Search results for "tyrosine phosphatases"

showing 10 items of 22 documents

Endocytosis of the glutamate transporter 1 is regulated by laforin and malin: Implications in Lafora disease.

2020

Postprint 36 páginas, 7 figuras

0301 basic medicineArrestinsAmino Acid Transport System X-AGPhosphataseProgressive myoclonus epilepsyBiologyEndocytosisLafora diseaseArticle03 medical and health sciencesCellular and Molecular NeuroscienceMice0302 clinical medicineUbiquitinmedicineAnimalsNedd4.2Lafora diseaseGlutamate receptorUbiquitinationTransportermedicine.diseaseProtein Tyrosine Phosphatases Non-ReceptorEndocytosisCell biologyGLT-1030104 developmental biologyNeurologyLafora Diseasebiology.proteinGlutamateLaforin030217 neurology & neurosurgeryGlia
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Assessing the biological activity of the glucan phosphatase laforin

2016

Glucan phosphatases are a recently discovered family of enzymes that dephosphorylate either starch or glycogen and are essential for proper starch metabolism in plants and glycogen metabolism in humans. Mutations in the gene encoding the only human glucan phosphatase, laforin, result in the fatal, neurodegenerative, epilepsy known as Lafora disease. Here, we describe phosphatase assays to assess both generic laforin phosphatase activity and laforin's unique glycogen phosphatase activity.

0301 basic medicinePhosphataseLafora diseaseArticleSubstrate SpecificityNitrophenols03 medical and health scienceschemistry.chemical_compound0302 clinical medicineOrganophosphorus CompoundsDual-specificity phosphatasemedicineHumansGlucanEnzyme Assayschemistry.chemical_classificationGlycogenbiologyfood and beveragesBiological activitymedicine.diseaseFluoresceinsProtein Tyrosine Phosphatases Non-Receptor030104 developmental biologyEnzymechemistryBiochemistryLafora Diseasebiology.proteinLaforin030217 neurology & neurosurgeryGlycogen
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Fungicide resistance towards fludioxonil conferred by overexpression of the phosphatase gene Mo PTP 2 in Magnaporthe oryzae

2018

The fungicide fludioxonil causes hyperactivation of the Hog1p MAPK within the high-osmolarity glycerol signaling pathway essential for osmoregulation in pathogenic fungi. The molecular regulation of MoHog1p phosphorylation is not completely understood in pathogenic fungi. Thus, we identified and characterized the putative MoHog1p-interacting phosphatase gene MoPTP2 in the filamentous rice pathogen Magnaporthe oryzae. We found overexpression of MoPTP2 conferred fludioxonil resistance in M. oryzae, whereas the 'loss of function' mutant ΔMoptp2 was more susceptible toward the fungicide. Additionally, quantitative phosphoproteome profiling of MoHog1p phosphorylation revealed lower phosphorylati…

0301 basic medicineProteomeMutantPhosphataseGene ExpressionDioxolesBiologyFludioxonilMicrobiologyMicrobiologyFungal Proteins03 medical and health sciencesDrug Resistance FungalGene expressionPyrrolesPhosphorylationMolecular BiologyGenePlant DiseasesOryzaPhosphoproteinsFungicides IndustrialFungicideMagnaporthe030104 developmental biologyPhosphorylationMitogen-Activated Protein KinasesProtein Tyrosine PhosphatasesSignal transductionProtein Processing Post-TranslationalGene DeletionMolecular Microbiology
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Islet autoantibodies in Latvian subjects with non-insulin-dependent diabetes mellitus: slow-onset type 1 diabetes or polyendocrine autoimmunity?

