Search results for "MESH: Phosphorylation"

showing 4 items of 4 documents

Phosphorylation of serine residues is fundamental for the calcium-binding ability of Orchestin, a soluble matrix protein from crustacean calcium stor…

2003

International audience; Orchestia cavimana is a terrestrial crustacean, which cyclically stores calcium in diverticula of the midgut, in the form of calcified amorphous concretions. These concretions are associated with a proteinaceous matrix, the main constituent of the soluble matrix is Orchestin, an acidic calcium-binding protein [Testenière et al., Biochem. J. 361 (2002) 327-335]. In the present paper, we clearly demonstrate that Orchestin is phosphorylated on serine and tyrosine residues, but that calcium binding only occurs via the phosphoserine residues. To our knowledge, this is the first example of an invertebrate mineralization for which a post-translational modification is clearl…

BiomineralizationMESH: Amino Acid SequenceMESH: Calcium-Binding ProteinsMatrix (biology)01 natural sciencesBiochemistryCalcium in biologyMESH: TyrosineSerinechemistry.chemical_compoundMESH: Structure-Activity RelationshipStructural BiologyCrustaceaSerineElectrophoresis Gel Two-DimensionalMESH: AnimalsTyrosinePhosphorylation0303 health sciencesBiochemistryMESH: CalciumPhosphorylationElectrophoresis Polyacrylamide GelOrganic matrixProtein BindingMolecular Sequence DataBiophysicschemistry.chemical_elementCrustaceanCalciumBiology010402 general chemistryMESH: Calcification Physiologic03 medical and health sciencesStructure-Activity RelationshipCalcification PhysiologicMESH: CrustaceaGeneticsAnimalsMESH: Protein Binding[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyAmino Acid SequenceMESH: SerineMolecular Biology030304 developmental biologyCalcium metabolismMESH: Molecular Sequence DataMESH: PhosphorylationCalcium-Binding ProteinsCell BiologyMESH: Electrophoresis Gel Two-Dimensional0104 chemical scienceschemistryPhosphoserineMESH: Protein Processing Post-TranslationalTyrosineCalciumCalcium bindingProtein Processing Post-TranslationalMESH: Electrophoresis Polyacrylamide Gel
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A phosphorylation cycle shapes gradients of the DYRK family kinase Pom1 at the plasma membrane.

2011

http://linkinghub.elsevier.com/; International audience; Concentration gradients regulate many cell biological and developmental processes. In rod-shaped fission yeast cells, polar cortical gradients of the DYRK family kinase Pom1 couple cell length with mitotic commitment by inhibiting a mitotic inducer positioned at midcell. However, how Pom1 gradients are established is unknown. Here, we show that Tea4, which is normally deposited at cell tips by microtubules, is both necessary and, upon ectopic cortical localization, sufficient to recruit Pom1 to the cell cortex. Pom1 then moves laterally at the plasma membrane, which it binds through a basic region exhibiting direct lipid interaction. …

MESH : Molecular Sequence Data[SDV]Life Sciences [q-bio]CellMESH: Cell CycleMESH: Amino Acid SequenceAmino Acid Sequence; Cell Cycle; Cell Membrane/metabolism; Microtubule-Associated Proteins/metabolism; Molecular Sequence Data; Phosphorylation; Protein Kinases/chemistry; Protein Kinases/metabolism; Schizosaccharomyces/cytology; Schizosaccharomyces/metabolism; Schizosaccharomyces pombe Proteins/metabolism; Sequence AlignmentMESH : Phosphorylation0302 clinical medicinePhosphorylation0303 health sciencesKinaseMESH : Amino Acid SequenceMESH : Sequence AlignmentCell CycleCortical gradientMESH : Schizosaccharomyces pombe ProteinsFission yeastCell biologymedicine.anatomical_structureMESH: SchizosaccharomycesPom1PhosphorylationMicrotubule-Associated ProteinsMESH : Cell MembraneMolecular Sequence DataMESH: Sequence AlignmentMESH : Protein KinasesBiologyGeneral Biochemistry Genetics and Molecular BiologyPom1Dephosphorylation03 medical and health sciencesMicrotubuleMESH : Cell CycleSchizosaccharomycesCell cortexmedicineAmino Acid SequenceMitosisMESH: Protein Kinases030304 developmental biologyMESH: Molecular Sequence Data[ SDV ] Life Sciences [q-bio]Phosphorylation cycleMESH: PhosphorylationBiochemistry Genetics and Molecular Biology(all)Cell MembraneMESH: Schizosaccharomyces pombe ProteinsMESH: Microtubule-Associated ProteinsMESH : SchizosaccharomycesMESH : Microtubule-Associated ProteinsSchizosaccharomyces pombe ProteinsDYRK family kinaseProtein KinasesSequence Alignment030217 neurology & neurosurgeryMESH: Cell Membrane
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Use of CDC2 from etoposide-treated cells as substrate to assay CDC25 phosphatase activity

