (BBC1 protein, S cerevisiae); 0 (Cytoskeletal Proteins); 0 (Electron Transport Chain Complex Proteins); 0 (Saccharomyces cerevisiae Proteins); EC 3.6.4.2 (Dyneins) [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: 170715 [St] Status: MEDLINE [do] DOI: 10.1083/jcb.201604123

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[PMID]: 28642367 [Au] Autor: Vig AT; Földi I; Szikora S; Migh E; Gombos R; Tóth MÁ; Huber T; Pintér R; Talián GC; Mihály J; Bugyi B [Ad] Endereço: From the Department of Biophysics, Medical School, University of Pécs, Szigeti Str. 12, Pécs H-7624. [Ti] Título: The activities of the C-terminal regions of the formin protein disheveled-associated activator of morphogenesis (DAAM) in actin dynamics. [So] Source: J Biol Chem;292(33):13566-13583, 2017 Aug 18. [Is] ISSN: 1083-351X [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Disheveled-associated activator of morphogenesis (DAAM) is a diaphanous-related formin protein essential for the regulation of actin cytoskeleton dynamics in diverse biological processes. The conserved formin homology 1 and 2 (FH1-FH2) domains of DAAM catalyze actin nucleation and processively mediate filament elongation. These activities are indirectly regulated by the N- and C-terminal regions flanking the FH1-FH2 domains. Recently, the C-terminal diaphanous-autoregulatory domain (DAD) and the C terminus (CT) of formins have also been shown to regulate actin assembly by directly interacting with actin. Here, to better understand the biological activities of DAAM, we studied the role of DAD-CT regions of DAAM in its interaction with actin with biochemical and genetic approaches. We found that the DAD-CT region binds actin and that its main actin-binding element is the CT region, which does not influence actin dynamics on its own. However, we also found that it can tune the nucleating activity and the filament end-interaction properties of DAAM in an FH2 domain-dependent manner. We also demonstrate that DAD-CT makes the FH2 domain more efficient in antagonizing with capping protein. Consistently, data suggested that the CT region contributes to DAAM-mediated filopodia formation and dynamics in primary neurons. In conclusion, our results demonstrate that the CT region of DAAM plays an important role in actin assembly regulation in a biological context. [Mh] Termos MeSH primário: Citoesqueleto de Actina/metabolismo Proteínas Adaptadoras de Transdução de Sinal/metabolismo Proteínas de Drosophila/metabolismo Drosophila melanogaster/metabolismo Modelos Moleculares Proteínas do Tecido Nervoso/metabolismo Neurônios/metabolismo Pseudópodes/metabolismo [Mh] Termos MeSH secundário: Proteínas de Capeamento de Actina/química Proteínas de Capeamento de Actina/metabolismo Citoesqueleto de Actina/química Proteínas Adaptadoras de Transdução de Sinal/química Proteínas Adaptadoras de Transdução de Sinal/genética Substituição de Aminoácidos Animais Células Cultivadas Cristalografia por Raios X Proteínas de Drosophila/química Proteínas de Drosophila/genética Drosophila melanogaster/citologia Embrião não Mamífero/citologia Deleção de Genes Glutationa Transferase/química Glutationa Transferase/genética Glutationa Transferase/metabolismo Proteínas de Fluorescência Verde/genética Proteínas de Fluorescência Verde/metabolismo Mutação Proteínas do Tecido Nervoso/química Proteínas do Tecido Nervoso/genética Neurônios/citologia Fragmentos de Peptídeos/química Fragmentos de Peptídeos/genética Fragmentos de Peptídeos/metabolismo Conformação Proteica Domínios e Motivos de Interação entre Proteínas Estabilidade Proteica Proteínas Recombinantes de Fusão/química Proteínas Recombinantes de Fusão/metabolismo Homologia Estrutural de Proteína [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Actin Capping Proteins); 0 (Adaptor Proteins, Signal Transducing); 0 (DAAM protein, Drosophila); 0 (Drosophila Proteins); 0 (Nerve Tissue Proteins); 0 (Peptide Fragments); 0 (Recombinant Fusion Proteins); 147336-22-9 (Green Fluorescent Proteins); EC 2.5.1.18 (Glutathione Transferase) [Em] Mês de entrada: 1709 [Cu] Atualização por classe: 170906 [Lr] Data última revisão: 170906 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170624 [St] Status: MEDLINE [do] DOI: 10.1074/jbc.M117.799247

