Search results for "AUTOPHOSPHORYLATION"

showing 10 items of 20 documents

Structural and Functional Characterization of Autophosphorylation in Bacterial Histidine Kinases

2019

Autophosphorylation of histidine kinases (HK) is the first step for signal transduction in bacterial two-component signalling systems. As HKs dimerize, the His residue is phosphorylated in cis or trans depending on whether the ATP molecule used in the reaction is bound to the same or the neighboring subunit, respectively. The cis or trans autophosphorylation results from an alternative directionality in the connection between helices α1 and α2 in the HK DHp domain, in such a way that α2 could be oriented almost 90° counterclockwise or clockwise with respect to α1. Sequence and length variability of this connection appears to lie behind the different directionality and is implicated in partn…

0303 health sciencesKinaseChemistryProtein subunitAutophosphorylation03 medical and health sciencesResponse regulator0302 clinical medicineBiophysicsPhosphorylationDirectionalitySignal transduction030217 neurology & neurosurgeryHistidine030304 developmental biology
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Vanillin cell sensor

2007

Our project for iGEM 2006 consisted of designing a cellular vanillin biosensor. We used an EnvZ -E. coli strain as a chassis, and constructed two different devices: a sensor and an actuator, assembled using OmpR-P as a standardised mediator. The sensor device contained a computation- ally designed vanillin receptor and a synthetic two-component signal transduction protein (Trz). The receptor protein was based on a ribose-binding protein as scaffold. The Trz was built by fusion of the periplasmic and transmembrane domains of a Trg protein with an EnvZ kinase domain. When the receptor complex binds Trg, an allosteric motion is propagated to the cyto- plasmic EnvZ kinase domain, resulting in a…

0303 health sciencesReceptor complex030303 biophysicsAllosteric regulationAutophosphorylationBioengineeringCell BiologyBiologyCell biology03 medical and health sciencesSynthetic biologyTransmembrane domainProtein kinase domainBiochemistry[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologySignal transductionMolecular BiologyTranscription factor030304 developmental biologyBiotechnologyIET Synthetic Biology
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The malate sensing two-component system MaeKR is a non-canonical class of sensory complex for C4-dicarboxylates

2017

16 páginas, 7 figuras, 2 tablas

0301 basic medicineModels MolecularAdenosine Triphosphate / metabolismProtein ConformationScienceMalatesBacterial proteins/chemistry/metabolism/geneticsPlasma protein bindingBiologyModels BiologicalArticleConserved sequence03 medical and health sciencesAdenosine TriphosphateBacterial ProteinsAdenosine Triphosphate / chemistryDicarboxylic AcidsProtein Interaction Domains and MotifsAmino Acid SequenceKinase activityPhosphorylationLactobacilus cassei/classification/physiologyMalates/metabolismPromoter Regions GeneticConserved SequencePhylogenyMultidisciplinaryQAutophosphorylationfungiRTwo-component regulatory systemResponse regulatorLacticaseibacillus casei030104 developmental biologyBiochemistryMedicineModelsbiologica/moleculPhosphorylationCconserved secuenceProtein MultimerizationBinding domainProtein BindingScientific Reports
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Cellular Concentrations of the Transporters DctA and DcuB and the Sensor DcuS of Escherichia coli and the Contributions of Free and Complexed DcuS to…

2017

ABSTRACT In Escherichia coli , the catabolism of C 4 -dicarboxylates is regulated by the DcuS-DcuR two-component system. The functional state of the sensor kinase DcuS is controlled by C 4 -dicarboxylates (like fumarate) and complexation with the C 4 -dicarboxylate transporters DctA and DcuB, respectively. Free DcuS (DcuS F ) is known to be constantly active even in the absence of fumarate, whereas the DcuB-DcuS and DctA-DcuS complexes require fumarate for activation. To elucidate the impact of the transporters on the functional state of DcuS and the concentrations of DcuS F and DcuB-DcuS (or DctA-DcuS), the absolute levels of DcuS, DcuB, and DctA were determined in aerobically or anaerobic…

0301 basic medicine030106 microbiologyBiologymedicine.disease_causeMicrobiologyDNA-binding proteinMass Spectrometry03 medical and health sciencesFumaratesTranscriptional regulationmedicineEscherichia coliDicarboxylic AcidsAnaerobiosisPhosphorylationMolecular BiologyTranscription factorEscherichia coliDicarboxylic Acid TransportersCatabolismKinaseEscherichia coli ProteinsAutophosphorylationGene Expression Regulation BacterialAerobiosisDNA-Binding Proteins030104 developmental biologyBiochemistryPhosphorylationProtein KinasesSignal TransductionTranscription FactorsResearch ArticleJournal of bacteriology
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LS104, a non-ATP-competitive small-molecule inhibitor of JAK2, is potently inducing apoptosis in JAK2V617F-positive cells