2006

In Latvia diabetes mellitus is diagnosed using the WHO's clinical criteria; assays for the detection of autoantibodies are not available, and hence slowly progressive autoimmune diabetes is likely to be missed. Autoantibodies against glutamic acid decarboxylase (GAD65) and protein tyrosine phosphatase (IA-2) among patients with clinically diagnosed NIDDM identify group of patients with slow-onset type 1 diabetes or LADA. The aim of this study was to estimate the risk of polyendocrine autoimmunity among clinically diagnosed NIDDM patients from Latvia. One hundred NIDDM patients and 100 healthy controls were tested for GAD65 and IA-2 autoantibodies as well as 21-hydroxylase (21-OH) and tissue…

AdultMalemedicine.medical_specialtyendocrine system diseasesAdolescentTissue transglutaminasemedicine.medical_treatmentOverweightmedicine.disease_causeAutoantigensGeneral Biochemistry Genetics and Molecular BiologyAutoimmunityDiagnosis DifferentialHistory and Philosophy of ScienceInternal medicineDiabetes mellitusmedicineHumansReceptor-Like Protein Tyrosine Phosphatases Class 8ChildPolyendocrinopathies AutoimmuneAutoantibodiesProtein Tyrosine Phosphatase Non-Receptor Type 1Type 1 diabetesbiologybusiness.industryGlutamate DecarboxylaseGeneral NeuroscienceInsulinAutoantibodynutritional and metabolic diseasesMembrane Proteinsmedicine.diseaseLatviaIsoenzymesEndocrinologyDiabetes Mellitus Type 1Child Preschoolbiology.proteinFemalemedicine.symptomProtein Tyrosine PhosphatasesbusinessBody mass indexBiomarkersAnnals of the New York Academy of Sciences
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Parthenolide induces superoxide anion production by stimulating EGF receptor in MDA-MB-231 breast cancer cells

2013

The sesquiterpene lactone parthenolide (PN) has recently attracted considerable attention because of its anti-microbial, anti-inflammatory and anticancer effects. However, the mechanism of its cytotoxic action on tumor cells remains scarcely defined. We recently provided evidence that the effect exerted by PN in MDA-MB-231 breast cancer cells was mediated by the production of reactive oxygen species (ROS). The present study shows that PN promoted the phosphorylation of EGF receptor (phospho-EGFR) at Tyr1173, an event which was observed already at 1  h of incubation with 25  µM PN and reached a peak at 8-16  h. This effect seemed to be a consequence of ROS production, because N-acetylcystein…

Cancer Researchparthenolide epidermal growth factor receptor NADPH oxidase breast cancer cellsBreast NeoplasmsAntioxidantschemistry.chemical_compoundSuperoxidesCell Line TumorSettore BIO/10 - BiochimicaHumansParthenolideEnzyme InhibitorsPhosphorylationchemistry.chemical_classificationReactive oxygen speciesNADPH oxidasebiologySuperoxideKinaseAnti-Inflammatory Agents Non-SteroidalNF-kappa BAcetophenonesNADPH OxidasesTyrphostinsMolecular biologyAcetylcysteineErbB ReceptorsOncologychemistryApoptosisApocyninQuinazolinesbiology.proteinPhosphorylationFemaleProtein Tyrosine PhosphatasesSesquiterpenesInternational Journal of Oncology
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Interaction of Mitogen-activated Protein Kinases with the Kinase Interaction Motif of the Tyrosine Phosphatase PTP-SL Provides Substrate Specificity …

1999

ERK1 and ERK2 associate with the tyrosine phosphatase PTP-SL through a kinase interaction motif (KIM) located in the juxtamembrane region of PTP-SL. A glutathione S-transferase (GST)-PTP-SL fusion protein containing the KIM associated with ERK1 and ERK2 as well as with p38/HOG, but not with the related JNK1 kinase or with protein kinase A or C. Accordingly, ERK2 showed in vitro substrate specificity to phosphorylate GST-PTP-SL in comparison with GST-c-Jun. Furthermore, tyrosine dephosphorylation of ERK2 by the PTP-SLDeltaKIM mutant was impaired. The in vitro association of ERK1/2 with GST-PTP-SL was highly stable; however, low concentrations of nucleotides partially dissociated the ERK1/2.P…

