Search results for "Signal Transducing"

showing 10 items of 156 documents

cIAP1-dependent TRAF2 degradation regulates the differentiation of monocytes into macrophages and their response to CD40 ligand.

2008

AbstractPeripheral blood monocytes are plastic cells that migrate to tissues and differentiate into various cell types, including macrophages, dendritic cells, and osteoclasts. We have described the migration of cellular inhibitor of apoptosis protein 1 (cIAP1), a member of the IAP family of proteins, from the nucleus to the Golgi apparatus in monocytes undergoing differentiation into macrophages. Here we show that, once in the cytoplasm, cIAP1 is involved in the degradation of the adaptor protein tumor necrosis factor receptor–associated factor 2 (TRAF2) by the proteosomal machinery. Inhibition of cIAP1 prevents the decrease in TRAF2 expression that characterizes macrophage formation. We d…

TRAF2CytoplasmCellular differentiationImmunologyCD40 LigandDown-RegulationGene ExpressionGolgi ApparatusBiologyBiochemistryMonocytesProinflammatory cytokineInhibitor of Apoptosis ProteinsPhagocytes Granulocytes and MyelopoiesisPhagocytosisMacrophageHumansRNA Small InterferingCD40U937 cellMacrophagesSignal transducing adaptor proteinCell DifferentiationCell BiologyHematologyU937 CellsTNF Receptor-Associated Factor 2Molecular biologyCell biologybiology.proteinTumor necrosis factor alphaBlood
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Kti12, a PSTK-like tRNA dependent ATPase essential for tRNA modification by Elongator

2019

Abstract Posttranscriptional RNA modifications occur in all domains of life. Modifications of anticodon bases are of particular importance for ribosomal decoding and proteome homeostasis. The Elongator complex modifies uridines in the wobble position and is highly conserved in eukaryotes. Despite recent insights into Elongator's architecture, the structure and function of its regulatory factor Kti12 have remained elusive. Here, we present the crystal structure of Kti12′s nucleotide hydrolase domain trapped in a transition state of ATP hydrolysis. The structure reveals striking similarities to an O-phosphoseryl-tRNA kinase involved in the selenocysteine pathway. Both proteins employ similar …

TRNA modificationSaccharomyces cerevisiae ProteinsProtein ConformationWobble base pairSaccharomyces cerevisiaeBiologyChaetomiumCrystallography X-Ray03 medical and health scienceschemistry.chemical_compound0302 clinical medicineRNA TransferATP hydrolysisGeneticsRNA and RNA-protein complexesAnticodonRNA Processing Post-TranscriptionalUridine030304 developmental biologyAdaptor Proteins Signal TransducingAdenosine Triphosphatases0303 health sciencesSelenocysteineRNATRNA bindingCell biologychemistryTransfer RNASelenocysteine incorporationCarrier ProteinsRibosomes030217 neurology & neurosurgery
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Binding properties and stability of the Ras-association domain of Rap1-GTP interacting adapter molecule (RIAM).

2012

The Rap1-GTP interacting adapter protein (RIAM) is an important protein in Rap1-mediated integrin activation. By binding to both Rap1 GTPase and talin, RIAM recruits talin to the cell membrane, thus facilitating talin-dependent integrin activation. In this article, we studied the role of the RIAM Ras-association (RA) and pleckstrin-homology (PH) domains in the interaction with Rap1. We found that the RA domain was sufficient for GTP-dependent interaction with Rap1B, and the addition of the PH domain did not change the binding affinity. We also detected GTP-independent interaction of Rap1B with the N-terminus of RIAM. In addition, we found that the PH domain stabilized the RA domain both in …