1999

International audience; Cyclin-dependent kinases (CDKs) regulate the key transition of the cell cycle in all organisms. In response to Etoposide (VP-16) induced DNA damage, cells undergo a G2-phase arrest resulting in the accumulation of inactive CDK1 (CDC2) kinase complexes. Here we report that upon Etoposide treatment CDC2 is phosphorylated on tyrosine 15 and is dephosphorylated and activated in vitro by recombinant CDC25 phosphatase. We also show that inactive CDC2 kinase from Etoposide-treated cells can be used as a substrate in a sensitive two-step assay of CDC25 phosphatase. This assay, which is very simple to set-up, is based on the monitoring of CDC2 kinase activity after CDC25-depe…

MESH: HumansMESH: Phosphorylation[SDV]Life Sciences [q-bio]Cell Cycle Proteins[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]MESH: CDC2 Protein KinaseMESH: Tyrosine[SDV] Life Sciences [q-bio]AGENT ANTITUMORALenzymes and coenzymes (carbohydrates)MESH: Cell Cycle ProteinsMESH: cdc25 PhosphatasesCDC2 Protein KinaseMESH: HeLa CellsMESH: Phosphoprotein PhosphatasesPhosphoprotein PhosphatasesHumansTyrosinecdc25 PhosphatasesPhosphorylationbiological phenomena cell phenomena and immunityEtoposideHeLa CellsMESH: Etoposide
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Wee1 inhibition potentiates Wip1-dependent p53-negative tumor cell death during chemotherapy

2016

AbstractInactivation of p53 found in more than half of human cancers is often associated with increased tumor resistance to anti-cancer therapy. We have previously shown that overexpression of the phosphatase Wip1 in p53-negative tumors sensitizes them to chemotherapeutic agents, while protecting normal tissues from the side effects of anti-cancer treatment. In this study, we decided to search for kinases that prevent Wip1-mediated sensitization of cancer cells, thereby interfering with efficacy of genotoxic anti-cancer drugs. To this end, we performed a flow cytometry-based screening in order to identify kinases that regulated the levels of γH2AX, which were used as readout. Another criter…

Wip1ApoptosisCell Cycle ProteinsPharmacologyMESH: G2 Phase Cell Cycle CheckpointsHistonesMESH : PhosphorylationMiceMESH : Cell Cycle ProteinsMESH: AnimalsMESH: Tumor Suppressor Protein p53MESH: HistonesKinaseTp53 mutationsMESH : Mice Transgenic3. Good healthProtein Phosphatase 2CSurvival RateMESH : Antineoplastic AgentsH2ax phosphorylationP53 activationMESH: Protein Phosphatase 2CRNA InterferenceMESH : Colorectal NeoplasmsMESH : Carrier ProteinsHistone H2axMESH: MitochondriaImmunologyHuman fibroblastsMESH: Carrier ProteinsAntineoplastic AgentsMESH: Protein-Tyrosine KinasesMESH: Protein-Serine-Threonine KinasesMESH : Cisplatin03 medical and health sciencesMESH: Cell Cycle ProteinsGenotoxic stressMESH : Protein-Tyrosine KinasesHumansMESH : HistonesAnticancer TherapyMESH: DNA DamageCisplatinMESH: HumansMESH: Phosphorylation[ SDV.BC ] Life Sciences [q-bio]/Cellular BiologyMESH : HumansMESH : Nuclear Proteins030104 developmental biologyCancer cellMESH: Antineoplastic AgentsCisplatinCarrier ProteinsMESH: Nuclear ProteinsMESH : ApoptosisDna-damage response0301 basic medicineCancer ResearchMESH: Caspase 3MESH : Caspase 3PhosphorylationCytotoxicityMESH : DNA DamageSensitizationmedicine.diagnostic_testCaspase 3Nuclear ProteinsProtein-Tyrosine KinasesMESH : Survival RateMitochondriaG2 Phase Cell Cycle CheckpointsWee1medicine.anatomical_structureMESH : Protein Phosphatase 2COriginal ArticleMESH : MitochondriaColorectal Neoplasmsmedicine.drugMESH : Protein-Serine-Threonine KinasesMESH: Cell Line TumorMESH: Survival RateMESH: Mice TransgenicMESH: RNA InterferencePhosphataseMice Transgenic[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyProtein Serine-Threonine KinasesFlow cytometryCellular and Molecular NeuroscienceCell Line TumorMESH : MicemedicineAnimalsMESH: MiceMESH : Cell Line TumorMESH: ApoptosisCell BiologyMESH : Tumor Suppressor Protein p53MESH: CisplatinCancer researchbiology.proteinMESH : AnimalsMESH : G2 Phase Cell Cycle CheckpointsMESH : RNA InterferenceTumor Suppressor Protein p53MESH: Colorectal NeoplasmsDNA DamageCell Death & Disease
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