Cytoplasmanimal structuresProtein Kinase C-alphaRecombinant Fusion ProteinsCèl·lulesNerve Tissue ProteinsProtein tyrosine phosphataseMitogen-activated protein kinase kinaseTransfectionenvironment and public healthBiochemistrySH3 domainReceptor tyrosine kinaseMAP2K7Substrate SpecificitySerineAnimalsc-RafAmino Acid SequenceMolecular BiologyProtein Kinase CSequence DeletionMitogen-Activated Protein Kinase 1Binding SitesMitogen-Activated Protein Kinase 3biologyCyclin-dependent kinase 2Intracellular Signaling Peptides and ProteinsJNK Mitogen-Activated Protein KinasesCell BiologyCyclic AMP-Dependent Protein KinasesIsoenzymesenzymes and coenzymes (carbohydrates)KineticsBiochemistryAmino Acid SubstitutionCOS CellsCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinMutagenesis Site-DirectedCyclin-dependent kinase 9CattleMitogen-Activated Protein KinasesProtein Tyrosine PhosphatasesProteïnes
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A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase

1999

Protein tyrosine phosphatase PTP-SL retains mitogen-activated protein (MAP) kinases in the cytoplasm in an inactive form by association through a kinase interaction motif (KIM) and tyrosine dephosphorylation. The related tyrosine phosphatases PTP-SL and STEP were phosphorylated by the cAMP-dependent protein kinase A (PKA). The PKA phosphorylation site on PTP-SL was identified as the Ser231 residue, located within the KIM. Upon phosphorylation of Ser231, PTP-SL binding and tyrosine dephosphorylation of the MAP kinases extracellular signal–regulated kinase (ERK)1/2 and p38α were impaired. Furthermore, treatment of COS-7 cells with PKA activators, or overexpression of the Cα catalytic subunit …

Cytoplasmanimal structuresRecombinant Fusion ProteinsCèl·lulesAmino Acid MotifsNerve Tissue ProteinsProtein tyrosine phosphataseSH2 domainTransfectionenvironment and public healthModels Biologicalp38 Mitogen-Activated Protein KinasesReceptor tyrosine kinaseSH3 domainCell LinePhosphoserinetyrosine phosphatasesAnimalsHumansProtein phosphorylationPKAReceptor-Like Protein Tyrosine Phosphatases Class 7PhosphorylationPTP-SLCell NucleusMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3biologyBrief ReportIntracellular Signaling Peptides and ProteinsBiological TransportCell BiologyProtein Tyrosine Phosphatases Non-ReceptorCyclic AMP-Dependent Protein KinasesEnzyme Activationenzymes and coenzymes (carbohydrates)MAP kinasesBiochemistryMitogen-activated protein kinaseCOS CellsMutationbiology.proteinPhosphorylationMitogen-Activated Protein KinasesProtein Tyrosine PhosphatasesEnzimssignal transductionProto-oncogene tyrosine-protein kinase Src
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Identification of Two Mannoproteins Released from Cell Walls of a Saccharomyces cerevisiae mnn1 mnn9 Double Mutant by Reducing Agents

1999

The cell wall of Saccharomyces cerevisiae represents some 30% of the total weight of the cell and is made up of β-glucans, mannose-containing glycoproteins (mannoproteins), and small amounts of chitin (9, 15). The mannoproteins can be divided into three groups according to the linkages that bind them to the structure of the cell wall: (i) noncovalently bound, (ii) covalently bound to the structural glucan, and (iii) disulfide bound to other proteins that are themselves covalently bound to the structural glucan of the cell wall (8). Our work has focused on the disulfide-bound mannoproteins, probably the least well known of the three groups mentioned above. Previous work (25) showed that trea…