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[PMID]: 28542408 [Au] Autor: Li L; Chen X; Zhang S; Yang J; Chen D; Liu M; Zhang H; Zheng X; Wang P; Peng Y; Zhang Z [Ad] Endereço: Department of Plant Pathology, College of Plant Protection, Nanjing Agricultural University, and Key Laboratory of Integrated Management of Crop Diseases and Pests, Ministry of Education, Nanjing, China. [Ti] Título: MoCAP proteins regulated by MoArk1-mediated phosphorylation coordinate endocytosis and actin dynamics to govern development and virulence of Magnaporthe oryzae. [So] Source: PLoS Genet;13(5):e1006814, 2017 May. [Is] ISSN: 1553-7404 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Actin organization is a conserved cellular process that regulates the growth and development of eukaryotic cells. It also governs the virulence process of pathogenic fungi, such as the rice blast fungus Magnaporthe oryzae, with mechanisms not yet fully understood. In a previous study, we found that actin-regulating kinase MoArk1 displays conserved functions important in endocytosis and actin organization, and MoArk1 is required for maintaining the growth and full virulence of M. oryzae. To understand how MoArk1 might function, we identified capping protein homologs from M. oryzae (MoCAP) that interact with MoArk1 in vivo. MoCAP is heterodimer consisting of α and ß subunits MoCapA and MoCapB. Single and double deletions of MoCAP subunits resulted in abnormal mycelial growth and conidia formation. The ΔMocap mutants also exhibited reduced appressorium penetration and invasive hyphal growth within host cells. Furthermore, the ΔMocap mutants exhibited delayed endocytosis and abnormal cytoskeleton assembly. Consistent with above findings, MoCAP proteins interacted with MoAct1, co-localized with actin during mycelial development, and participated in appressorial actin ring formation. Further analysis revealed that the S85 residue of MoCapA and the S285 residue of MoCapB were subject to phosphorylation by MoArk1 that negatively regulates MoCAP functions. Finally, the addition of exogenous phosphatidylinositol 4,5-bisphosphate (PIP2) failed to modulate actin ring formation in ΔMocap mutants, in contrast to the wild-type strain, suggesting that MoCAP may also mediate phospholipid signaling in the regulation of the actin organization. These results together demonstrate that MoCAP proteins whose functions are regulated by MoArk1 and PIP2 are important for endocytosis and actin dynamics that are directly linked to growth, conidiation and pathogenicity of M. oryzae. [Mh] Termos MeSH primário: Proteínas de Capeamento de Actina/metabolismo Actinas/metabolismo Endocitose Proteínas Fúngicas/metabolismo Magnaporthe/metabolismo Processamento de Proteína Pós-Traducional Proteínas Serina-Treonina Quinases/metabolismo [Mh] Termos MeSH secundário: Proteínas de Capeamento de Actina/genética Magnaporthe/crescimento & desenvolvimento Magnaporthe/patogenicidade Micélio/crescimento & desenvolvimento Fosfatidilinositol 4,5-Difosfato/metabolismo Fosforilação Proteínas Serina-Treonina Quinases/genética Virulência [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Actin Capping Proteins); 0 (Actins); 0 (Fungal Proteins); 0 (Phosphatidylinositol 4,5-Diphosphate); EC 2.7.11.1 (Protein-Serine-Threonine Kinases) [Em] Mês de entrada: 1706 [Cu] Atualização por classe: 170628 [Lr] Data última revisão: 170628 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170526 [St] Status: MEDLINE [do] DOI: 10.1371/journal.pgen.1006814

