Search results for "Phosphorylation"

showing 10 items of 975 documents

PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163

1996

AbstractThe 80kDa Myristolated Alanine-Rich C-Kinase Substrate (MARCKS) in a major in vivo substrate of protein kinase C (PKC). Here we report that MARCKS is a major substrate for the lipid-activated PKC-related kinase (PRK1) in cell extracts. Furthermore, PRK1 is shown to phosphorylate MARCKS on the same sites as PKC in vitro. Thus, control of MARCKS phosphorylation on these previously identified ‘PKC’ sites may be regulated under certain circumstances by PRK as well as PKC mediated signalling pathways. The implications for MARCKS as a marker of PKC activation and as a point of signal convergence are discussed.

PhosphopeptidesMARCKSPRKRecombinant Fusion ProteinsMolecular Sequence DataBiophysicsKidneyBiochemistryCell-free systemCell LineSerineStructural BiologyProtein kinase CGeneticsAnimalsAmino Acid SequenceBinding siteMARCKSPKCPhosphorylationMyristoylated Alanine-Rich C Kinase SubstrateMolecular BiologyProtein kinase CGlutathione TransferaseBinding SitesCell-Free SystemKinaseChemistryIntracellular Signaling Peptides and ProteinsMembrane ProteinsProteinsCell BiologyHaplorhiniPeptide FragmentsBiochemistryPhosphorylationElectrophoresis Polyacrylamide GelSignal transductionSequence AnalysisSignal TransductionFEBS Letters
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Correlations in palmitoylation and multiple phosphorylation of rat bradykinin B2 receptor in Chinese hamster ovary cells.

1999

Rat bradykinin B2 receptor from unstimulated Chinese hamster ovary cells transfected with the corresponding cDNA has been isolated, and subsequent mass spectrometric analysis of multiple phosphorylated species and of the palmitoylation attachment site is described. Bradykinin B2 receptor was isolated on oligo(dT)-cellulose using N-(epsilon-maleimidocaproyloxy)succinimide-Met-Lys-bradykinin coupled to a protected (dA)30-mer. This allowed a one-step isolation of the receptor on an oligo(dT)-cellulose column via variation solely of salt concentration. After enzymatic in-gel digestion, matrix-assisted laser desorption ionization and electrospray ion trap mass spectrometric analysis of the isola…

PhosphopeptidesReceptor Bradykinin B2AcylationMolecular Sequence DataPalmitatesCHO CellsTransfectionBiochemistryMass SpectrometryCell membranePhosphoserinePalmitoylationCricetinaemedicineAnimalsTrypsinAmino Acid SequenceBradykinin receptorPhosphorylationReceptorPhosphotyrosineMolecular BiologyChemistryChinese hamster ovary cellReceptors BradykininCell BiologyTransfectionPeptide FragmentsRatsmedicine.anatomical_structurePhosphothreonineBiochemistryPhosphorylationSignal transductionProtein Processing Post-TranslationalThe Journal of biological chemistry
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Functional characterization of the plastidial 3-phosphoglycerate dehydrogenase family in Arabidopsis.

2013

This work contributes to unraveling the role of the phosphorylated pathway of serine (Ser) biosynthesis in Arabidopsis (Arabidopsis thaliana) by functionally characterizing genes coding for the first enzyme of this pathway, 3-phosphoglycerate dehydrogenase (PGDH). We identified two Arabidopsis plastid-localized PGDH genes (3-PGDH and EMBRYO SAC DEVELOPMENT ARREST9 [EDA9]) with a high percentage of amino acid identity with a previously identified PGDH. All three genes displayed a different expression pattern indicating that they are not functionally redundant. pgdh and 3-pgdh mutants presented no drastic visual phenotypes, but eda9 displayed delayed embryo development, leading to aborted emb…

PhysiologyMutantMolecular Sequence DataArabidopsisPlant SciencePlant RootsGene Expression Regulation EnzymologicSerineBiochemistry and MetabolismGene Expression Regulation PlantComplementary DNAArabidopsisGeneticsSerineArabidopsis thalianaMetabolomicsAmino Acid SequencePlastidsPhosphorylationGenePhosphoglycerate DehydrogenasePhylogenyTapetumMicroscopy ConfocalbiologySequence Homology Amino AcidArabidopsis ProteinsReverse Transcriptase Polymerase Chain ReactionGenetic Complementation Testfood and beveragesPlant Components Aerialbiology.organism_classificationPlants Genetically ModifiedPhenotypeIsoenzymesBiochemistryMultigene FamilyMutationSeedsPollenPlant physiology
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Early signaling network in tobacco cells elicited with methyl jasmonate and cyclodextrins.