TalinIntegrinsGTP'lcsh:MedicineGTPaseSignal transductionBiochemistryProtein structureMolecular cell biologyRIAMlcsh:Science0303 health sciencesMultidisciplinarybiologyProtein Stability030302 biochemistry & molecular biologySignal transducing adaptor proteinrap1 GTP-Binding ProteinssitoutuminenCell biologyPleckstrin homology domainRap1Research Articleendocrine systemvuorovaikutusProtein domainIntegrinSignaling in cellular processesPhosphoinositide Signal TransductionSignaling Pathways03 medical and health sciencesCell AdhesionHumansProtein InteractionsBiologyGTPase signaling030304 developmental biologyRas signalingAdaptor Proteins Signal Transducingintegriinitlcsh:RProteinsMembrane ProteinsRegulatory ProteinsProtein Structure TertiaryCytoskeletal Proteinsenzymes and coenzymes (carbohydrates)rap GTP-Binding ProteinsCell movement signalingbiology.proteinta1181lcsh:QPLoS ONE
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In human endothelial cells rapamycin causes mTORC2 inhibition and impairs cell viability and function.

2008

Aim Drug-eluting stents are widely used to prevent restenosis but are associated with late endothelial damage. To understand the basis for this effect, we have studied the consequences of a prolonged incubation with rapamycin on the viability and functions of endothelial cells. Methods and results Human umbilical vein or aorta endothelial cells were exposed to rapamycin in the absence or in the presence of tumour necrosis factor α (TNFα). After a 24 h-incubation, rapamycin (100 nM) caused a significant cell loss associated with the increase of both apoptosis and necrosis, as quantified by propidium iodide staining, caspase 3 activity, and lactate dehydrogenase release. Rapamycin also impair…

Time FactorsPhysiologyApoptosismTORC1Polymerase Chain Reactionchemistry.chemical_compoundCell MovementStress FibersMicroscopy ConfocalCaspase 3TOR Serine-Threonine KinasesNitric Oxide Synthase Type IIIRibosomal Protein S6 Kinases 70-kDaUp-RegulationEndothelial stem cellmedicine.anatomical_structureBiochemistryCardiology and Cardiovascular MedicineE-SelectinEndotheliumNitric Oxide Synthase Type IIICell SurvivalBlotting WesternEnzyme-Linked Immunosorbent AssayBiologyMechanistic Target of Rapamycin Complex 1Nitric OxideTacrolimusNecrosisTheophyllinePhysiology (medical)medicineHumansImmunoprecipitationViability assayPropidium iodideProtein kinase BAdaptor Proteins Signal TransducingSirolimusDose-Response Relationship DrugL-Lactate DehydrogenaseTumor Necrosis Factor-alphaEndothelial CellsProteinsCardiovascular AgentsRegulatory-Associated Protein of mTORMolecular biologyRapamycin-Insensitive Companion of mTOR ProteinchemistryMultiprotein ComplexesTOR Serine-Threonine KinasesCarrier ProteinsProtein KinasesTranscription FactorsCardiovascular research
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Reduction of Cardiac Fibrosis by Interference With YAP-Dependent Transactivation

2022

Background: Conversion of cardiac stromal cells into myofibroblasts is typically associated with hypoxia conditions, metabolic insults, and/or inflammation, all of which are predisposing factors to cardiac fibrosis and heart failure. We hypothesized that this conversion could be also mediated by response of these cells to mechanical cues through activation of the Hippo transcriptional pathway. The objective of the present study was to assess the role of cellular/nuclear straining forces acting in myofibroblast differentiation of cardiac stromal cells under the control of YAP (yes-associated protein) transcription factor and to validate this finding using a pharmacological agent that interf…

Transcriptional ActivationPhysiologyfibrosismyofibroblastsVerteporfinheart failureYAP-Signaling ProteinsSettore MED/11 - Malattie dell'Apparato CardiovascolareSettore MED/23 - Chirurgia Cardiacafibrosis; heart failure; myofibroblasts; stromal cell; transcription factorsstromal cellPhosphoproteinscell mechanics; fibrosis; heart failure; myofibroblasts; stromal cell; YAP transcription factor;MiceYAP transcription factorcell mechanicsSettore CHIM/09 - Farmaceutico Tecnologico Applicativotranscription factorsTrans-ActivatorsAnimalsHumansCardiology and Cardiovascular MedicineAdaptor Proteins Signal Transducing
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Binding of PTEN to specific PDZ domains contributes to PTEN protein stability and phosphorylation by microtubule-associated serine/threonine kinases