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[PMID]: 28101692 [Au] Autor: Maninova M; Caslavsky J; Vomastek T [Ad] Endereço: Institute of Microbiology, Academy of Sciences of the Czech Republic, Videnska 1083, 142 00, Prague, Czech Republic. [Ti] Título: The assembly and function of perinuclear actin cap in migrating cells. [So] Source: Protoplasma;254(3):1207-1218, 2017 May. [Is] ISSN: 1615-6102 [Cp] País de publicação: Austria [La] Idioma: eng [Ab] Resumo: Stress fibers are actin bundles encompassing actin filaments, actin-crosslinking, and actin-associated proteins that represent the major contractile system in the cell. Different types of stress fibers assemble in adherent cells, and they are central to diverse cellular processes including establishment of the cell shape, morphogenesis, cell polarization, and migration. Stress fibers display specific cellular organization and localization, with ventral fibers present at the basal side, and dorsal fibers and transverse actin arcs rising at the cell front from the ventral to the dorsal side and toward the nucleus. Perinuclear actin cap fibers are a specific subtype of stress fibers that rise from the leading edge above the nucleus and terminate at the cell rear forming a dome-like structure. Perinuclear actin cap fibers are fixed at three points: both ends are anchored in focal adhesions, while the central part is physically attached to the nucleus and nuclear lamina through the linker of nucleoskeleton and cytoskeleton (LINC) complex. Here, we discuss recent work that provides new insights into the mechanism of assembly and the function of these actin stress fibers that directly link extracellular matrix and focal adhesions with the nuclear envelope. [Mh] Termos MeSH primário: Proteínas de Capeamento de Actina/metabolismo Movimento Celular/fisiologia Forma Celular/fisiologia Mecanotransdução Celular/fisiologia Fibras de Estresse/fisiologia [Mh] Termos MeSH secundário: Núcleo Celular/metabolismo Polaridade Celular/fisiologia Adesões Focais/fisiologia Seres Humanos Membrana Nuclear/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE; REVIEW [Nm] Nome de substância: 0 (Actin Capping Proteins) [Em] Mês de entrada: 1705 [Cu] Atualização por classe: 171012 [Lr] Data última revisão: 171012 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170120 [St] Status: MEDLINE [do] DOI: 10.1007/s00709-017-1077-0

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[PMID]: 28056837 [Au] Autor: Song P; He S; Zhou A; Lv G; Guo J; Zhou J; Han Y; Zhou H; Hao Z; Cong H [Ad] Endereço: Department of Parasitology, Shandong University School of Medicine, Jinan, Shandong Province, 250012, People's Republic of China. [Ti] Título: Vaccination with toxofilin DNA in combination with an alum-monophosphoryl lipid A mixed adjuvant induces significant protective immunity against Toxoplasma gondii. [So] Source: BMC Infect Dis;17(1):19, 2017 Jan 05. [Is] ISSN: 1471-2334 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: BACKGROUND: A widely prevalent disease, toxoplasmosis poses serious health threats to both humans and animals; therefore, development of an ideal DNA vaccine against Toxoplasma gondii is needed eagerly. The purpose of the present study is to assess the protective efficacy of a DNA vaccine encoding the T. gondii toxofilin gene (pEGFP-toxofilin). In addition, toxofilin DNA vaccine combined with the individual adjuvants, alum or monophosphoryl lipid A (MPLA), or a mixture of alum-MPLA adjuvant were screened for their ability to enhance antibody responses. METHODS: Using bioinformatics, we analyzed the gene and amino acid sequences of the toxofilin protein, recognizing and identifying several potential linear B and T helper (Th)-1 cell epitopes. BALB/c mice were immunized three times with either toxofilin DNA vaccine alone or in combination with the adjuvants such as alum, MPLA or an alum-MPLA mixture. The systemic immune response was evaluated by cytokine, the percentage of CD4 (+) and CD8 (+) T cells and specific antibody measurement. Two weeks after the last immunization, protective efficacy was evaluated by challenging intraperitoneally with 1 × 10 tachyzoites of T. gondii or intragastrically with 20 cysts of T. gondii PRU strain. RESULTS: All experimentally immunized mice developed strong humoral and cellular immune responses compared with the control groups. Moreover, by comparison with the non-adjuvant toxofilin DNA vaccine group, adding alum adjuvant to toxofilin DNA vaccine resulted in an increase in humoral response and a skewed Th2 response. However, the MPLA adjuvant with toxofilin DNA vaccine induced significantly enhanced humoral and Th1-biased immune responses. Importantly, the co-administration of alum-MPLA adjuvant in combination with the