2012

We analyze, for the first time, the early signal transduction pathways triggered by methyl jasmonate (MJ) and cyclodextrins (CDs) in tobacco (Nicotiana tabacum) cell cultures, paying particular attention to changes in cytosolic free Ca(2+) concentration ([Ca(2+)](cyt)), the production of hydrogen peroxide (H(2)O(2)) and nitric oxide (NO), and late events like the induction of capsidiol. Our data indicate that MJ and CDs trigger a [Ca(2+)](cyt) rise promoted by Ca(2+) influx through Ca(2+)-permeable channels. The joint presence of MJ and CDs provokes a first increase in [Ca(2+)](cyt) similar to that observed in MJ-treated cells, followed by a second peak similar to that found in the presence…

PhysiologyNicotiana tabacum[SDV]Life Sciences [q-bio]nicotiana tabacumPlant ScienceCyclopentanesAcetatesNitric OxideCapsidiolchemistry.chemical_compoundCytosolOnium CompoundsPlant CellsTobaccoGeneticsProtein phosphorylationOxylipinsPhosphorylationCells CulturedRespiratory BurstCyclodextrinsMethyl jasmonatebiologyMolecular StructureHydrogen Peroxidemethyl jasmonatebiology.organism_classificationcell culturesRespiratory burstCulture MediaCytosolEGTABiochemistrychemistry[SDE]Environmental SciencesBiophysicsPhosphorylationCalciumSesquiterpenesSignal TransductionPlant physiology and biochemistry : PPB
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6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase from frog skeletal muscle: purification, kinetics and immunological properties.

1993

Fructose 2,6-bisphosphate is the most potent activator of 6-phosphofructo-1-kinase, a key regulatory enzyme of glycolysis in animal tissues. This study was prompted by the finding that the content of fructose 2,6-bisphosphate in frog skeletal muscle was dramatically increased at the initiation of exercise and was closely correlated with the glycolytic flux during exercise. 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, the enzyme system catalyzing the synthesis and degradation of fructose 2,6-bisphosphate, was purified from frog (Rana esculenta) skeletal muscle and its properties were compared with those of the rat muscle type enzyme expressed in Escherichia coli using recombinant DN…

PhysiologyPhosphofructokinase-2BiologyBiochemistrychemistry.chemical_compoundEndocrinologymedicineFructosediphosphatesAnimalsGlycolysisPhosphorylationEcology Evolution Behavior and Systematicschemistry.chemical_classificationMolecular massImmunochemistryMusclesPhosphotransferasesSkeletal muscleRana esculentaFructoseHydrogen-Ion ConcentrationMolecular WeightKineticsmedicine.anatomical_structureEnzymechemistryFructose 26-bisphosphateBiochemistryGRENOUILLEAnimal Science and ZoologyPhosphoenolpyruvate carboxykinaseProtein KinasesJournal of comparative physiology. B, Biochemical, systemic, and environmental physiology
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Molecular characterization and evolution of the protein phosphatase 2A B' regulatory subunit family in plants.

2002

Abstract Type 2A serine/threonine protein phosphatases (PP2A) are important components in the reversible protein phosphorylation events in plants and other organisms. PP2A proteins are oligomeric complexes constituted by a catalytic subunit and several regulatory subunits that modulate the activity of these phosphatases. The analysis of the complete genome of Arabidopsis allowed us to characterize four novel genes, AtB′ε, AtB′ζ,AtB′η, and AtB′θ, belonging to the PP2A B′ regulatory subunit family. Because four genes of this type had been described previously, this family is composed of eight members. Reverse transcriptase-polymerase chain reaction experiments showed thatAtB′ε mRNAs are prese…

PhysiologyProtein subunitMolecular Sequence DataArabidopsisPlant ScienceGene Expression Regulation EnzymologicEvolution MolecularGene Expression Regulation PlantArabidopsisGeneticsPhosphoprotein PhosphatasesArabidopsis thalianaProtein phosphorylationAmino Acid SequenceProtein Phosphatase 2GenePeptide sequencePhylogenyGenomic organizationGeneticsExpressed Sequence TagsbiologySequence Homology Amino AcidOryzaProtein phosphatase 2Plantsbiology.organism_classificationIsoenzymesBiochemistryMultigene FamilyResearch ArticlePlant physiology
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Cold exposure enhances fat utilization but not non-esterified fatty acids, glycerol or catecholamines availability during submaximal walking and runn…

