Search results for "GTPASE"

showing 10 items of 83 documents

NMR structure of a non-conjugatable, ADP-ribosylation associated, ubiquitin-like domain from Tetrahymena thermophila polyubiquitin locus.

2019

Abstract Background Ubiquitin-like domains (UbLs), in addition to being post-translationally conjugated to the target through the E1-E2-E3 enzymatic cascade, can be translated as a part of the protein they ought to regulate. As integral UbLs coexist with the rest of the protein, their structural properties can differ from canonical ubiquitin, depending on the protein context and how they interact with it. In this work, we investigate T.th-ubl5, a UbL present in a polyubiquitin locus of Tetrahymena thermophila, which is integral to an ADP-ribosyl transferase protein. Only one other co-occurrence of these two domains within the same protein has been reported. Methods NMR, multiple sequence al…

UBL DOMAINspektroskopiaGTPasePARKINBiochemistryPROTEIN BACKBONEACTIVATIONprotein-protein interaction0302 clinical medicineProtein-protein interactionUbiquitinmolekyylidynamiikkaNMR-spektroskopiaPolyubiquitinADP Ribose Transferases0303 health sciencesMultiple sequence alignmentbiologyFERM domainChemistryTetrahymenastructure-function relationshipFAMILYCell biologyRECEPTORSPost-translational modificationSignal TransductionBiophysicsSequence alignmentMolecular Dynamics SimulationUbiquitin-like domainsMECHANISMSProtein–protein interactionTetrahymena thermophila03 medical and health sciencesNMR spectroscopyADP-RibosylationubikitiinitMolecular BiologyNuclear Magnetic Resonance Biomolecular030304 developmental biologyMolecular dynamics simulationsStructure-function relationshipmolecular dynamics simulationsbiology.organism_classificationProtein Structure Tertiarypost-translational modificationProteasomeMOLECULAR-DYNAMICSbiology.protein1182 Biochemistry cell and molecular biologyproteiinitGTPASEProtein Processing Post-Translational030217 neurology & neurosurgeryFERM DOMAINBiochimica et biophysica acta. General subjects
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RPGR ORF15 isoform co-localizes with RPGRIP1 at centrioles and basal bodies and interacts with nucleophosmin

2005

The ORF15 isoform of RPGR (RPGR(ORF15)) and RPGR interacting protein 1 (RPGRIP1) are mutated in a variety of retinal dystrophies but their functions are poorly understood. Here, we show that in cultured mammalian cells both RPGR(ORF15) and RPGRIP1 localize to centrioles. These localizations are resistant to the microtubule destabilizing drug nocodazole and persist throughout the cell cycle. RPGR and RPGRIP1 also co-localize at basal bodies in cells with primary cilia. The C-terminal (C2) domain of RPGR(ORF15) (ORF15(C2)) is highly conserved across 13 mammalian species, suggesting that it is a functionally important domain. Using matrix-assisted laser desorption ionization time-of-flight mas…

CentrioleFluorescent Antibody TechniqueMicechemistry.chemical_compoundChlorocebus aethiopsGuanine Nucleotide Exchange FactorsProtein IsoformsBasal bodyConserved SequenceGenetics (clinical)CentriolesGlutathione Transferaseintegumentary systemNuclear ProteinsExonsGeneral MedicineRetinitis pigmentosa GTPase regulatorImmunohistochemistryNocodazoleCOS CellsNucleophosminCell NucleolusRecombinant Fusion ProteinsMolecular Sequence DataBiologyOpen Reading FramesMicrotubuleTwo-Hybrid System TechniquesGeneticsAnimalsHumansAmino Acid SequenceEye ProteinsMolecular BiologyNucleophosminSequence Homology Amino AcidProteinsPrecipitin TestsMolecular biologyeye diseasesProtein Structure TertiaryMice Inbred C57BLCytoskeletal ProteinschemistryCentrosomeCytoplasmSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationMutationCattleHeLa CellsHuman Molecular Genetics
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Absence of mutation at the GAP-related domain of the neurofibromatosis type 1 gene in sporadic neurofibrosarcomas and other bone and soft tissue sarc…

