Search results for "ubiquitin ligase"

showing 10 items of 41 documents

The MID1 protein is a central player during development and in disease.

2015

Loss-of-function mutations in the MID1 gene cause a rare monogenic disorder, Opitz BBB/G syndrome (OS), which is characterized by malformations of the ventral midline. The MID1 gene encodes the MID1 protein, which assembles a large microtubule-associated protein complex. Intensive research over the past several years has shed light on the function of the MID1 protein as a ubiquitin ligase and regulator of mTOR signalling and translational activator. As a central player in the cell MID1 has been implicated in the pathogenesis of various other disorders in addition to OS including cancer and neurodegenerative diseases. Influencing the activity of the MID1 protein complex is a promising new st…

0301 basic medicinephysiopathology [Huntington Disease]CarcinogenesisUbiquitin-Protein LigasesRegulatorDiseaseBiologyBioinformaticsmedicine.disease_causephysiopathology [Alzheimer Disease]Congenital AbnormalitiesPathogenesis03 medical and health sciencesMiceAlzheimer Diseasephysiology [Nuclear Proteins]medicineAnimalsHumansgenetics [Microtubule Proteins]ddc:610GenePI3K/AKT/mTOR pathwayActivator (genetics)Nuclear Proteinsgenetics [Nuclear Proteins]genetics [Transcription Factors]physiology [Transcription Factors]Ubiquitin ligase030104 developmental biologyHuntington DiseaseMutationbiology.proteinMicrotubule Proteinsphysiology [Microtubule Proteins]CarcinogenesisMid1 protein humanTranscription FactorsFrontiers in bioscience (Landmark edition)
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The Role of p53 Signaling in Colorectal Cancer.

2021

Simple Summary The transcription factor p53 is a crucial tumor suppressor that regulates diverse cellular responses to protect against cancer development. Deactivating p53 signaling either by altering p53 regulators or by p53 mutations occurs frequently in human colorectal carcinoma (CRC). Forty-three percent of CRCs harbor p53 mutations that reduce wild-type p53 tumor suppressor activity and often provide neo-morphic functions, which contribute to tumorigenesis. In this review, we summarize wild-type p53 signaling, how it can be deregulated in CRC, and the functional and phenotypical effects of p53 mutations. We also discuss current therapeutic strategies of targeting p53. Abstract The tra…

0301 basic medicinewild type p53Cancer ResearchDNA repairCellular differentiationcolorectal cancerReview03 medical and health sciences0302 clinical medicinemedicineTranscription factorRC254-282gain-of-functionbiologyCell growthmutant p53CancerNeoplasms. Tumors. Oncology. Including cancer and carcinogensmedicine.diseaseUbiquitin ligasep53 signaling030104 developmental biologyOncology030220 oncology & carcinogenesisCancer cellbiology.proteinCancer researchMdm2cancer therapyp53 pathwayCancers
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Arabidopsis TCP Transcription Factors Interact with the SUMO Conjugating Machinery in Nuclear Foci

2017

In Arabidopsis more than 400 proteins have been identified as SUMO targets, both in vivo and in vitro. Among others, transcription factors (TFs) are common targets for SUMO conjugation. Here we aimed to exhaustively screen for TFs that interact with the SUMO machinery using an arrayed yeast two-hybrid library containing more than 1,100 TFs. We identified 76 interactors that foremost interact with the SUMO conjugation enzyme SCE1 and/or the SUMO E3 ligase SIZ1. These interactors belong to various TF families, which control a wide range of processes in plant development and stress signaling. Amongst these interactors, the TCP family was overrepresented with several TCPs interacting with diffe…

0301 basic medicineyeast two-hybridTwo-hybrid screeninggenetic processesSUMO proteinLaboratory of VirologyPlant Sciencemacromolecular substanceslcsh:Plant cultureenvironment and public healthLaboratorium voor Virologie03 medical and health sciencesArabidopsistranscription factorsTranscription factorslcsh:SB1-1110Transcription factorOriginal ResearchGeneticschemistry.chemical_classificationbiologySUMO conjugationChemistryYeast two-hybridbiology.organism_classificationIn vitroYeastCell biologyUbiquitin ligaseenzymes and coenzymes (carbohydrates)030104 developmental biologyEnzymeSUMObiology.proteinhealth occupationsEPSTCP
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TORC1 controls G1–S cell cycle transition in yeast via Mpk1 and the greatwall kinase pathway

2015

The target of rapamycin complex 1 (TORC1) pathway couples nutrient, energy and hormonal signals with eukaryotic cell growth and division. In yeast, TORC1 coordinates growth with G1–S cell cycle progression, also coined as START, by favouring the expression of G1 cyclins that activate cyclin-dependent protein kinases (CDKs) and by destabilizing the CDK inhibitor Sic1. Following TORC1 downregulation by rapamycin treatment or nutrient limitation, clearance of G1 cyclins and C-terminal phosphorylation of Sic1 by unknown protein kinases are both required for Sic1 to escape ubiquitin-dependent proteolysis prompted by its flagging via the SCFCdc4 (Skp1/Cul1/F-box protein) ubiquitin ligase complex.…