2013

Cold exposure modulates the use of carbohydrates and fat during exercise. This phenomenon has mostly been observed in controlled cycling studies, but not during walking and running when core temperature and oxygen consumption are controlled, as both may alter energy metabolism. This study aimed at examining energy substrate availability and utilization during walking and running in the cold when core temperature and oxygen consumption are maintained. Ten lightly clothed male subjects walked or ran for 60-min, at 50% and 70% of maximal oxygen consumption, respectively, in a climatic chamber set at 0°C or 22°C. Thermal, cardiovascular, and oxidative responses were measured every 15-…

Physiologykylmäaltistuscold exposurerasvahapotchemistry.chemical_elementBlood lipidsOxidative phosphorylationglycerol030204 cardiovascular system & hematologyBiologyOxygenthermal responseslcsh:Physiologyrasva-aineenvaihdunta03 medical and health scienceschemistry.chemical_compound0302 clinical medicineAnimal sciencePhysiology (medical)fatHeart rateGlycerolglyseroliOriginal Research Articleta315Exerciselcsh:QP1-981kuormauskuormitusfat metabolismVO2 max030229 sport sciencesRespiratory quotientGlucosechemistryBiochemistrykatakolamiinitEnergy sourceEnergy Metabolismkatekoliamiinit
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Activation of MAPK homologues by elicitors in tobacco cells

1998

International audience; Elicitors of plant defence reactions (such as cryptogein, an elicitin produced by Phytophthora cryptogea, or oligogalacturonides (OGs)), induced in tobacco cell suspensions (Nicotiana tabacum var Xanthi) a rapid and transient activation of two protein kinases (PKs) with apparent molecular masses of 50 and 46 kDa, respectively. These PKs activated and phosphorylated at tyrosine residues, phosphorylated myelin basic protein (MBP) at serine/threonine residues. Both are recognized by anti-MAPK antibodies. The two MBP kinases possessed the same kinetics of activation, and their activation depended, to the same extent, on different exogenously applied compounds (staurospor…

Plant ExtractsAlgal ProteinsStaurosporineEnzyme ActivationFungal Proteins[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants geneticsGlycogen Synthase Kinase 3Plants ToxicCULTURE DE CELLULE[SDV.GEN.GPL] Life Sciences [q-bio]/Genetics/Plants geneticsCalcium-Calmodulin-Dependent Protein KinasesTobaccoTyrosine[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyCalciumEnzyme InhibitorsPhosphorylationReactive Oxygen Species
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A critical role of plastidial glycolytic Glyceraldehyde-3-Phosphate Dehydrogenase in the control of plant metabolism and development

2009

3 páginas.

PlastidArabidopsisDehydrogenasePlant ScienceSerine biosynthesisGenes PlantPlant RootsGene Expression Regulation EnzymologicSerinechemistry.chemical_compoundBiosynthesisGene Expression Regulation PlantSerineGlycolysisRNA MessengerPlastidsAmino AcidsPhosphorylationPhylogenyGlyceraldehyde 3-phosphate dehydrogenasebiologyArabidopsis ProteinsGAPDHGenetic Complementation TestGlyceraldehyde-3-Phosphate DehydrogenasesMetabolismLipid MetabolismArticle AddendumPlant LeavesProtein TransportCytosolMetabolic pathwayPhenotypeBiochemistrychemistryMutationbiology.proteinCarbohydrate MetabolismGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)GlycolysisResearch Article
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Presence of phosphorylatedO-ribosyl-adenosine In T-ψ-stem of yeast methlonine initiator tRNA

1989

We report in this paper on isolation and characterization of two unknown nucleosides G* and [A*] located in the T-psi-stem of yeast methionine initiator tRNA, using the combined means of HPLC protocols, real time UV-absorption spectrum, and post-run mass spectrometry by electron impact or fast atom bombardment. The G* nucleoside in position 65 was identified as unmodified guanosine. The structure of the unknown [A*] in position 64 was characterized as an isomeric form of O-ribosyl-adenosine by comparison of its chromatographic, UV-spectral and mass spectrometric properties with those of authentic O-alpha-ribofuranosyl-(1"----2')-adenosine isolated from biosynthetic poly(adenosine diphosphat…

Poly Adenosine Diphosphate RiboseAdenosineRNA Transfer MetIon chromatographySaccharomyces cerevisiaeGuanosineSaccharomyces cerevisiaeBiologyChromatography DEAE-CelluloseGas Chromatography-Mass Spectrometrychemistry.chemical_compoundMethionineGeneticsmedicinePhosphorylationChromatography High Pressure LiquidGuanosineAdenosine diphosphate riboseNucleosidesRNA Transfer Amino Acid-SpecificFast atom bombardmentbiology.organism_classificationAdenosineYeastchemistryBiochemistryNucleic Acid ConformationNucleosidemedicine.drugNucleic Acids Research
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