1995

The NF1 gene encodes neurofibromin, a GTPase-activating protein containing a GAP-related domain (NF1-GRD) that is capable of downregulating ras by stimulating ras intrinsic GTPase activity. We tested 44 sarcomas, nine of which corresponded to sporadic neurofibrosarcomas, for mutations at the NF1-GRD by the polymerase chain reaction-single strand conformation polymorphism (PCR-SSCP) technique, finding no mutation in every sample tested. We suggest that inactivation of the NF1-GRD by gene mutation seems not to be an important event in the tumorigenesis of sarcomas.

congenital hereditary and neonatal diseases and abnormalitiesCancer ResearchNeurofibromatosis 1DNA Mutational AnalysisBone NeoplasmsSoft Tissue NeoplasmsGTPaseBiologyGene mutationmedicine.disease_causePolymerase Chain ReactionGeneticsmedicineHumansneoplasmsMolecular BiologyGenePolymorphism Single-Stranded ConformationalGeneticsMutationNeurofibromin 1ProteinsSarcomaSingle-strand conformation polymorphismmedicine.diseaseNeurofibromin 1eye diseasesnervous system diseasesNeurofibrosarcomaCancer researchbiology.proteinSarcomaCarcinogenesisCancer Genetics and Cytogenetics
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Lysosomal Signaling Licenses Embryonic Stem Cell Differentiation via Inactivation of Tfe3

2019

International audience; Self-renewal and differentiation of pluripotent murine embryonic stem cells (ESCs) is regulated by extrinsic signaling pathways. It is less clear whether cellular metabolism instructs developmental progression. In an unbiased genome-wide CRISPR/Cas9 screen, we identified components of a conserved amino-acid-sensing pathway as critical drivers of ESC differentiation. Functional analysis revealed that lysosome activity, the Ragulator protein complex, and the tumor-suppressor protein Folliculin enable the Rag GTPases C and D to bind and seclude the bHLH transcription factor Tfe3 in the cytoplasm. In contrast, ectopic nuclear Tfe3 represses specific developmental and met…

MaleTranscription GeneticGTPaseGTP PhosphohydrolasesPATHWAYMice0302 clinical medicineNeural Stem CellsCRISPRTUMOR-SUPPRESSORCell Self RenewalPhosphorylationSPECIFICATIONdevelopmental disorder0303 health sciencesGenomeBasic Helix-Loop-Helix Leucine Zipper Transcription FactorsCell DifferentiationMouse Embryonic Stem CellsFlcndifferentiationCell biologymedicine.anatomical_structuremTORMolecular MedicineFemaleSignal transductionProtein BindingSignal TransductionRECRUITMENTBiology03 medical and health sciencesRag GTPasesLysosomeGeneticsmedicineAnimalsHumansPoint MutationNAIVE PLURIPOTENCYAMINO-ACID LEVELSTranscription factorAllelesPI3K/AKT/mTOR pathway030304 developmental biologyCOMPLEXFOLLICULINRagulatorCell Biologypluripotencyembryonic stem cellEmbryonic stem cellTfe3[SDV.GEN.GH]Life Sciences [q-bio]/Genetics/Human geneticsCytoplasmLysosomes030217 neurology & neurosurgeryCell Stem Cell
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Ras, Rap, and Rac Small GTP-binding Proteins Are Targets for Clostridium sordellii Lethal Toxin Glucosylation

1996

Lethal toxin (LT) from Clostridium sordellii is one of the high molecular mass clostridial cytotoxins. On cultured cells, it causes a rounding of cell bodies and a disruption of actin stress fibers. We demonstrate that LT is a glucosyltransferase that uses UDP-Glc as a cofactor to covalently modify 21-kDa proteins both in vitro and in vivo. LT glucosylates Ras, Rap, and Rac. In Ras, threonine at position 35 was identified as the target amino acid glucosylated by LT. Other related members of the Ras GTPase superfamily, including RhoA, Cdc42, and Rab6, were not modified by LT. Incubation of serum-starved Swiss 3T3 cells with LT prevents the epidermal growth factor-induced phosphorylation of m…