toxofilin DNA vaccine shifted the Th2 immune response to a Th1 response compared with the alum-toxofilin group, and elicited the strongest humoral and Th1 responses among all the groups. At the same time, a longer survival time and less cyst amounts against T. gondii infection were also observed in the alum-MPLA-toxofilin group in comparison with single or no adjuvant groups. CONCLUSIONS: Toxoplasma gondii toxofilin is a promising vaccine candidate that warrants further development. Co-administration of the alum-MPLA adjuvant mixture with DNA vaccine could effectively enhance immunogenicity and strongly skew the cellular immune response towards a Th1 phenotype. [Mh] Termos MeSH primário: Proteínas de Capeamento de Actina/genética Adjuvantes Imunológicos/farmacologia Lipídeo A/análogos & derivados Proteínas de Protozoários/genética Vacinas Protozoárias/farmacologia Toxoplasmose/imunologia [Mh] Termos MeSH secundário: Proteínas de Capeamento de Actina/imunologia Compostos de Alúmen/farmacologia Animais Formação de Anticorpos/efeitos dos fármacos Feminino Imunidade Celular Lipídeo A/imunologia Lipídeo A/farmacologia Camundongos Endogâmicos BALB C Proteínas de Protozoários/imunologia Vacinas Protozoárias/imunologia Toxoplasma/imunologia Toxoplasma/patogenicidade Toxoplasmose/prevenção & controle Vacinas de DNA/imunologia Vacinas de DNA/farmacologia [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Actin Capping Proteins); 0 (Adjuvants, Immunologic); 0 (Alum Compounds); 0 (Lipid A); 0 (Protozoan Proteins); 0 (Protozoan Vaccines); 0 (Vaccines, DNA); 0 (toxofilin protein, Toxoplasma gondii); 34S289N54E (aluminum sulfate); MWC0ET1L2P (monophosphoryl lipid A) [Em] Mês de entrada: 1709 [Cu] Atualização por classe: 170904 [Lr] Data última revisão: 170904 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170107 [St] Status: MEDLINE [do] DOI: 10.1186/s12879-016-2147-1

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[PMID]: 27909046 [Au] Autor: Li J; Cao L; Staiger CJ [Ad] Endereço: Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907-2064 (J.L., L.C., C.J.S.); and. [Ti] Título: Capping Protein Modulates Actin Remodeling in Response to Reactive Oxygen Species during Plant Innate Immunity. [So] Source: Plant Physiol;173(2):1125-1136, 2017 Feb. [Is] ISSN: 1532-2548 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Plants perceive microbe-associated molecular patterns and damage-associated molecular patterns to activate innate immune signaling events, such as bursts of reactive oxygen species (ROS). The actin cytoskeleton remodels during the first 5 min of innate immune signaling in Arabidopsis (Arabidopsis thaliana) epidermal cells; however, the immune signals that impinge on actin cytoskeleton and its response regulators remain largely unknown. Here, we demonstrate that rapid actin remodeling upon elicitation with diverse microbe-associated molecular patterns and damage-associated molecular patterns represent a conserved plant immune response. Actin remodeling requires ROS generated by the defense-associated NADPH oxidase, RBOHD. Moreover, perception of flg22 by its cognate receptor complex triggers actin remodeling through the activation of RBOHD-dependent ROS production. Our genetic studies reveal that the ubiquitous heterodimeric capping protein transduces ROS signaling to the actin cytoskeleton during innate immunity. Additionally, we uncover a negative feedback loop between actin remodeling and flg22-induced ROS production. [Mh] Termos MeSH primário: Proteínas de Capeamento de Actina/metabolismo Actinas/metabolismo Proteínas de Arabidopsis/metabolismo Arabidopsis/imunologia Imunidade Inata/efeitos dos fármacos Imunidade Vegetal Espécies Reativas de Oxigênio/metabolismo [Mh] Termos MeSH secundário: Citoesqueleto de Actina/efeitos dos fármacos Citoesqueleto de Actina/metabolismo Alarminas Arabidopsis/efeitos dos fármacos Compostos de Bifenilo/farmacologia Flagelina/metabolismo Peróxido de Hidrogênio/farmacologia NADPH Oxidases/metabolismo Oniocompostos/farmacologia Padrões Moleculares Associados a Patógenos/metabolismo Imunidade Vegetal/efeitos dos fármacos Transdução de Sinais/efeitos dos fármacos [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Actin Capping Proteins); 0 (Actins); 0 (Alarmins); 0 (Arabidopsis Proteins); 0 (Biphenyl Compounds); 0 (Onium Compounds); 0 (Pathogen-Associated Molecular Pattern Molecules); 0 (Reactive Oxygen Species); 10182-84-0 (diphenyliodonium); 12777-81-0 (Flagellin); BBX060AN9V (Hydrogen Peroxide); EC 1.6.3.- (NADPH Oxidases) [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: 161203 [St] Status: MEDLINE [do] DOI: 10.1104/pp.16.00992