2008

Abstract The activating JAK2V617F mutation has been described in the majority of patients with BCR-ABL-negative myeloproliferative disorders (MPD). In this report, we characterize the small-molecule LS104 as a novel non-ATP-competitive JAK2 inhibitor: Treatment of JAK2V617F-positive cells with LS104 resulted in dose-dependent induction of apoptosis and inhibition of JAK2 autophosphorylation and of downstream targets. Activation of these targets by JAK2 was confirmed in experiments using small interfering RNA. LS104 inhibited JAK2 kinase activity in vitro. This effect was not reversible using elevated ATP concentrations, whereas variation of the kinase substrate peptide led to modulation of …

Cancer ResearchSmall interfering RNAApoptosisStyrenesMiceAdenosine TriphosphateCell Line Tumorhemic and lymphatic diseasesAnimalsHumansPhosphorylationKinase activityProtein Kinase InhibitorsMyeloproliferative DisordersJanus kinase 2AcrylonitrileDose-Response Relationship DrugbiologyKinaseAutophosphorylationJanus Kinase 2Molecular biologyIn vitroOncologyApoptosisbiology.proteinSignal transductionK562 CellsSignal TransductionMolecular Cancer Therapeutics
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Control of the bifunctional O 2 ‐sensor kinase NreB of Staphylococcus carnosus by the nitrate sensor NreA: Switching from kinase to phosphatase state

2019

The NreB-NreC two-component system of Staphylococcus carnosus for O2 sensing cooperates with the accessory nitrate sensor NreA in the NreA-NreB-NreC system for coordinated sensing and regulation of nitrate respiration by O2 and nitrate. ApoNreA (NreA in the absence of nitrate) interacts with NreB and inhibits NreB autophosphorylation (and activation). NreB contains the phosphatase motif DxxxQ. The present study shows that NreB on its own was inactive for the dephosphorylation of the phosphorylated response regulator NreC (NreC-P), but co-incubation with NreB and NreA stimulated NreC-P dephosphorylation. Either the presence of NreA · NO 3 - instead of apoNreA or mutation of the phosphatase m…

0303 health sciencesbiology030306 microbiologyKinasePhosphataseAutophosphorylationbiology.organism_classificationMicrobiologyCofactorDephosphorylation03 medical and health sciencesResponse regulatorBiochemistrybiology.proteinPhosphorylationMolecular Biology030304 developmental biologyStaphylococcus carnosusMolecular Microbiology
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Agonist-induced formation of FGFR1 homodimers and signaling differ among members of the FGF family

2011

Fibroblast growth factor receptor 1 (FGFR1) is known to be activated by homodimerization in the presence of both the FGF agonist ligand and heparan sulfate glycosaminoglycan. FGFR1 homodimers in turn trigger a variety of downstream signaling cascades via autophosphorylation of tyrosine residues in the cytoplasmic domain of FGFR1. By means of Bioluminescence Energy Resonance Transfer (BRET) as a sign of FGFR1 homodimerization, we evaluated in HEK293T cells the effects of all known FGF agonist ligands on homodimer formation. A significant correlation between BRET(2) signaling and ERK1/2 phosphorylation was observed, leading to a further characterization of the binding and signaling properties…

AgonistMAPK/ERK pathwaymedicine.drug_classBiophysicsSettore BIO/11 - Biologia MolecolareBiologyLigandsFibroblast growth factorSettore BIO/09 - FisiologiaBiochemistrychemistry.chemical_compoundFluorescence Resonance Energy TransfermedicineHumansReceptor Fibroblast Growth Factor Type 1Molecular BiologyMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Fibroblast growth factor receptor 1HEK 293 cellsAutophosphorylationCell BiologyHeparan sulfateFibroblast growth factors FGFR1 Homodimerization BRET MAPKCell biologyFibroblast Growth Factorsstomatognathic diseasesHEK293 CellschemistrySettore BIO/14 - FarmacologiaPhosphorylationHeparitin SulfateProtein MultimerizationBiochemical and Biophysical Research Communications
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The Nature of the Stimulus and of the Fumarate Binding Site of the Fumarate Sensor DcuS of Escherichia coli