2005

The tumor suppressor phosphatase PTEN is a key regulator of cell growth and apoptosis that interacts with PDZ domains from regulatory proteins, including MAGI-1/2/3, hDlg, and MAST205. Here we identified novel PTEN-binding PDZ domains within the MAST205-related proteins, syntrophin-associated serine/threonine kinase and MAST3, characterized the regions of PTEN involved in its interaction with distinctive PDZ domains, and analyzed the functional consequences on PTEN of PDZ domain binding. Using a panel of PTEN mutations, as well as PTEN chimeras containing distinct domains of the related protein TPTE, we found that the PTP and C2 domains of PTEN do not affect PDZ domain binding and that the …

Tumor Suppressor Proteins/chemistry/ metabolismTime FactorsAmino Acid MotifsPlasma protein bindingBiochemistryMicrotubulesSerineDiscs Large Homolog 1 ProteinProtein structureSaccharomyces cerevisiae/metabolismPhosphorylationGlutathione Transferaseddc:616Nucleoside-Phosphate Kinase/metabolismbiologyChemistryDystrophin-Associated Proteins/ chemistrySignal transducing adaptor proteinProtein-Serine-Threonine Kinases/metabolismRecombinant Fusion Proteins/chemistryGuanylate KinaseCell biologyCOS CellsMicrotubule-Associated Proteins/metabolismPhosphorylationProteins/metabolismGlutathione Transferase/metabolismMicrotubule-Associated ProteinsMicrotubules/ metabolismPlasmidsProtein BindingCèl·lulesRecombinant Fusion ProteinsPDZ domainSaccharomyces cerevisiaeProtein Serine-Threonine KinasesTransfectionModels BiologicalTwo-Hybrid System TechniquesDiscs Large Homolog 1 ProteinPTENAnimalsHumansImmunoprecipitationProteïnes supressores de tumorsMolecular BiologyAdaptor Proteins Signal TransducingTumor Suppressor ProteinsPTEN PhosphohydrolaseProteinsMembrane ProteinsCell BiologyPlasmids/metabolismPhosphoric Monoester HydrolasesProtein Structure TertiaryDystrophin-Associated ProteinsMutationCancer researchbiology.proteinNucleoside-Phosphate KinaseCarrier ProteinsGuanylate KinasesPhosphoric Monoester Hydrolases/chemistry/ metabolism
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Ubiquitin conjugating enzyme E2-N and sequestosome-1 (p62) are components of the ubiquitination process mediated by the malin-laforin E3-ubiquitin li…

2015

11 páginas, 9 figuras.

Ubiquitin-Protein LigasesUbiquitin-conjugating enzymeBiochemistryLafora diseaseSequestosome 1UbiquitinE2-conjugaseLaforinPhagosomesSequestosome-1 ProteinmedicineAutophagyLC3HumanseducationE3-ubiquitin ligaseAdaptor Proteins Signal Transducingchemistry.chemical_classificationDNA ligaseeducation.field_of_studybiologyUbiquitinationAutophagosomesCell Biologymedicine.diseaseProtein Tyrosine Phosphatases Non-ReceptorMalinUbiquitin ligaseCell biologyp62 (SQSTM1)UBE2NHEK293 CellschemistryBiochemistryGene Knockdown TechniquesUbiquitin-Conjugating Enzymesbiology.proteinCarrier ProteinsLaforinUbiquitin-Conjugating Enzyme E2 NProtein Binding
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Intraflagellar transport protein 172 is essential for primary cilia formation and plays a vital role in patterning the mammalian brain