BioquímicaBiologiaSaccharomyces cerevisiae ProteinsImmunoblottingGeneral Physics and AstronomyCell Cycle ProteinsSaccharomyces cerevisiaeMechanistic Target of Rapamycin Complex 1ArticleGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciences0302 clinical medicineCyclin-dependent kinaseCyclinsImmunoprecipitationProtein Phosphatase 2Cell division control protein 4PhosphorylationProtein kinase ACyclin-Dependent Kinase Inhibitor Proteins030304 developmental biology0303 health sciencesMultidisciplinarybiologyTOR Serine-Threonine KinasesUbiquitin-Protein Ligase ComplexesGeneral ChemistryBlotting NorthernFlow CytometryG1 Phase Cell Cycle CheckpointsSic1Cyclin-Dependent KinasesCell biologyBiochemistryMultiprotein Complexes030220 oncology & carcinogenesisUbiquitin ligase complexbiology.proteinIntercellular Signaling Peptides and ProteinsPhosphorylationTOR Serine-Threonine KinasesMitogen-Activated Protein KinasesPeptidesProtein KinasesCyclin-dependent kinase inhibitor proteinNature Communications
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The MDM2-p53 pathway is involved in preconditioning-induced neuronal tolerance to ischemia

2018

Brain preconditioning (PC) refers to a state of transient tolerance against a lethal insult that can be evoked by a prior mild event. It is thought that PC may induce different pathways responsible for neuroprotection, which may involve the attenuation of cell damage pathways, including the apoptotic cell death. In this context, p53 is a stress sensor that accumulates during brain ischemia leading to neuronal death. The murine double minute 2 gene (MDM2), a p53-specific E3 ubiquitin ligase, is the main cellular antagonist of p53, mediating its degradation by the proteasome. Here, we study the role of MDM2-p53 pathway on PC-induced neuroprotection both in cultured neurons (in vitro) and rat …

Cell death0301 basic medicineProgrammed cell deathCell SurvivalNeuronalScience2415 Biología MolecularIschemiaNeuroprotectionArticleBrain ischemiaMiceBrain ischemia03 medical and health sciences0302 clinical medicineIschemiaXarxes neuronals (Neurobiologia)medicineAnimalsIschemic PreconditioningCell damageCells CulturedBrain preconditioningNeuronsMultidisciplinarybiologyChemistryQRBrainProto-Oncogene Proteins c-mdm2MDM2-p53medicine.diseaseNeuroprotectionRatsCell biologyUbiquitin ligaseDisease Models Animal030104 developmental biology2490 Neurocienciasbiology.proteinMedicineIschemic preconditioningMdm2Tumor Suppressor Protein p53030217 neurology & neurosurgerySignal Transduction
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Identification and characterization of the nano-sized vesicles released by muscle cells

2013

AbstractSeveral cell types secrete small membranous vesicles that contain cell-specific collections of proteins, lipids, and genetic material. The function of these vesicles is to allow cell-to-cell signaling and the horizontal transfer of their cargo molecules. Here, we demonstrate that muscle cells secrete nano-sized vesicles and that their release increases during muscle differentiation. Analysis of these nanovesicles allowed us to characterize them as exosome-like particles and to define the potential role of the multifunctional protein Alix in their biogenesis.

Cell typeCellular differentiationBiophysicsBiologyExosomesBiochemistryExosomeExosome; Nanovesicle; Alix; Ozz-E3 ubiquitin ligase; Muscle cellArticleCell Line03 medical and health sciencesMice0302 clinical medicineOzz-E3 ubiquitin ligaseStructural BiologyGeneticsMyocyteAnimalsSecretionMolecular Biology030304 developmental biology0303 health sciencesMuscle CellsSettore BIO/16 - Anatomia UmanaVesicleCalcium-Binding ProteinsCell MembraneMuscle cellCell DifferentiationCell BiologyCell biologyNanostructuresExosomeAlixCell culture030220 oncology & carcinogenesisNanovesicleBiogenesisFEBS Letters
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A variant of Smurf2 protects mice against colitis-associated colon cancer by inducing transforming growth factor β signaling.

