Search results for "cytoskeleton"

showing 10 items of 272 documents

SIK2 orchestrates actin-dependent host response upon Salmonella infection

2021

Significance Through conducting quantitative proteomics upon Salmonella infection, we identified a SIK2 signaling network, implementing the kinase into a so far concealed biological function. Our data exposed SIK2 as a central orchestrator of an actin regulatory network, coordinating the stability of Salmonella-containing vacuole (SCV) and cellular actin assembly, in order to limit the acute phase of the infection. Most strikingly, SIK2 is not exclusively acting locally on actin assembly associated with the SCV but impacts the actin cytoskeleton architecture in its entirety upon Salmonella infection. Our work provides a mechanistic framework for how the actin cytoskeleton is regulated and h…

ProteomicsSalmonellaactin cytoskeletonImmunoblottingArp2/3 complexSalmonella infectionmacromolecular substancesProtein Serine-Threonine Kinasesmedicine.disease_causeBiochemistry03 medical and health sciencesMice0302 clinical medicineSalmonellamedicineXenophagyAnimalsHumansArp2/3 complexProtein Interaction MapsPhosphorylationActinCells Cultured030304 developmental biologyActin nucleation0303 health sciencesMultidisciplinarybiologyEpithelial CellsBiological Sciencesmedicine.diseaseActin cytoskeletonHCT116 CellsPhosphoproteinsActinsCell biologySalmonella-containing vacuoleHEK293 CellsFormins407Host-Pathogen Interactionsbiology.proteinRNA Interference030217 neurology & neurosurgeryhost–pathogen interactionsHeLa CellsSignal TransductionProceedings of the National Academy of Sciences of the United States of America
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Membrane vesicles containing matrix metalloproteinase-9 and fibroblast growth factor-2 are released into the extracellular space from mouse mesoangio…

2010

Certain proteins, including fibroblast growth factor-2 (FGF-2) and matrix metalloproteinase-9 (MMP-9), have proved very effective in increasing the efficacy of mesoangioblast stem cell therapy in repairing damaged tissue. We provide the first evidence that mouse mesoangioblast stem cells release FGF-2 and MMP-9 in their active form through the production of membrane vesicles. These vesicles are produced and turned over continuously, but are stable for some time in the extracellular milieu. Mesoangioblasts shed membrane vesicles even under oxygen tensions that are lower than those typically used for cell culture and more like those of mouse tissues. These findings suggest that mesoangioblast…

ProteomicsTime FactorsPhysiologyClinical BiochemistryBiologyFibroblast growth factorCell LineMiceMembrane MicrodomainsTubulinParacrine CommunicationmedicineExtracellularAnimalsSecretionSettore BIO/06 - Anatomia Comparata E CitologiaFibroblastCytoskeletonMembrane vesicles MMP9 FGF2 mouse mesoangioblastMesoangioblastSecretory VesiclesVesicleBiological TransportMesenchymal Stem CellsCell BiologyCell biologyOxygenmedicine.anatomical_structureMatrix Metalloproteinase 9Cell cultureFibroblast Growth Factor 2Stem cellExtracellular Space
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B-Raf Acts via the ROCKII/LIMK/Cofilin Pathway To Maintain Actin Stress Fibers in Fibroblasts

2004

Members of the Raf family of serine/threonine protein kinases have been well studied in a variety of organisms ranging from Drosophila to humans. Three raf homologues (raf-1, B-raf, and A-raf) exist in mammals, while a single prototypic homologue exists in lower organisms. A wealth of genetic and biochemical data have indicated that Raf family members are signaling kinases that are integral components of the conserved Ras/Raf/MEK/ERK signaling cascade. Following activation by Ras-dependent mechanisms, Raf protein kinases act as mitogen-activated protein (MAP) kinase kinase kinases, which phosphorylate and activate the type 1/2 MAP kinase kinases, also known as MEK1/2. These dual-specificity…

Proto-Oncogene Proteins B-rafMAPK/ERK pathwaymacromolecular substancesProtein Serine-Threonine KinasesTransfectionCell LineProto-Oncogene Proteins B-rafLim kinaseMiceCell MovementStress FibersAnimalsHumansPhosphorylationKinase activityCell Growth and DevelopmentMolecular BiologyRho-associated protein kinaseCytoskeletonrho-Associated KinasesbiologyKinaseMicrofilament ProteinsIntracellular Signaling Peptides and ProteinsLim KinasesCell BiologyFibroblastsMolecular biologyActinsCell biologyProto-Oncogene Proteins c-rafActin Depolymerizing FactorsMitogen-activated protein kinasebiology.proteinProto-Oncogene Proteins c-rafMitogen-Activated Protein KinasesProtein KinasesSignal TransductionMolecular and Cellular Biology
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The Enterotoxin from Clostridium difficile (ToxA) Monoglucosylates the Rho Proteins