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[PMID]: 27922825 [Au] Autor: McMillen LM; Vavylonis D [Ad] Endereço: Department of Physics, Lehigh University, Bethlehem PA 18015, USA. [Ti] Título: Model of turnover kinetics in the lamellipodium: implications of slow- and fast- diffusing capping protein and Arp2/3 complex. [So] Source: Phys Biol;13(6):066009, 2016 Dec 06. [Is] ISSN: 1478-3975 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: Cell protrusion through polymerization of actin filaments at the leading edge of motile cells may be influenced by spatial gradients of diffuse actin and regulators. Here we study the distribution of two of the most important regulators, capping protein and Arp2/3 complex, which regulate actin polymerization in the lamellipodium through capping and nucleation of free barbed ends. We modeled their kinetics using data from prior single molecule microscopy experiments on XTC cells. These experiments have provided evidence for a broad distribution of diffusion coefficients of both capping protein and Arp2/3 complex. The slowly diffusing proteins appear as extended 'clouds' while proteins bound to the actin filament network appear as speckles that undergo retrograde flow. Speckle appearance and disappearance events correspond to assembly and dissociation from the actin filament network and speckle lifetimes correspond to the dissociation rate. The slowly diffusing capping protein could represent severed capped actin filament fragments or membrane-bound capping protein. Prior evidence suggests that slowly diffusing Apr2/3 complex associates with the membrane. We use the measured rates and estimates of diffusion coefficients of capping protein and Arp2/3 complex in a Monte Carlo simulation that includes particles in association with a filament network and diffuse in the cytoplasm. We consider two separate pools of diffuse proteins, representing fast and slowly diffusing species. We find a steady state with concentration gradients involving a balance of diffusive flow of fast and slow species with retrograde flow. We show that simulations of FRAP are consistent with prior experiments performed on different cell types. We provide estimates for the ratio of bound to diffuse complexes and calculate conditions where Arp2/3 complex recycling by diffusion may become limiting. We discuss the implications of slowly diffusing populations and suggest experiments to distinguish among mechanisms that influence long range transport. [Mh] Termos MeSH primário: Proteínas de Capeamento de Actina/metabolismo Complexo 2-3 de Proteínas Relacionadas à Actina/metabolismo Modelos Teóricos Pseudópodes/metabolismo [Mh] Termos MeSH secundário: Citoesqueleto de Actina/metabolismo Complexo 2-3 de Proteínas Relacionadas à Actina/química Animais Membrana Celular/metabolismo Citoesqueleto/metabolismo Difusão Recuperação de Fluorescência Após Fotodegradação Cinética Método de Monte Carlo [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Actin Capping Proteins); 0 (Actin-Related Protein 2-3 Complex) [Em] Mês de entrada: 1710 [Cu] Atualização por classe: 171017 [Lr] Data última revisão: 171017 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 161207 [St] Status: MEDLINE

