Search results for "GTPase"

showing 10 items of 83 documents

Epigenetic activation of a cryptic TBC1D16 transcript enhances melanoma progression by targeting EGFR

2015

Metastasis is respoMetastasis is responsible for most cancer-related deaths, and, among common tumor types, melanoma is one with great potential to metastasize. Here we study the contribution of epigenetic changes to the dissemination process by analyzing the changes that occur at the DNA methylation level between primary cancer cells and metastases. We found a hypomethylation event that reactivates a cryptic transcript of the Rab GTPase activating protein TBC1D16 (TBC1D16-47 kDa; referred to hereafter as TBC1D16-47KD) to be a characteristic feature of the metastatic cascade. This short isoform of TBC1D16 exacerbates melanoma growth and metastasis both in vitro and in vivo. By combining imm…

Transcriptional ActivationGTPase-activating proteinImmunoprecipitationMice NudeEditorials: Cell Cycle FeaturesBiologyBioinformaticsMethylationGeneral Biochemistry Genetics and Molecular BiologyEpigenesis GeneticMetastasisMetastasisEpigènesiMetàstasiCell Line TumormedicineAnimalsImmunoprecipitationProtein IsoformsRNA MessengerEpigeneticsNeoplasm MetastasisRNA Small InterferingPromoter Regions GeneticProteïnes supressores de tumorsProtein Kinase InhibitorsMelanomaMelanomaGTPase-Activating ProteinsGeneral MedicineMethylationDNA MethylationPrognosismedicine.diseaseTumor suppressor proteinErbB ReceptorsMolecular WeightTreatment Outcomerab GTP-Binding ProteinsDNA methylationDisease ProgressionCancer researchRabMetilacióProtein BindingSignal TransductionEpigenesisNature Medicine
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Transcriptional activation of the small GTPase gene rhoB by genotoxic stress is regulated via a CCAAT element

2001

The gene encoding the Ras-related GTPase RhoB-specific is immediate-early inducible by genotoxic treatments. Regulation of transcriptional activation of rhoB is still unclear. Here we show that cells lacking either p53 or c-Fos are not different from wild-type cells with respect to the level of rhoB induction upon UV irradiation, indicating that these transcription factors are not crucial for stimulation of rhoB mRNA expression. Extracts from UV-irradiated and non-irradiated cells revealed similar DNA-binding activities to a 0.17 kb rhoB promoter fragment harboring the functional element(s) necessary for stimulation of rhoB by UV light. By means of immunoprecipitation we found that an ATF-2…

Transcriptional ActivationImmunoprecipitationUltraviolet RaysRHOBMolecular Sequence DataCAAT boxOligonucleotidesBiologyResponse ElementsArticlechemistry.chemical_compoundMiceRhoB GTP-Binding ProteinGeneticsAnimalsSmall GTPaseRNA MessengerPromoter Regions GeneticrhoB GTP-Binding ProteinTranscription factorBinding SitesCcaat-enhancer-binding proteinsBase Sequence3T3 CellsDNAMolecular biologyMethyl methanesulfonatechemistryCCAAT-Binding FactorMutationCCAAT-Enhancer-Binding ProteinsProtein BindingTranscription Factors
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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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cIAP1 oncogenic properties analysis : contribution of its partners cdc42 and E2F1

2014

The inhibitor of apoptosis protein cIAP1 (cellular inhibitor of apoptosis protein-1) from the IAP family (Inhibitor of Apoptosis Protein) is an oncogene with an E3 ubiquitin ligase activity. cIAP1 is relocalized from the nucleus to the cytoplasm during the differentiation of many kind of cellular models (macrophages, dendritic cells, colon epithelial cells, hematopoietic stem cells, cardiomyocytes) and this relocalization is associated with a proliferation arrest. The well-known functions of cIAP1 are associated with its cytoplasmic localization, where it regulates the TNFa receptors and NF-?B signaling pathways. However, cIAP1 is mainly expressed in the nucleus on many cell types which is …

[ SDV.BC ] Life Sciences [q-bio]/Cellular BiologyTNF-aFilipodiaProliferationActin cytoskeleton[SDV.BC]Life Sciences [q-bio]/Cellular BiologyCIAP1E2F1Rho GTPasesHRasCytosquelette d’actineOncogenic transformation[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyCdc42ProliférationFilipodes[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular Biology[SDV.BC] Life Sciences [q-bio]/Cellular BiologyTransformation oncogénique
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Plexin-B1 activates NF-κB and IL-8 to promote a pro-angiogenic response in endothelial cells.