GlycosylationSaccharomyces cerevisiae ProteinsGlycosylationBlotting WesternMolecular Sequence DataSaccharomyces cerevisiaeSaccharomyces cerevisiaeMicrobiologyGene Expression Regulation EnzymologicFungal ProteinsCell wallOpen Reading FramesSurface-Active Agentschemistry.chemical_compoundCell WallGene Expression Regulation FungalEndopeptidasesAspartic Acid EndopeptidasesAmino Acid SequenceSubtilisinsFluorescent Antibody Technique IndirectMolecular BiologyMercaptoethanolGlucanGel electrophoresischemistry.chemical_classificationFungal proteinMembrane GlycoproteinsbiologySodium Dodecyl SulfateBiological Transportbiology.organism_classificationRecombinant ProteinsYeastMolecular Weightcarbohydrates (lipids)Cytoskeletal ProteinsEukaryotic CellsPhenotypechemistryBiochemistryMutagenesisReducing AgentsElectrophoresis Polyacrylamide GelProprotein ConvertasesProtein Tyrosine PhosphatasesGlycoproteinGene DeletionJournal of Bacteriology
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HACD1, a regulator of membrane composition and fluidity, promotes myoblast fusion and skeletal muscle growth

2015

International audience; The reduced diameter of skeletal myofibres is a hallmark of several congenital myopathies, yet the underlying cellular and molecular mechanisms remain elusive. In this study, we investigate the role of HACD1/PTPLA, which is involved in the elongation of the very long chain fatty acids, in muscle fibre formation. In humans and dogs, HACD1 deficiency leads to a congenital myopathy with fibre size disproportion associated with a generalized muscle weakness. Through analysis of HACD1-deficient Labradors, Hacd1-knockout mice, and Hacd1-deficient myoblasts, we provide evidence that HACD1 promotes myoblast fusion during muscle development and regeneration. We further demons…

Male[SPI.GPROC] Engineering Sciences [physics]/Chemical and Process EngineeringCellular differentiationGeneralized muscle weaknessBiologyMuscle Developmentcentronuclear myopathyCell LineMyoblasts03 medical and health scienceschemistry.chemical_compoundMyoblast fusionMice0302 clinical medicineDogsVLCFA[SDV.IDA]Life Sciences [q-bio]/Food engineeringGeneticsmedicineMyocyteAnimalsHumans[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringMUFACentronuclear myopathyMuscle SkeletalMolecular Biology030304 developmental biologyMice Knockout0303 health sciencesPTPLACell MembraneSkeletal muscleCell DifferentiationCell BiologyGeneral MedicineArticles[SDV.IDA] Life Sciences [q-bio]/Food engineeringmedicine.diseaseCongenital myopathyLysophosphatidylcholinemedicine.anatomical_structureLPCchemistryBiochemistryFemaleProtein Tyrosine Phosphatasescentronuclear myopathy;lpc;mufa;ptpla;vlcfa030217 neurology & neurosurgery
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UNC-52/perlecan affects gonadal leader cell migrations in C. elegans hermaphrodites through alterations in growth factor signaling.

2003

0012-1606 doi: DOI: 10.1016/S0012-1606(03)00014-9; The unc-52 gene of Claenorhabditis elegans encodes a homologue of the basement membrane heparan sulfate proteoglycan perlecan. Viable alleles reduce the abundance of UNC-52 in late larval stages and increase the frequency of distal tip cell (DTC) migration defects caused by mutations disrupting the UNC-6/netrin guidance system. These unc-52 alleles do not cause circumferential DTC migration defects in an otherwise wild-type genetic background. The effects of unc-52 mutations on DTC migrations are distinct from effects on myofilament organization and can be partially suppressed by mutations in several genes encoding growth factor-like molecu…

Malemedicine.medical_treatmentOrganogenesisCellDisorders of Sex DevelopmentReceptor-Like Protein Tyrosine PhosphatasesFibroblast growth factorAnimals Genetically ModifiedCell MovementNetrinGrowth SubstancesGenes HelminthGeneticsMusclesCell migrationsWnt signaling pathwayHelminth Proteinsmedicine.anatomical_structurePhenotypeLarvaC. elegansFemaleNetrinsProteoglycansSignal transductionSignal TransductionUNC-52Nerve Tissue ProteinsReceptors Cell SurfacePerlecanmacromolecular substancesBiologymedicineAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsGonadsGeneMolecular BiologyGrowth factorfungiMembrane ProteinsCell BiologyPerlecanReceptors Fibroblast Growth Factornervous systemMutationbiology.proteinProtein Tyrosine PhosphatasesDevelopmental BiologyDevelopmental biology
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