Search results for "Protein kinases"

showing 10 items of 427 documents

Polar Localization of a Tripartite Complex of the Two-Component System DcuS/DcuR and the Transporter DctA in Escherichia coli Depends on the Sensor K…

2014

The C4-dicarboxylate responsive sensor kinase DcuS of the DcuS/DcuR two-component system of E. coli is membrane-bound and reveals a polar localization. DcuS uses the C4-dicarboxylate transporter DctA as a co-regulator forming DctA/DcuS sensor units. Here it is shown by fluorescence microscopy with fusion proteins that DcuS has a dynamic and preferential polar localization, even at very low expression levels. Single assemblies of DcuS had high mobility in fast time lapse acquisitions, and fast recovery in FRAP experiments, excluding polar accumulation due to aggregation. DctA and DcuR fused to derivatives of the YFP protein are dispersed in the membrane or in the cytosol, respectively, when …

Yellow fluorescent proteinCardiolipinslcsh:MedicineMicrobiologyMreBMicrobial PhysiologyBacterial Physiologylcsh:ScienceCytoskeletonMicrobial MetabolismDicarboxylic Acid TransportersMultidisciplinaryEscherichia coli K12biologyBacterial GrowthEscherichia coli Proteinslcsh:RMicrobial Growth and DevelopmentBiology and Life SciencesFluorescence recovery after photobleachingBacteriologyFusion proteinTwo-component regulatory systemBacterial BiochemistryTransport proteinDNA-Binding ProteinsProtein TransportBiochemistryCytoplasmMultiprotein ComplexesBiophysicsbiology.proteinlcsh:QProtein KinasesResearch ArticleDevelopmental BiologyTranscription FactorsPLoS ONE
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Polar accumulation of the metabolic sensory histidine kinases DcuS and CitA in Escherichia coli

2008

Signal transduction in prokaryotes is frequently accomplished by two-component regulatory systems in which a histidine protein kinase is the sensory component. Many of these sensory kinases control metabolic processes that do not show an obvious requirement for inhomogeneous distribution within bacterial cells. Here, the sensory kinases DcuS and CitA, two histidine kinases of Escherichia coli, were investigated. Both are membrane-integral and involved in the regulation of carboxylate metabolism. The two-component sensors were fused with yellow fluorescent protein (YFP) and live images of immobilized cells were obtained by confocal laser fluorescence microscopy. The fluorescence of the fusio…

Yellow fluorescent proteinbiologyKinaseEscherichia coli ProteinsRecombinant Fusion ProteinsCell PolarityMicrobiologyFusion proteinLuminescent ProteinsProtein TransportBacterial ProteinsBiochemistryCytoplasmEscherichia colibiology.proteinSignal transductionCell fractionationProtein kinase AProtein KinasesHistidineMicrobiology
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Sea urchin deciliation induces thermoresistance and activates the p38 mitogen-activated protein kinase pathway.

2003

In this study, we demonstrate by a variety of approaches (ie, morphological analysis, Western blots, immunolocalization, and the use of specific antibodies) that hyperosmotic deciliation stress of sea urchin embryos induces a thermotolerant response. Deciliation is also able to activate a phosphorylation signaling cascade the effector of which might be the p38 stress-activated protein kinase because we found that the administration of the p38 inhibitor SB203580 to sea urchin deciliated gastrula embryos makes the hyperosmotic deciliation stress lethal.

animal structuresHot TemperaturePyridinesp38 mitogen-activated protein kinasesSEA URCHIN DECILIATION p38MAP KINASEBiochemistryp38 Mitogen-Activated Protein KinasesEnzyme activatorStress Physiologicalbiology.animalAnimalsCiliaSettore BIO/06 - Anatomia Comparata E CitologiaPhosphorylationProtein kinase ASea urchinbiologyEffectorImidazolesAntibodies MonoclonalCell BiologyGastrulaOriginal ArticlesMolecular biologyBlotEnzyme ActivationSea Urchinsembryonic structuresPhosphorylationElectrophoresis Polyacrylamide GelSignal transductionMitogen-Activated Protein KinasesSignal TransductionCell stresschaperones
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Cabut, a C2H2 zinc finger transcription factor, is required during Drosophila dorsal closure downstream of JNK signaling.

2005

AbstractDuring dorsal closure, the lateral epithelia on each side of the embryo migrate dorsally over the amnioserosa and fuse at the dorsal midline. Detailed genetic studies have revealed that many molecules are involved in this epithelial sheet movement, either with a signaling function or as structural or motor components of the process. Here, we report the characterization of cabut (cbt), a new Drosophila gene involved in dorsal closure. cbt is expressed in the yolk sac nuclei and in the lateral epidermis. The Cbt protein contains three C2H2-type zinc fingers and a serine-rich domain, suggesting that it functions as a transcription factor. cbt mutants die as embryos with dorsal closure …

animal structuresMorphogenesisBiologyCabutZinc fingerMorphogenesismedicineAnimalsDrosophila ProteinsDorsal closureYolk sacMolecular BiologyTranscription factorYolk nucleiCytoskeletonGeneticsZinc fingerEpidermis (botany)C2H2 Zinc FingerJNK Mitogen-Activated Protein KinasesZinc FingersCell BiologyDorsal closureCell biologymedicine.anatomical_structureDrosophila melanogasterEpidermal Cellsembryonic structuresMutationJNK cascadeDrosophilaJNKDevelopmental BiologySignal TransductionTranscription FactorsDevelopmental biology
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A frozen analogue approach to aminopyridinylimidazoles leading to novel and promising p38 MAP kinase inhibitors.

