Search results for "gtp-binding"

showing 10 items of 178 documents

rhoB encoding a UV-inducible Ras-related small GTP-binding protein is regulated by GTPases of the Rho family and independent of JNK, ERK, and p38 MAP…

1998

The small GTPase RhoB is immediate-early inducible by DNA damaging treatments and thus part of the early response of eukaryotic cells to genotoxic stress. To investigate the regulation of this cellular response, we isolated the gene for rhoB from a mouse genomic library. Sequence analysis of the rhoB gene showed that its coding region does not contain introns. The promoter region of rhoB harbors regulatory elements such as TATA, CAAT, and Sp1 boxes but not consensus sequences for AP-1, Elk-1, or c-Jun/ATF-2. The rhoB promoter was activated by UV irradiation, but not by 12-O-tetradecanoylphorbol-13-acetate treatment. rhoB promoter deletion constructs revealed a fragment of 0.17 kilobases in …

Ultraviolet RaysRHOBMolecular Sequence DataMAP Kinase Kinase Kinase 1BiologyProtein Serine-Threonine KinasesBiochemistryp38 Mitogen-Activated Protein KinasesGTP PhosphohydrolasesWortmanninchemistry.chemical_compoundMiceGTP-Binding ProteinsRhoB GTP-Binding ProteinAnimalsCloning MolecularEnzyme InhibitorsPromoter Regions GeneticrhoB GTP-Binding ProteinMolecular BiologyPhosphoinositide-3 Kinase InhibitorsMAP kinase kinase kinaseBase SequenceKinaseMEK inhibitorJNK Mitogen-Activated Protein KinasesMembrane ProteinsCell BiologyMolecular biologychemistryMitogen-activated protein kinaseCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinras ProteinsSignal transductionMitogen-Activated Protein KinasesThe Journal of biological chemistry
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UDP-glucose deficiency in a mutant cell line protects against glucosyltransferase toxins from Clostridium difficile and Clostridium sordellii.

1996

Abstract We have previously isolated a fibroblast mutant cell with high resistance to the two Rho-modifying glucosyltransferase toxins A and B of Clostridium difficile. We demonstrate here a low level of UDP-glucose in the mutant, which explains its toxin resistance since: (i) to obtain a detectable toxin B-mediated Rho modification in lysates of mutant cells, addition of UDP-glucose was required, and it promoted the Rho modification dose-dependently; (ii) high pressure liquid chromatography analysis of nucleotide extracts of cells indicated that the level of UDP-glucose in the mutant (0.8 nmol/106 cells) was lower than in the wild type (3.7 nmol/106 cells); and (iii) sensitivity to toxin B…

Uridine Diphosphate GlucoseMicroinjectionsMutantBacterial ToxinsClostridium difficile toxin AClostridium sordelliiClostridium difficile toxin Bmedicine.disease_causeBiochemistryMicrobiologyCell LineCricetulusBacterial ProteinsGTP-Binding ProteinsCricetinaemedicineAnimalsMolecular BiologyClostridiumbiologyToxinClostridioides difficileWild typeCell BiologyClostridium difficilebiology.organism_classificationGlucosyltransferasesMutationbiology.proteinGlucosyltransferaseThe Journal of biological chemistry
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Mosaic activating mutations in GNA11 and GNAQ are associated with phakomatosis pigmentovascularis and extensive dermal melanocytosis

2016

Common birthmarks can be an indicator of underlying genetic disease but are often overlooked. Mongolian blue spots (dermal melanocytosis) are usually localized and transient, but they can be extensive, permanent, and associated with extracutaneous abnormalities. Co-occurrence with vascular birthmarks defines a subtype of phakomatosis pigmentovascularis, a group of syndromes associated with neurovascular, ophthalmological, overgrowth, and malignant complications. Here, we discover that extensive dermal melanocytosis and phakomatosis pigmentovascularis are associated with activating mutations in GNA11 and GNAQ, genes that encode Gα subunits of heterotrimeric G proteins. The mutations were det…

WT wild typeDNA Mutational AnalysisMolecular Sequence Datapostzygotic mutationsMutation MissenseSWS Sturge-Weber syndromeDermatologycesioflammeagermlineBiochemistrySkin DiseasesAnimals Genetically Modifiedg-proteinDNA deoxyribonucleic acidMongolian Spotoculodermal melanocytosis[ SDV.MHEP ] Life Sciences [q-bio]/Human health and pathologyGeneticsAnimalsHumansddc:610Phosphorylationchoroidal melanomaMolecular BiologyAllelesZebrafishdiseaseBase SequenceNeurocutaneous Syndromessturge-weberInfantCell Biologymongolian spotPPV phakomatosis pigmentovascularisGTP-Binding Protein alpha SubunitsHEK293 CellsPhenotypeMutationGTP-Binding Protein alpha Subunits Gq-G11Original Articleuveal melanoma[SDV.MHEP]Life Sciences [q-bio]/Human health and pathologySignal Transduction
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Focus on the Small GTPase Rab1: A Key Player in the Pathogenesis of Parkinson’s Disease