2011

Background The semaphorins and their receptors, the plexins, are proteins related to c-Met and the scatter factors that have been implicated in an expanding signal transduction network involving co-receptors, RhoA and Ras activation and deactivation, and phosphorylation events. Our previous work has demonstrated that Semaphorin 4D (Sema4D) acts through its receptor, Plexin-B1, on endothelial cells to promote angiogenesis in a RhoA and Akt-dependent manner. Since NF-κB has been linked to promotion of angiogenesis and can be activated by Akt in some contexts, we wanted to examine NF-κB in Sema4D treated cells to determine if there was biological significance for the pro-angiogenic phenotype o…

animal structuresRHOAProto-Oncogene Proteins c-aktAngiogenesisSignaling in cellular processesG-protein signalingCancer TreatmentSEMA4Dlcsh:MedicineSignal transductionBiology03 medical and health sciencesMolecular cell biology0302 clinical medicineSemaphorinSettore BIO/10 - BiochimicaAkt Signaling CascadeMembrane Receptor SignalingInterleukin 8lcsh:ScienceBiologyProtein kinase BGTPase signalingRas signaling030304 developmental biology0303 health sciencesMultidisciplinaryMechanisms of Signal Transductionlcsh:RSignaling Cascades3. Good healthCell biologyPlexin B1RNA interferencepro-angiogenicendothelial cellsOncology030220 oncology & carcinogenesisembryonic structuresCancer researchbiology.proteinMedicinelcsh:QAntiangiogenesis TherapyAntiapoptotic signalingSignal transductionResearch ArticlePLoS ONE
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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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GTPases of the Rho Subfamily Are Required for Brucella abortus Internalization in Nonprofessional Phagocytes

2001

Members of the genus Brucella are intracellular -Proteobacteria responsible for brucellosis, a chronic disease of humans and animals. Little is known about Brucella virulence mechanisms, but the abilities of these bacteria to invade and to survive within cells are decisive factors for causing disease. Transmission electron and fluorescence microscopy of infected nonprofessional phagocytic HeLa cells revealed minor membrane changes accompanied by discrete recruitment of F-actin at the site of Brucella abortus entry. Cell uptake of B. abortus was negatively affected to various degrees by actin, actin-myosin, and microtubule chemical inhibitors. Modulators of MAPKs and protein-tyrosine kinases…

biologymedia_common.quotation_subjectIntracellular parasiteBRUCELLA ABORTUSVirulenceCell BiologyCDC42BrucellaGTPasebiology.organism_classificationBiochemistryMicrobiologyBRUCELOSISCytotoxic T cellBRUCELLAESCHERICHIA COLIBACTERIASInternalizationMolecular BiologyIntracellularmedia_commonJournal of Biological Chemistry
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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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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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The closure of Pak1-dependent macropinosomes requires the phosphorylation of CtBP1/BARS

2007

Membrane fission is an essential process in membrane trafficking and other cellular functions. While many fissioning and trafficking steps are mediated by the large GTPase dynamin, some fission events are dynamin independent and involve C-terminal-binding protein-1/brefeldinA-ADP ribosylated substrate (CtBP1/BARS). To gain an insight into the molecular mechanisms of CtBP1/BARS in fission, we have studied the role of this protein in macropinocytosis, a dynamin-independent endocytic pathway that can be synchronously activated by growth factors. Here, we show that upon activation of the epidermal growth factor receptor, CtBP1/BARS is (a) translocated to the macropinocytic cup and its surroundi…

genetic structuresEndocytic cycleGTPaseBiologyTRANSCRIPTIONAL COREPRESSOREPIDERMAL GROWTH-FACTORArticleGeneral Biochemistry Genetics and Molecular BiologySYNAPTIC VESICLE ENDOCYTOSISMembrane fissionCell Line TumorMacropinocytic cupHumansPhosphorylationMacropinosomeMolecular BiologyDynaminEpidermal Growth FactorGeneral Immunology and MicrobiologyMEMBRANE FISSIONGeneral NeuroscienceActinsEnterovirus B HumanProtein Structure TertiaryTransport proteinCell biologyDNA-Binding ProteinsAlcohol OxidoreductasesProtein Transportp21-Activated KinasesPLASMA-MEMBRANEPinocytosisPhosphorylationCell Surface ExtensionsIntegrin alpha2beta1The EMBO Journal
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