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[PMID]: 27647239 [Au] Autor: González-Rodríguez VE; Garrido C; Cantoral JM; Schumacher J [Ad] Endereço: Departamento de Biomedicina, Biotecnología y Salud Pública, Laboratorio de Microbiología, Facultad de Ciencias de Mar y Ambientales, Instituto Universitario de Investigación Vitivinícola y Agroalimentaria (IVAGRO), Universidad de Cádiz, Polígono Río San Pedro, 11510 Puerto Real, Spain. Electronic ad [Ti] Título: The F-actin capping protein is required for hyphal growth and full virulence but is dispensable for septum formation in Botrytis cinerea. [So] Source: Fungal Biol;120(10):1225-35, 2016 Oct. [Is] ISSN: 1878-6146 [Cp] País de publicação: Netherlands [La] Idioma: eng [Ab] Resumo: Filamentous (F-) actin is an integral part of the cytoskeleton allowing for cell growth, intracellular motility, and cytokinesis of eukaryotic cells. Its assembly from G-actin monomers and its disassembly are tightly regulated processes involving a number of actin-binding proteins (ABPs) such as F-actin nucleators and cross-linking proteins. F-actin capping protein (CP) is an alpha/beta heterodimer known from yeast and higher eukaryotes to bind to the fast growing ends of the actin filaments stabilizing them. In this study, we identified the orthologs of the two CP subunits, named BcCPA1 and BcCPB1, in the plant pathogenic fungus Botrytis cinerea and showed that the two proteins physically interact in a yeast two-hybrid approach. GFP-BcCPA1 fusion proteins were functional and localized to the assumed sites of F-actin accumulation, i.e. to the hyphal tips and the sites of actin ring formation. Deletion of bccpa1 had a profound effect on hyphal growth, morphogenesis, and virulence indicating the importance of F-actin capping for an intact actin cytoskeleton. As polarized growth - unlike septum formation - is impaired in the mutants, it can be concluded that the organization and/or localization of actin patches and cables are disturbed rather than the functionality of the actin rings. [Mh] Termos MeSH primário: Proteínas de Capeamento de Actina/metabolismo Botrytis/metabolismo Proteínas Fúngicas/metabolismo Hifas/crescimento & desenvolvimento Phaseolus/microbiologia Doenças das Plantas/microbiologia [Mh] Termos MeSH secundário: Proteínas de Capeamento de Actina/genética Sequência de Aminoácidos Botrytis/genética Botrytis/crescimento & desenvolvimento Botrytis/patogenicidade Proteínas Fúngicas/genética Hifas/genética Hifas/metabolismo Dados de Sequência Molecular Alinhamento de Sequência Virulência [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Actin Capping Proteins); 0 (Fungal Proteins) [Em] Mês de entrada: 1707 [Cu] Atualização por classe: 170718 [Lr] Data última revisão: 170718 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 160921 [St] Status: MEDLINE

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[PMID]: 27206859 [Au] Autor: Baker K; Kirkham S; Halova L; Atkin J; Franz-Wachtel M; Cobley D; Krug K; Macek B; Mulvihill DP; Petersen J [Ad] Endereço: School of Biosciences, University of Kent, Giles Lane, Canterbury, Kent CT2 7NJ, UK. [Ti] Título: TOR complex 2 localises to the cytokinetic actomyosin ring and controls the fidelity of cytokinesis. [So] Source: J Cell Sci;129(13):2613-24, 2016 07 01. [Is] ISSN: 1477-9137 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: The timing of cell division is controlled by the coupled regulation of growth and division. The target of rapamycin (TOR) signalling network synchronises these processes with the environmental setting. Here, we describe a novel interaction of the fission yeast TOR complex 2 (TORC2) with the cytokinetic actomyosin ring (CAR), and a novel role for TORC2 in regulating the timing and fidelity of cytokinesis. Disruption of TORC2 or its localisation results in defects in CAR morphology and constriction. We provide evidence that the myosin II protein Myp2 and the myosin V protein Myo51 play roles in recruiting TORC2 to the CAR. We show that Myp2 and TORC2 are co-dependent upon each other for their normal localisation to the cytokinetic machinery. We go on to show that TORC2-dependent phosphorylation of actin-capping protein 1 (Acp1, a known regulator of cytokinesis) controls CAR stability, modulates Acp1-Acp2 (the equivalent of the mammalian CAPZA-CAPZB) heterodimer formation and is essential for survival upon stress. Thus, TORC2 localisation to the CAR, and TORC2-dependent Acp1 phosphorylation contributes to timely control and the fidelity of cytokinesis and cell division. [Mh] Termos MeSH primário: Proteínas de Capeamento de Actina/genética Citocinese/genética Complexos Multiproteicos/genética