2021

Parkinson’s disease (PD) is the second most frequent neurodegenerative disease. It is characterized by the loss of dopaminergic neurons in the substantia nigra and the formation of large aggregates in the survival neurons called Lewy bodies, which mainly contain α-synuclein (α-syn). The cause of cell death is not known but could be due to mitochondrial dysfunction, protein homeostasis failure, and alterations in the secretory/endolysosomal/autophagic pathways. Survival nigral neurons overexpress the small GTPase Rab1. This protein is considered a housekeeping Rab that is necessary to support the secretory pathway, the maintenance of the Golgi complex structure, and the regulation of macroau…

autophagyParkinson's diseaseQH301-705.5Substantia nigraReviewBiologyCatalysisInorganic Chemistryα-synucleinmedicineAnimalsHumansSmall GTPaseBiology (General)Physical and Theoretical ChemistryQD1-999Molecular BiologySpectroscopySecretory pathwayRab1GTPasesOrganic ChemistryNeurodegenerationDopaminergicRAB1Parkinson DiseaseLRRK2General Medicinemedicine.diseaseLRRK2Computer Science Applicationssecretory pathwayrab1 GTP-Binding ProteinsChemistrynervous systemParkinson’s diseaseNeuroscienceGolgi fragmentationInternational Journal of Molecular Sciences
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The binding of G-protein to rod outer segment phospholipids at the nitrogen–water interface

1989

In the visual process, one photoexcited rhodopsin (R*) catalyzes the activation of hundreds of G-proteins. It remains to be determined whether G-protein and R* find one another by membrane surface diffusion of these components (diffusion model) or by diffusion of G-protein through the aqueous phase (hopping model). A monolayer of each main rod outer segment (ROS) phospholipid interacting with a subphase containing G-protein, has been used to simulate the interaction of G-protein with the cytoplasmic surface of discal membranes. The possible diffusion of G-protein through the aqueous phase was then measured by observing its adsorption–desorption in the monolayer of each main ROS phospholipi…

biologyChemistryAqueous two-phase systemPhospholipidMembrane ProteinsCell BiologySurface pressureBiochemistryCrystallographychemistry.chemical_compoundMembraneGTP-Binding ProteinsCytoplasmRhodopsinMonolayerbiology.proteinAnimalsCattlePhotoreceptor CellsDiffusion (business)Molecular BiologyPhospholipidsBiochemistry and Cell Biology
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Impact of amino acids 22-27 of Rho-subfamily GTPases on glucosylation by the large clostridial cytotoxins TcsL-1522, TcdB-1470 and TcdB-8864

1999

Here we report data describing some principles of the interaction between small GTP-binding proteins and large Clostridial cytotoxins (LCTs). Our investigation was based on the differential glucosylation of Rac1 versus RhoA by LCTs TcsL-1522, TcdB-1470 and TcdB-8864. Chimeric RhoA/Rac1 proteins and GTPases mutated at defined regions or single amino acids were used as substrates. Starting with chimeric Rac/Rho proteins we demonstrated that proteins containing the N-terminal 73 amino acids of Rac1 (but not those of RhoA) were efficiently glucosylated. Within this stretch, three regions differ significantly in Rac1 and RhoA. Regions containing amino acids 41-45 and 50-54 had no effect on toxin…

chemistry.chemical_classificationRHOAGlycosylationbiologyRAC1GTPaseBiochemistryAmino acidchemistry.chemical_compoundBiochemistrychemistryCdc42 GTP-Binding Proteinbiology.proteinBinding sitePeptide sequenceEuropean Journal of Biochemistry
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Stimulation with carbachol alters endomembrane distribution and plasma membrane expression of intracellular proteins in lacrimal acinar cells.

2000

The events that lead to Sjogren's autoimmune processes in the lacrimal gland remain poorly understood. The acinar cell's responses to acute cholinergic stimulation include release of secretory products across the apical plasma membrane (apm) and a number of processes related to traffic between endomembrane compartments and the basal-lateral plasma membranes (blm), such as recruitment of Na, K-ATPase, accelerated recycling, and accelerated transcytosis of secretory IgA. We tested the hypothesis that stimulation-induced acceleration of endomembrane traffic is accompanied by changes in compartmentation and increased blm expression of proteins that are normally sequestered in endomembrane compa…

medicine.medical_specialtyAcid PhosphataseImmunoblottingGolgi ApparatusStimulationBiologyCholinergic AgonistsCathepsin BCathepsin BCellular and Molecular Neurosciencesymbols.namesakeInternal medicinemedicineAcinar cellAnimalsEndomembrane systemCells Culturedrab5 GTP-Binding ProteinsDifferential centrifugationEnzyme PrecursorsCell MembraneHistocompatibility Antigens Class IIMembrane Proteinsalpha-GlucosidasesGolgi apparatusGalactosyltransferasesCathepsinsSensory SystemsStimulation Chemicalbeta-N-AcetylhexosaminidasesCell biologyOphthalmologyEndocrinologySjogren's SyndromeTranscytosisrab GTP-Binding ProteinssymbolsCarbacholElectrophoresis Polyacrylamide GelFemaleRabbitsSodium-Potassium-Exchanging ATPaseIntracellularExperimental eye research
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Adrenergic modulation of astroglial phospholipase D activity and cell proliferation.