2008

AbstractIFT172, also known as Selective Lim-domain Binding protein (SLB), is a component of the intraflagellar transport (IFT) complex. In order to evaluate the biological role of the Ift172 gene, we generated a loss-of-function mutation in the mouse. The resulting Slb mutant embryos die between E12.5 and 13.0, and exhibit severe cranio-facial malformations, failure to close the cranial neural tube, holoprosencephaly, heart edema and extensive hemorrhages. Cilia outgrowth in cells of the neuroepithelium is initiated but the axonemes are severely truncated and do not contain visible microtubules. Morphological and molecular analyses revealed a global brain-patterning defect along the dorsal–…

animal structuresBody PatterningNodal ProteinSlbNodalBiologyArticleMiceFGF8Intraflagellar transportHoloprosencephalymedicineMHB boundaryAnimalsHedgehog ProteinsRNA MessengerCiliaNodeMolecular BiologyAdaptor Proteins Signal TransducingBody PatterningGeneticsMammalsCell DeathCiliumEndodermNeural tubeIntracellular Signaling Peptides and ProteinsBrainGene Expression Regulation DevelopmentalCell BiologyEmbryo MammalianCell biologyNeuroepithelial cellGastrulationCytoskeletal Proteinsmedicine.anatomical_structurePhenotypeIFT172Gene Targetingembryonic structuresNODALBiomarkersGene DeletionDevelopmental BiologySignal TransductionDevelopmental Biology
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Effective targeting of breast cancer stem cells by combined inhibition of Sam68 and Rad51

2022

AbstractBreast cancer (BC) is the second cause of cancer-related deceases in the worldwide female population. Despite the successful treatment advances, 25% of BC develops resistance to current therapeutic regimens, thereby remaining a major hurdle for patient management. Current therapies, targeting the molecular events underpinning the adaptive resistance, still require effort to improve BC treatment. Using BC sphere cells (BCSphCs) as a model, here we showed that BC stem-like cells express high levels of Myc, which requires the presence of the multifunctional DNA/RNA binding protein Sam68 for the DNA-damage repair. Analysis of a cohort of BC patients displayed that Sam68 is an independen…

cancer stem cellCancer Researchtherapy resistanceDNA RepairSettore MED/50 - Scienze Tecniche Mediche ApplicateCell Cycle ProteinsBreast NeoplasmsTriple Negative Breast NeoplasmsMycCell LineBreast cancerSettore MED/04 - PATOLOGIA GENERALECell Line TumorGeneticsHumansMolecular BiologyAdaptor Proteins Signal TransducingTumorSignal TransducingRNA-Binding ProteinsAdaptor ProteinsDNA-Binding ProteinsSam68Neoplastic Stem CellsFemaleRad51 RecombinaseSettore MED/46 - Scienze Tecniche Di Medicina Di Laboratorio
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MiR-33a Controls hMSCS Osteoblast Commitment Modulating the Yap/Taz Expression Through EGFR Signaling Regulation

2019

Mesenchymal stromal cells (hMSCs) display a pleiotropic function in bone regeneration. The signaling involved in osteoblast commitment is still not completely understood, and that determines the failure of current therapies being used. In our recent studies, we identified two miRNAs as regulators of hMSCs osteoblast differentiation driving hypoxia signaling and cytoskeletal reorganization. Other signalings involved in this process are epithelial to mesenchymal transition (EMT) and epidermal growth factor receptor (EGFR) signalings through the regulation of Yes-associated protein (YAP)/PDZ-binding motif (TAZ) expression. In the current study, we investigated the role of miR-33a family as a (…

epithelial mesenchymal transitionregenerative medicinePDZ DomainsCell CommunicationArticlemicroRNAmedicineHumansEpidermal growth factor receptorEpithelial–mesenchymal transitionBone regenerationCells CulturedEGFR inhibitorsAdaptor Proteins Signal TransducingOsteoblastsmicroRNAbiologyMesenchymal stem cellComputational BiologyOsteoblastMesenchymal Stem CellsYAP-Signaling ProteinsGeneral MedicinePhenotypeCell biologymicroRNAsErbB Receptorsmedicine.anatomical_structureTranscriptional Coactivator with PDZ-Binding Motif Proteinsmesenchymal stromal cellbiology.proteinTrans-Activatorsmesenchymal stromal cellsEGFR signalingSignal TransductionTranscription FactorsCells
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