2012

In this study we report the design, synthesis, and biological evaluation of constrained aminopyridinylimidazoles as p38α MAP kinase inhibitors. The frozen analogue approach focused on the pyridinyl unit, using purine bioisosteres as constrained structure analogues. The identification of the most potent bioisostere was followed by a further derivatization to address hydrophobic region II. In combination with C-2 modifications of the imidazole core, we were able to design highly active inhibitors on the p38α MAP kinase. The inhibitor design presented herein represents a promising and highly efficient advancement of recent stages of development in this class of p38 MAP kinase inhibitors. In co…

biologyChemistryStereochemistryPyridinesp38 mitogen-activated protein kinasesEntropyImidazolesMolecular ConformationCombinatorial chemistryp38 Mitogen-Activated Protein KinasesMolecular conformationMolecular Docking Simulationchemistry.chemical_compoundStructure-Activity RelationshipPurinesMitogen-activated protein kinaseDrug DesignDrug Discoverybiology.proteinMolecular MedicineStructure–activity relationshipBioisostereBiological evaluationJournal of medicinal chemistry
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p38 MAPK: A dual role in hepatocyte proliferation through reactive oxygen species

2013

p38 MAPKs are important mediators of signal transduction that respond to a wide range of extracellular stressors such as UV radiation, osmotic shock, hypoxia, pro-inflammatory cytokines, and oxidative stress. The most abundant family member is p38α, which helps to couple cell proliferation and growth in response to certain damaging stimuli. In fact, increased proliferation and impaired differentiation are hallmarks of p38α-deficient cells. It has been reported that reactive oxygen species (ROS) play a critical role in cytokine-induced p38α activation. Under physiological conditions, p38α can function as a mediator of ROS signaling and either activate or suppress cell cycle progression depen…

chemistry.chemical_classificationMAPK/ERK pathwayReactive oxygen speciesMAP Kinase Signaling SystemCell growthp38 mitogen-activated protein kinasesCell Growth ProcessesGeneral MedicineCell cycleBiologymedicine.disease_causep38 Mitogen-Activated Protein KinasesBiochemistryLiver regenerationCell biologychemistryHepatocytesmedicineAnimalsHumansSignal transductionReactive Oxygen SpeciesOxidative stressFree Radical Research
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Integrin α2β1 Mediates Isoform-Specific Activation of p38 and Upregulation of Collagen Gene Transcription by a Mechanism Involving the α2 Cytoplasmic…

1999

Two collagen receptors, integrins alpha1beta1 and alpha2beta1, can regulate distinct functions in cells. Ligation of alpha1beta1, unlike alpha2beta1, has been shown to result in recruitment of Shc and activation of the Ras/ERK pathway. To identify the downstream signaling molecules activated by alpha2beta1 integrin, we have overexpressed wild-type alpha2, or chimeric alpha2 subunit with alpha1 integrin cytoplasmic domain in human osteosarcoma cells (Saos-2) lacking endogenous alpha2beta1. The chimeric alpha2/alpha1 chain formed a functional heterodimer with beta1. In contrast to alpha2/alpha1 chimera, forced expression of alpha2 integrin resulted in upregulation of alpha1 (I) collagen gene …

collagenIntegrinsReceptors CollagenTranscription GeneticintegrinIntegrincytoplasmic domainCDC42Biologyp38 MAPKTransfectionCD49cp38 Mitogen-Activated Protein KinasesCollagen receptorTumor Cells CulturedHumansProtein IsoformsCell BiologyMolecular biologyCell biologyUp-RegulationEnzyme ActivationIntegrin alpha Mbiology.proteinIntegrin beta 6Original ArticleSignal transductionMitogen-Activated Protein KinasesITGA6Signal TransductionThe Journal of Cell Biology
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The endopolygalacturonase 1 from botrytis cinerea activates grapevine defense reactions unrelated to its enzyumatic activity

