Search results for "MESH: Tyrosine"

showing 2 items of 2 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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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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