ThreonineUridine Diphosphate GlucoseRHOABacterial ToxinsMolecular Sequence DataClostridium sordelliimacromolecular substancesCDC42GTPaseBiologyCell morphologyBiochemistryGTP PhosphohydrolasesProto-Oncogene Proteins p21(ras)MiceGTP-binding protein regulatorsGTP-Binding ProteinsAnimalsHumansAmino Acid SequenceMolecular BiologyClostridiumEpidermal Growth FactorKinase3T3 CellsCell Biologybiology.organism_classificationMolecular biologyActinsrac GTP-Binding ProteinsActin CytoskeletonKineticsGlucoserap GTP-Binding ProteinsGlucosyltransferasesCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinPhosphorylationGuanosine TriphosphateHeLa CellsJournal of Biological Chemistry
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Rab33B Controls Hepatitis B Virus Assembly by Regulating Core Membrane Association and Nucleocapsid Processing

2017

Many viruses take advantage of cellular trafficking machineries to assemble and release new infectious particles. Using RNA interference (RNAi), we demonstrate that the Golgi/autophagosome-associated Rab33B is required for hepatitis B virus (HBV) propagation in hepatoma cell lines. While Rab33B is dispensable for the secretion of HBV subviral envelope particles, its knockdown reduced the virus yield to 20% and inhibited nucleocapsid (NC) formation and/or NC trafficking. The overexpression of a GDP-restricted Rab33B mutant phenocopied the effect of deficit Rab33B, indicating that Rab33B-specific effector proteins may be involved. Moreover, we found that HBV replication enhanced Rab33B expres…

0301 basic medicineHepatitis B virusBiologymedicine.disease_causeVirusArticleCell LineCell membraneRab33B03 medical and health sciencesnucleocapsid assemblyTranscription (biology)RNA interferenceVirologymedicineHumansSecretionNucleocapsidcore/capsid membrane associationHepatitis B virus030102 biochemistry & molecular biologyEffectorVirus AssemblyCell MembraneVirologyHepatitis B Core Antigenshepatitis B virus; Rab GTPase; Rab33B; core/capsid membrane association; nucleocapsid assembly; virus traffickingTransport proteinProtein Transport030104 developmental biologyInfectious Diseasesmedicine.anatomical_structurevirus traffickingrab GTP-Binding ProteinsHost-Pathogen InteractionsHepatocytesRab GTPaseViruses; Volume 9; Issue 6; Pages: 157
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Competitive binding of Rab21 and p120RasGAP to integrins regulates receptor traffic and migration

2011

P120RasGAP competes with Rab21 for binding to the cytoplasmic domain of integrin α-subunits, thereby promoting receptor escape from early endosomes and recycling to the plasma membrane.

CytoplasmIntegrinsEndosomeEndocytic cycleIntegrinVesicular Transport ProteinsEndosomesCD49cBinding CompetitiveModels BiologicalArticleCollagen receptor03 medical and health sciencesMice0302 clinical medicineSDG 3 - Good Health and Well-beingCell MovementCell Line TumorAnimalsHumansResearch Articles030304 developmental biology0303 health sciencesbiologyCell Membranep120 GTPase Activating ProteinCell BiologyCell biologyProtein Structure TertiaryIntegrin alpha Mrab GTP-Binding Proteins030220 oncology & carcinogenesisbiology.protein/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_beingIntegrin beta 6RabProtein Binding
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Identification and characterization of a gene encoding a putative mouse Rho GTPase activating protein gene 8, Arhgap8.

2003

Rho GTPase activating proteins promote the intrinsic GTP hydrolysis activity of Rho family proteins. We isolated a putative mouse ortholog of the human Rho GTPase activating protein 8, ARHGAP8. The open reading frame encodes a peptide of 387 amino acids with high homology to human ARHGAP8 in its N-terminal domain. Both radiation hybrid mapping and fluorescent in situ hybridization localized the gene to mouse chromosome 15E. The 23 kb genomic Arhgap8 sequence consists of eight exons and seven introns. Northern blot and RT-PCR analyses showed that a transcript of approximately 1.9 kb is ubiquitously expressed in various adult mouse tissues with particularly strong expression in kidney.