1999

As phospholipase D (PLD) activation has been associated with mitogenic signalling in several cell types, we tested an association between adrenergic activation of PLD and cellular proliferation in primary cultures of rat cortical astrocytes. In 2-week old cultures, PLD activation by noradrenaline (EC50: 0.49 microM) was inhibited by prazosin, a specific antagonist at alpha1-adrenergic receptors (IC50: 0.23 microM). Adrenergic PLD activation was not affected by genistein, an inhibitor of tyrosine kinases, or by Ro 31-8220, an inhibitor of protein kinase C (PKC), but was dose-dependently depressed in the presence of brefeldin A (1-100 microg/ml), an inhibitor of ARF activation. In experiments…

medicine.medical_specialtyAdrenergic AntagonistsAdrenergicBiologyPharmacologychemistry.chemical_compoundNorepinephrineGTP-Binding ProteinsIsoprenalineInternal medicinemedicineAdrenergic antagonistPrazosinPhospholipase DPhospholipase D activityAnimalsMolecular BiologyProtein kinase CCells CulturedBrefeldin APhospholipase DGeneral NeurosciencePrazosinBrefeldin AAdrenergic AgonistsPropranololRatsReceptors AdrenergicEndocrinologychemistryAlcoholsAstrocyteslipids (amino acids peptides and proteins)Neurology (clinical)Cell DivisionDevelopmental Biologymedicine.drugSignal TransductionBrain research
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Can you blame cold feet on Epac (and Rap1A)? Focus on “Cyclic AMP-Rap1A signaling activates RhoA to induce α2C-adrenoceptor translocation to the cell…

2012

Intracellular signaling by the second messenger cyclic AMP (cAMP) activates the Ras-related small GTPase Rap1 through the guanine exchange factor Epac. This activation leads to effector protein interactions, activation, and biological responses in the vasculature, including vasorelaxation. In vascular smooth muscle cells derived from human dermal arterioles (microVSM), Rap1 selectively regulates expression of G protein-coupled α2C-adrenoceptors (α2C-ARs) through JNK-c-jun nuclear signaling. The α2C-ARs are generally retained in the trans-Golgi compartment and mobilize to the cell surface and elicit vasoconstriction in response to cellular stress. The present study used human microVSM to exa…

medicine.medical_specialtyRHOAPhysiologyMyocytes Smooth MuscleCellChromosomal translocationSmooth muscleReceptors Adrenergic alpha-2Internal medicineCyclic AMPmedicineAnimalsHumansReceptorbiologyrap1 GTP-Binding ProteinsArticlesCell Biologyα2c adrenoceptorCell biologyProtein Transportmedicine.anatomical_structureEndocrinologybiology.proteinmedicine.symptomrhoA GTP-Binding ProteinVasoconstrictionAmerican Journal of Physiology-Cell Physiology
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Regulation of the human bradykinin B2 receptor expressed in sf21 insect cells: A possible role for tyrosine kinases

2000

The functional regulation of the human bradykinin B2 receptor expressed in sf21 cells was studied. Human bradykinin B2 receptors were immunodetected as a band of 75–80 kDa in membranes from recombinant baculovirus-infected cells and visualized at the plasma membrane, by confocal microscopy, using an antibody against an epitope from its second extracellular loop. B2 receptors, detected in membranes by [3H-bradykinin] binding, showed a Kd of 0.66 nmol/L and an expression level of 2.57 pmol/mg of protein at 54 h postinfection. In these cells, bradykinin induced a transient increase of intracellular calcium ([Ca2+]i) in fura 2-AM loaded sf21 cells, and promoted [35S]-GTPγS binding to membranes.…

medicine.medical_specialtyReceptor Bradykinin B2G proteinGene Expressionchemistry.chemical_elementBradykininReceptors Cell SurfaceSpodopteraCalciumBiologyBradykininBiochemistryCalcium in biologychemistry.chemical_compoundGTP-Binding ProteinsInternal medicineHomologous desensitizationmedicineAnimalsHumansPhosphorylationBradykinin receptorPhosphoamino AcidsReceptorOctopamineMolecular BiologyBradykinin Receptor AntagonistsCells CulturedMicroscopy ConfocalReceptors BradykininCell MembraneCell BiologyProtein-Tyrosine KinasesTyrphostinsGenisteinMolecular biologyRecombinant ProteinsEndocrinologychemistryGuanosine 5'-O-(3-Thiotriphosphate)ThapsigarginCalciumBaculoviridaeTyrosine kinaseProtein BindingJournal of Cellular Biochemistry
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