2003

A purified glycoprotein from Botrytis cinerea(strain T4), identified as endopolygalacturonase 1 (T4BcPG1) by mass spectrometry analysis, has been shown to activate defense reactions in grapevine (Vitis vinifera cv. Gamay). These reactions include calcium influx, production of active oxygen species, activation of two mitogen-activated protein kinases, defense gene transcript accumulation, and phytoalexin production. Most of these defense reactions were also activated in grapevine in response to purified oligogalacturonides (OGA) with a degree of polymerization of 9 to 20. In vivo, these active OGA might be a part of the released products resulting from endopolygalacturonase activity on plan…

elicitor; endopolygalacturonase 1; Botrytis cinerea; plant defenceplant defencePhysiologyMolecular Sequence DataOligosaccharidesBiologyCell wallBotrytis cinereaGene Expression Regulation PlantSequence Homology Nucleic Acid[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyVitisAmino Acid SequencePectinaseendopolygalacturonase 1ComputingMilieux_MISCELLANEOUSBotrytis cinereachemistry.chemical_classificationelicitorBase SequenceSequence Homology Amino AcidKinasePhytoalexinfood and beveragesGeneral MedicineHydrogen Peroxidebiology.organism_classificationImmunity InnateElicitorEnzyme ActivationEnzymePolygalacturonasechemistryBiochemistryCalciumBotrytisMitogen-Activated Protein KinasesGlycoproteinAgronomy and Crop Science
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Resveratrol post-transcriptionally regulates pro-inflammatory gene expression via regulation of KSRP RNA binding activity

2014

Resveratrol shows beneficial effects in inflammation-based diseases like cancer, cardiovascular and chronic inflammatory diseases. Therefore, the molecular mechanisms of the anti-inflammatory resveratrol effects deserve more attention. In human epithelial DLD-1 and monocytic Mono Mac 6 cells resveratrol decreased the expression of iNOS, IL-8 and TNF-α by reducing mRNA stability without inhibition of the promoter activity. Shown by pharmacological and siRNA-mediated inhibition, the observed effects are SIRT1-independent. Target-fishing and drug responsive target stability experiments showed selective binding of resveratrol to the RNA-binding protein KSRP, a central post-transcriptional regul…

endocrine system diseasesMRNA destabilizationRNA Stabilityp38 mitogen-activated protein kinasesGene ExpressionRNA-binding proteinResveratrolBiologyp38 Mitogen-Activated Protein KinasesMicechemistry.chemical_compoundCell Line TumorStilbenesGene expressionGeneticsAnimalsHumansddc:610RNA Messengerskin and connective tissue diseasesMice KnockoutMessenger RNAGene knockdownExosome Multienzyme Ribonuclease Complexorganic chemicalsAnti-Inflammatory Agents Non-SteroidalGene regulation Chromatin and EpigeneticsRNA-Binding Proteinsfood and beveragesMolecular biology3. Good healthCell biologychemistryResveratrolMutationTrans-ActivatorsPhosphorylationInflammation Mediatorshormones hormone substitutes and hormone antagonistsNucleic Acids Research
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Mechanisms involved in lipid accumulation and apoptosis induced by 1-nitropyrene in Hepa1c1c7 cells

2011

International audience; 1-Nitropyrene (1-NP) is a nitro-polycyclic aromatic hydrocarbon (nitro-PAH) present in diesel exhaust and bound to particular matter in urban air. We show that 1-NP and the referent PAH benzo(a)pyrene (BP) induce apoptosis and a lipid accumulation dependent on cytochrome P450 1A1-metabolites in mouse hepatoma cells, whereas 1-amino-pyrene had no effect. The caspase inhibitor, N-benzyloxycarbonyl-Val-Ala-Asp(O-Me) fluoromethyl ketone (Z-VAD-fmk), inhibits 1-NP-induced apoptosis, but failed to alter 1-NP-triggered lipid accumulation determined by Nile red staining. We further show that cholesterol and fatty acid contents are modified after nitro-PAH exposure and that 1…

endoplasmic-reticulum stressMESH: PyrenesHepatoma cellsliver-cellsactivated protein-kinaseApoptosisAMP-Activated Protein KinasesToxicologyMESH: Liver Neoplasms ExperimentalMicechemistry.chemical_compoundMESH: CholesterolLiver Neoplasms ExperimentalMESH: AnimalsMESH: AMP-Activated Protein KinasesStearoyl-CoA desaturase 1CaspaseMESH: Lipid Metabolismchemistry.chemical_classificationhuman macrophages0303 health sciencesPyrenesbiology8-tetrachlorodibenzo-p-dioxin tcdd030302 biochemistry & molecular biologyGeneral Medicineinhibition[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM]CholesterolBiochemistry[SDV.TOX]Life Sciences [q-bio]/ToxicologyCaspaseslipids (amino acids peptides and proteins)stearoyl-coaStearoyl-CoA DesaturaseMESH: Cell Line Tumor[SDV.BC]Life Sciences [q-bio]/Cellular Biology03 medical and health sciencesMESH: Benzo(a)pyreneCell Line Tumor1-NitropyreneBenzo(a)pyreneAnimalsFatty acidsProtein kinase AMESH: Mice030304 developmental biologyaromatic-hydrocarbonsMESH: CaspasesCholesterolMESH: Apoptosisc-srcFatty acidAMPKCytochrome P450Lipid MetabolismMolecular biologychemistryApoptosisMESH: Stearoyl-CoA Desaturasebiology.proteinStearoyl-CoA desaturase-1desaturaseToxicology Letters
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