MaleARHGAP8DNA ComplementaryGTPase-activating proteinMolecular Sequence DataGene ExpressionGTPaseBiologyExonMiceGene expressionGeneticsAnimalsAmino Acid SequenceRNA MessengerCloning MolecularGenePeptide sequenceIn Situ Hybridization FluorescenceRadiation Hybrid MappingBase SequenceSequence Homology Amino AcidGTPase-Activating ProteinsChromosome MappingGeneral MedicineExonsSequence Analysis DNABlotting NorthernMolecular biologyIntronsOpen reading frameGenesSequence AlignmentGene
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Control of cellular phosphatidylinositol 4,5-bisphosphate levels by adhesion signals and Rho GTPases in NIH 3T3 fibroblasts

2000

The involvement of small GTPases of the Rho family in the control of phosphoinositide metabolism by adhesion signals was examined in NIH 3T3 fibroblasts. Abrogation of adhesion signals by detachment of cells from their substratum resulted in a time-dependent decrease in the cellular level of PtdIns(4,5)P2 by approximately 50%. This effect could be mimicked by treatment of adherent cells with Clostridium difficile toxin B and toxin B-1470, which inhibit specific subsets of Rho and Ras GTPases. Detachment of cells that had been pretreated with the clostridial toxins did not cause a further reduction in PtdIns(4,5)P2 levels, suggesting that the target GTPases are integrated into the control of…

Phosphatidylinositol 45-Diphosphaterac1 GTP-Binding Proteinrho GTP-Binding ProteinsBacterial ToxinsCellClostridium difficile toxin BRAC1GTPasePhospholipaseBiologyTransfectionBiochemistryMicechemistry.chemical_compoundPhosphoinositide Phospholipase CBacterial ProteinsCell AdhesionmedicineAnimalsPhosphorylationInositol phosphatechemistry.chemical_classificationPhospholipase CCytotoxinsPhosphoric Diester Hydrolases3T3 CellsMolecular biologyRecombinant ProteinsCell biologyKineticsPhosphotransferases (Alcohol Group Acceptor)medicine.anatomical_structurechemistryPhosphatidylinositol 45-bisphosphateType C PhospholipasesCalciumSignal TransductionEuropean Journal of Biochemistry
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Neuronal Cytoskeleton in Intellectual Disability: From Systems Biology and Modeling to Therapeutic Opportunities

2021

Intellectual disability (ID) is a pathological condition characterized by limited intellectual functioning and adaptive behaviors. It affects 1–3% of the worldwide population, and no pharmacological therapies are currently available. More than 1000 genes have been found mutated in ID patients pointing out that, despite the common phenotype, the genetic bases are highly heterogeneous and apparently unrelated. Bibliomic analysis reveals that ID genes converge onto a few biological modules, including cytoskeleton dynamics, whose regulation depends on Rho GTPases transduction. Genetic variants exert their effects at different levels in a hierarchical arrangement, starting from the molecular lev…

0301 basic medicineactin cytoskeletonReview0302 clinical medicineBorderline intellectual functioningIntellectual disabilityDisabilità Intellettiva GTPasi CitoscheletroBiology (General)CytoskeletonSpectroscopyNeuronseducation.field_of_studysystems biologyCognitionGeneral MedicinePhenotypeComputer Science ApplicationsChemistryPhenotypeintellectual disabilitySignal TransductionBoolean modelingQH301-705.5NeurogenesisIn silicoSystems biologyPopulationBiologyCatalysismicrotubulesInorganic Chemistry03 medical and health sciencesmedicineAnimalsHumansPhysical and Theoretical ChemistryeducationQD1-999Molecular BiologyGTPase signalingsmall Rho GTPasesOrganic Chemistrypharmacological modulationprotein:protein interaction networkActin cytoskeletonmedicine.disease030104 developmental biologySynapsesneuronal networksNeuroscience030217 neurology & neurosurgery
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