Cadeias Pesadas de Miosina/genética Miosinas/genética Proteínas de Schizosaccharomyces pombe/genética Serina-Treonina Quinases TOR/genética [Mh] Termos MeSH secundário: Proteínas de Capeamento de Actina/metabolismo Actinas/genética Actomiosina/genética Actomiosina/metabolismo Divisão Celular/genética Alvo Mecanístico do Complexo 2 de Rapamicina Complexos Multiproteicos/metabolismo Cadeias Pesadas de Miosina/metabolismo Miosinas/metabolismo Fosforilação Schizosaccharomyces/genética Proteínas de Schizosaccharomyces pombe/metabolismo Serina-Treonina Quinases TOR/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Actin Capping Proteins); 0 (Actins); 0 (Multiprotein Complexes); 0 (Myp2 protein, S pombe); 0 (Schizosaccharomyces pombe Proteins); 9013-26-7 (Actomyosin); EC 2.7.1.1 (TOR Serine-Threonine Kinases); EC 2.7.11.1 (Mechanistic Target of Rapamycin Complex 2); EC 3.6.4.1 (Myo51 protein, S pombe); EC 3.6.4.1 (Myosin Heavy Chains); EC 3.6.4.1 (Myosins) [Em] Mês de entrada: 1708 [Cu] Atualização por classe: 171124 [Lr] Data última revisão: 171124 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 160522 [St] Status: MEDLINE [do] DOI: 10.1242/jcs.190124

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MEDLINE

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[PMID]: 27093378 [Au] Autor: Xu X; Hu H; Wang X; Ye W; Su H; Hu Y; Dong L; Zhang R; Ying K [Ad] Endereço: a Department of Respiratory Medicine , Sir Run Run Shaw Hospital , Zhejiang University School of Medicine , Hangzhou, Zhejiang , China. [Ti] Título: Involvement of CapG in proliferation and apoptosis of pulmonary arterial smooth muscle cells and in hypoxia-induced pulmonary hypertension rat model. [So] Source: Exp Lung Res;42(3):142-53, 2016 Apr. [Is] ISSN: 1521-0499 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: PURPOSE: Actin-binding protein capping protein gelsolin-like (CapG) was preferentially expressed in human pulmonary arterial smooth muscle cells (PASMCs) under hypoxia, and reduced CapG expression was accompanied by impaired migration ability in vitro. We intended to investigate the effects of CapG on rat PASMCs and hypoxia-induced pulmonary hypertension (HPH) rat model. MATERIALS AND METHODS: We investigated the effect of RNA interference-medicated down-regulation of CapG expression in rat PASMCs as well as in HPH rat model. The proliferation, apoptosis and cell cycle of PASMCs were evaluated. The HPH rat model was established by intratracheal instillation of lentiviral vector and subsequent hypoxia exposure for four weeks. Right ventricular systolic pressure, right ventricular hypertrophy and the percentage of medial wall thickness were measured to evaluate the development of HPH. RESULTS: Knock-down CapG in PASMCs resulted in decreased proliferation, increased apoptosis and induced cell cycle inhibition. Down-regulation of CapG expression locally could attenuate pulmonary hypertension, pulmonary vascular remodeling and right ventricular hypertrophy in HPH rat model. CONCLUSIONS: Our study indicated that CapG participated in the pathogenesis of pulmonary vascular remodeling in HPH rats, which was probably mediated by promoting the proliferation and inhibiting the apoptosis of PASMCs. We proposed CapG modulating protective effects of pulmonary hypertension. [Mh] Termos MeSH primário: Proteínas de Capeamento de Actina/metabolismo Apoptose/fisiologia Proliferação Celular/fisiologia Gelsolina/metabolismo Hipertensão Pulmonar/fisiopatologia Miócitos de Músculo Liso/fisiologia Artéria Pulmonar/fisiologia [Mh] Termos MeSH secundário: Animais Regulação para Baixo/fisiologia Hipertensão Pulmonar/metabolismo Hipertrofia Ventricular Direita/metabolismo Hipertrofia Ventricular Direita/fisiopatologia Hipóxia/metabolismo Hipóxia/fisiopatologia Masculino Miócitos de Músculo Liso/metabolismo Artéria Pulmonar/metabolismo Ratos Ratos Sprague-Dawley Remodelação Vascular/fisiologia [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Actin Capping Proteins); 0 (Gelsolin) [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: 160420 [St] Status: MEDLINE [do] DOI: 10.3109/01902148.2016.1160304

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