2005

DcuS is a membrane-associated sensory histidine kinase of Escherichia coli specific for C(4) -dicarboxylates. The nature of the stimulus and its structural prerequisites were determined by measuring the induction of DcuS-dependent dcuB'-'lacZ gene expression. C(4)-dicarboxylates without or with substitutions at C2/C3 by hydrophilic (hydroxy, amino, or thiolate) groups stimulated gene expression in a similar way. When one carboxylate was replaced by sulfonate, methoxy, or nitro groups, only the latter (3-nitropropionate) was active. Thus, the ligand of DcuS has to carry two carboxylate or carboxylate/nitro groups 3.1-3.8 A apart from each other. The effector concentrations for half-maximal i…

Models MolecularMagnetic Resonance SpectroscopyHistidine KinaseRecombinant Fusion ProteinsMolecular Sequence Datamedicine.disease_causeBiochemistryCitric AcidStructure-Activity Relationshipchemistry.chemical_compoundFumaratesEscherichia colimedicineDicarboxylic AcidsAmino Acid SequenceCarboxylatePhosphorylationBinding siteKinase activityTartratesMolecular BiologyEscherichia coliPeptide sequenceDicarboxylic Acid TransportersBinding SitesChemistryEscherichia coli ProteinsAutophosphorylationHistidine kinaseGene Expression Regulation BacterialCell BiologyNitro CompoundsPeptide FragmentsEnzyme ActivationLac OperonBiochemistryMutagenesis Site-DirectedPropionatesProtein KinasesSequence AlignmentBinding domainJournal of Biological Chemistry
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Synthesis of polyfluoroalkyl sp2-iminosugar glycolipids and evaluation of their immunomodulatory properties towards anti-tumor, anti-leishmanial and …

2019

Immunomodulatory glycolipids, among which α-galactosylceramide (KRN7000) is an iconic example, have shown strong therapeutic potential in a variety of conditions ranging from cancer and infection to autoimmune or neurodegenerative diseases. A main difficulty for those channels is that they often provoke a cytokine storm comprising both pro- and anti-inflammatory mediators that antagonize each other and negatively affect the immune response. The synthesis of analogues with narrower cytokine secretion-inducing capabilities is hampered by the intrinsic difficulty at controlling the stereochemical outcome in glycosidation reactions, particularly if targeting the α-anomer, which seriously hamper…

Allosteric regulationIminosugar01 natural sciencesImmunomodulation03 medical and health sciencesGlycolipidGlycomimeticDrug DiscoverymedicineLeishmaniasisp38α MAPKCancer030304 developmental biologyInflammationPharmacology0303 health sciences010405 organic chemistryChemistryOrganic ChemistryAutophosphorylationBiological activityGeneral Medicinemedicine.disease0104 chemical sciencessp2-Iminosugar glycolipidsBiochemistryMechanism of actionPolyfluoroalkyl compoundsmedicine.symptomCytokine stormEuropean Journal of Medicinal Chemistry
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AML-associated Flt3 kinase domain mutations show signal transduction differences compared with Flt3 ITD mutations

2005

Activating mutations of Flt3 are found in approximately one third of patients with acute myeloid leukemia (AML) and are an attractive drug target. Two classes of Flt3 mutations occur: internal tandem duplications (ITDs) in the juxtamembrane and point mutations in the tyrosine kinase domain (TKD). We and others have shown that Flt3-ITD induced aberrant signaling including strong activation of signal transducer and activator of transcription 5 (STAT5) and repression of CCAAT/estradiol-binding protein α (c/EBPα) and Pu.1. Here, we compared the signaling properties of Flt3-ITD versus Flt3-TKD in myeloid progenitor cells. We demonstrate that Flt3-TKD mutations induced autonomous growth of 32D ce…

ImmunologyApoptosisBiologymedicine.disease_causeBiochemistryCell Linefluids and secretionsProto-Oncogene Proteinshemic and lymphatic diseasesSTAT5 Transcription FactormedicineAnimalsHumansPoint MutationMyeloid CellsPhosphorylationProtein kinase BProtein kinase CMutationPoint mutationAutophosphorylationIntracellular Signaling Peptides and ProteinsReceptor Protein-Tyrosine Kinaseshemic and immune systemsCell BiologyHematologyMilk ProteinsStaurosporineMolecular biologyProtein Structure TertiaryDNA-Binding ProteinsMuridaefms-Like Tyrosine Kinase 3Leukemia MyeloidTandem Repeat SequencesAcute Diseaseembryonic structuresFms-Like Tyrosine Kinase 3Mutagenesis Site-DirectedTrans-ActivatorsSignal transductionTyrosine kinaseSignal TransductionTranscription FactorsBlood
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