1995

The enterotoxin from Clostridium difficile (ToxA) is one of the causative agents of the antibiotic-associated pseudomembranous colitis. In cultured monolayer cells ToxA exhibits cytotoxic activity to induce disassembly of the actin cytoskeleton, which is accompanied by morphological changes. ToxA-induced depolymerization of actin filaments is correlated with a decrease in the ADP-ribosylation of the low molecular mass GTP-binding Rho proteins (Just, I., Selzer, J., von Eichel-Streiber, C., and Aktories, K. (1995) J. Clin. Invest. 95, 1026-1031). Here we report on the identification of the ToxA-induced modification of Rho. Applying electrospray mass spectrometry, the mass of the modification…

RHOAGlycoside HydrolasesBacterial ToxinsClostridium difficile toxin ARAC1macromolecular substancesEnterotoxinBiochemistrySubstrate SpecificityEnterotoxinsGTP-Binding ProteinsTumor Cells CulturedAmino AcidsMolecular BiologyActinbiologyMolecular massClostridioides difficileCell BiologyPseudomembranous colitisActin cytoskeletonMolecular biologycarbohydrates (lipids)GlucoseBiochemistrybiology.proteinrhoA GTP-Binding ProteinJournal of Biological Chemistry
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Inhibition of Rac1 GTPase Decreases Vascular Oxidative Stress, Improves Endothelial Function, and Attenuates Atherosclerosis Development in Mice

2021

Aims: Oxidative stress and inflammation contribute to atherogenesis. Rac1 GTPase regulates pro-oxidant NADPH oxidase activity, reactive oxygen species (ROS) formation, actin cytoskeleton organization and monocyte adhesion. We investigated the vascular effects of pharmacological inhibition of Rac1 GTPase in mice.Methods and Results: We treated wild-type and apolipoprotein E-deficient (ApoE−/−) mice with Clostridium sordellii lethal toxin (LT), a Rac1 inhibitor, and assessed vascular oxidative stress, expression and activity of involved proteins, endothelial function, macrophage infiltration, and atherosclerosis development. LT-treated wild-type mice displayed decreased vascular NADPH oxidase…

RHOAInflammationVascular permeabilityfree radicalsPharmacologyCardiovascular Medicinemedicine.disease_causeActin cytoskeleton organizationendothelial functionmedicineoxidative stressDiseases of the circulatory (Cardiovascular) systemddc:610Endothelial dysfunctionOriginal Researchchemistry.chemical_classificationReactive oxygen speciesNADPH oxidaseGTPasesbiologymedicine.diseasechemistryatherosclerosis endothelial function oxidative stress free radicals Rac1 GTPasesRC666-701biology.proteinmedicine.symptomatherosclerosisCardiology and Cardiovascular MedicineOxidative stressRac1Frontiers in Cardiovascular Medicine
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Clostridium difficile toxin A induces expression of the stress-induced early gene product RhoB.

2004

Clostridium difficile toxin A monoglucosylates the Rho family GTPases Rho, Rac, and Cdc42. Glucosylation leads to the functional inactivation of Rho GTPases and causes disruption of the actin cytoskeleton. A cDNA microarray revealed the immediate early gene rhoB as the gene that was predominantly up-regulated in colonic CaCo-2 cells after treatment with toxin A. This toxin A effect was also detectable in epithelial cells such as HT29 and Madin-Darby canine kidney cells, as well as NIH 3T3 fibroblasts. The expression of RhoB was time-dependent and correlated with the morphological changes of cells. The up-regulation of RhoB was approximately 15-fold and was based on the de novo synthesis of …

RHOAPyridinesRHOBBacterial ToxinsClostridium difficile toxin ARAC1GTPaseBiochemistryp38 Mitogen-Activated Protein KinasesGene Expression Regulation EnzymologicGene productEnterotoxinsStress PhysiologicalRhoB GTP-Binding ProteinHumansrhoB GTP-Binding ProteinMolecular BiologyOligonucleotide Array Sequence AnalysisbiologyImidazolesCell BiologyRhoBClostridium difficileActin cytoskeletonMolecular biologyUp-Regulationbiology.proteinGene expressionCaco-2 CellsThe Journal of biological chemistry
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Megakaryocytic cell line-specific hyperploidy by cytotoxic necrotizing factor bacterial toxins

1996

Cytotoxic necrotizing factor (CNF) toxins, isolated from certain Escherichia coli strains known to cause intestinal and extra intestinal infections, induce reorganization of the actin cytoskeleton and generate hyperploidy in adherent cell lines. We have examined the effect of CNF toxin on one of the few cell types that naturally increase nuclear DNA content, megakaryocytes. Our studies show that only hematopoietic cells capable of differentiating along the megakaryocyte lineage responded to the CNF2 toxin by becoming polyploid and by reorganizing actin. The K562, HEL, and CHRF-288–11 cell lines can be induced with phorbol ester to differentiate along the megakaryocyte lineage, and these cel…

RHOAbiologyCellular differentiation[SDV]Life Sciences [q-bio]ImmunologyCell BiologyHematologyActin cytoskeletonBiochemistryCell biology[SDV] Life Sciences [q-bio]medicine.anatomical_structureBiochemistryMegakaryocyteCell cultureFACTEUR CYTOTOXIQUE NECROSANTbiology.proteinmedicineCytotoxic T cellCytoskeletonActin
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p38α deficiency and oxidative stress cause cytokinesis failure in hepatocytes.

2015

Cytokinesis is the last step in mitosis and it implies re-organization of the actin cytoskeleton. Its failure is one of the major mechanisms of polyploidy and binucleation in mammals. Our aims were 1) to assess the role of redox-sensitive p38α MAPK in cytokinesis by studying the liver of wild type mice or liver-specific p38α knock-out mice; 2) to assess the role of oxidative stress associated with hepatocyte isolation on cytokinesis. When p38α was down-regulated in hepatocytes, MK2 phosphorylation on threonine 334 was completely abrogated. Activation of MNK-1, required for abscission of the intercellular bridge, was diminished. Key proteins of the RhoA pathway (phospho-PRK2, nuclear phospho…

RHOAmacromolecular substancesBiologyCell cycleCofilinActin cytoskeletonBiochemistryCell biologyCytosolPhysiology (medical)biology.proteinMitosisCytokinesisActinFree radical biologymedicine
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Reconstitution of vesicular transport to Rab11-positive recycling endosomes in vitro.

2003

Rab GTPases are key regulators of vesicular protein transport in both the endocytic and exocytic pathways. In endocytosis and recycling, Rab11 plays a role in receptor recycling to plasma membrane via the pericentriolar recycling compartment. However, little is known about the molecular requirements and partners that promote transport through Rab11-positive recycling endosomes. Here, we report a novel approach to reconstitute transport to immunoabsorbed recycling endosomes in vitro. We show that transport is temperature-, energy-, and time-dependent and requires the presence of Rab proteins, as it is inhibited by the Rab-interacting protein Rab GDP-dissociation inhibitor that removes Rab pr…

Receptor recyclingCytochalasin DEndosomeEndocytic cycleBiophysicsVesicular Transport ProteinsCHO CellsEndosomesEndocytosisBiochemistryCricetulusCricetinaeReceptors TransferrinAnimalsVesicular Protein TransportTransport VesiclesMolecular BiologyGuanine Nucleotide Dissociation InhibitorsChemistryCell BiologyActin cytoskeletonAdaptation PhysiologicalCell biologyVesicular transport proteinProtein Transportrab GTP-Binding ProteinsRabBiochemical and biophysical research communications
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Rho protein-mediated changes in the structure of the actin cytoskeleton regulate human inducible NO synthase gene expression ☆ ☆This article contains…

2003

Rho proteins (Rho, Rac, Cdc 42) are known to control the organization of the actin cytoskeleton as well as gene expression. Inhibition of Rho proteins by Clostridium difficile toxin B disrupted the F-actin cytoskeleton and enhanced cytokine-induced inducible nitric oxide synthase (iNOS) expression in human epithelial cells. Also specific inhibition by Y-27632 of p160ROCK, which mediates Rho effects on actin fibers, caused a disruption of the actin cytoskeleton and a superinduction of cytokine-induced iNOS expression. Accordingly, direct disruption of the actin cytoskeleton by cytochalasin D, latrunculin B, or jasplakinolide enhanced cytokine-induced iNOS expression. The transcription factor…

Regulation of gene expressionActin remodelingClostridium difficile toxin Bmacromolecular substancesCell BiologyBiologyActin cytoskeletonMolecular biologyCell biologyProfilinSerum response factorbiology.proteinMDia1CytoskeletonExperimental Cell Research
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