2011

Background & Aims Transforming growth factor (TGF)-β signaling, which is down-regulated by the E3 ubiquitin ligase Smad ubiquitin regulating factor 2 (Smurf2), promotes development of cancer. We identified a splice variant of Smurf2 (ΔE2Smurf2) and investigated its role in colon carcinogenesis in mice. Methods Colitis-associated colon cancer was induced in mice by administration of azoxymethane, followed by 3 cycles of oral administration of dextran sodium sulfate. Messenger RNA levels of Smurf2 in colon tumors and control tissue were measured by quantitative polymerase chain reaction; lymphocyte and cytokine levels were measured in tumor and tissue samples. Results Tumor-infiltrating CD4 +…

Colorectal cancermedicine.medical_treatmentLymphocyteUbiquitin-Protein LigasesSMADBiologyProinflammatory cytokineReceptors G-Protein-Coupledchemistry.chemical_compoundMiceTransforming Growth Factor betamedicineAnimalsCells CulturedHepatologyAzoxymethaneGene Expression ProfilingGastroenterologymedicine.diseaseColitisMolecular biologyUbiquitin ligaseMice Inbred C57BLProto-Oncogene Proteins c-kitCytokinemedicine.anatomical_structureHyaluronan ReceptorschemistryColonic Neoplasmsbiology.proteinCancer researchTransforming growth factorSignal TransductionGastroenterology
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Comparative genomics and protein domain graph analyses link ubiquitination and RNA metabolism.

2006

The human gene parkin, known to cause familial Parkinson disease, as well as several other genes, likely involved in other neurodegenerative diseases or in cancer, encode proteins of the RBR family of ubiquitin ligases. Here, we describe the structural diversity of the RBR family in order to infer their functional roles. Of particular interest is a relationship detected between RBR-mediated ubiquitination and RNA metabolism: a few RBR proteins contain RNA binding domains and DEAH-box RNA helicase domains. Global protein domain graph analyses demonstrate that this connection is not RBR-specific, but instead many other proteins contain both ubiquitination and RNA-related domains. These protei…

Comparative genomicsGeneticsbiologyProtein ConformationUbiquitinUbiquitin-Protein LigasesProtein domainMolecular Sequence DataRNAGenomicsF-box proteinRNA Helicase AParkinUbiquitin ligaseProtein Structure TertiaryStructural Biologybiology.proteinAnimalsCluster AnalysisHumansRNAMolecular BiologyGeneAlgorithmsJournal of molecular biology
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DAZAP2 acts as specifier of the p53 response to DNA damage.

2021

Abstract The DNA damage-responsive tumor suppressors p53 and HIPK2 are well established regulators of cell fate decision-making and regulate the cellular sensitivity to DNA-damaging drugs. Here, we identify Deleted in Azoospermia-associated protein 2 (DAZAP2), a small adaptor protein, as a novel regulator of HIPK2 and specifier of the DNA damage-induced p53 response. Knock-down or genetic deletion of DAZAP2 strongly potentiates cancer cell chemosensitivity both in cells and in vivo using a mouse tumour xenograft model. In unstressed cells, DAZAP2 stimulates HIPK2 polyubiquitination and degradation through interplay with the ubiquitin ligase SIAH1. Upon DNA damage, HIPK2 site-specifically ph…

DNA damageAcademicSubjects/SCI00010Ubiquitin-Protein LigasesRegulatorAntineoplastic AgentsCell fate determinationProtein Serine-Threonine Kinases03 medical and health sciencesMice0302 clinical medicineUbiquitinCell Line TumorGeneticsAnimalsPromoter Regions GeneticGeneMolecular BiologyCells Cultured030304 developmental biologyRegulation of gene expressionCell Nucleus0303 health sciencesbiologyNuclear ProteinsRNA-Binding ProteinsCell biologyUbiquitin ligaseGene Expression Regulation030220 oncology & carcinogenesisCancer cellbiology.proteinTumor Suppressor Protein p53Carrier ProteinsDNA DamageNucleic acids research
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γ2-Adaptin, a Ubiquitin-interacting Adaptor, Is a Substrate to Coupled Ubiquitination by the Ubiquitin Ligase Nedd4 and Functions in the Endosomal Pa…

2008

gamma2-Adaptin is a putative member of the clathrin adaptor protein family with unknown physiological function. We previously reported that gamma2-adaptin acts as a ubiquitin receptor by virtue of its ubiquitin-interacting motif. Here we demonstrate that this motif mediates a specific physical interaction with the ubiquitin ligase Nedd4 and promotes ubiquitination of gamma2-adaptin. By mapping regions of Nedd4 involved in binding to gamma2-adaptin, we identified its C2 domain to be essential, whereas the WW and HECT domains are dispensable. Consistent with this, we uncovered that the C2 domain of Nedd4 is ubiquitinated itself and as such is recruited by the ubiquitin-interacting motif of ga…

EndosomeNedd4 Ubiquitin Protein LigasesUbiquitin-Protein LigasesAmino Acid MotifsNEDD4Endosomesmacromolecular substancesUbiquitin-conjugating enzymeBiochemistryClathrinSubstrate SpecificityUbiquitinCell Line TumorHumansAdaptor Protein Complex gamma SubunitsMolecular BiologyC2 domainEndosomal Sorting Complexes Required for TransportEpidermal Growth FactorbiologyUbiquitinCell MembraneUbiquitinationSignal transducing adaptor proteinCell BiologyUbiquitin ligaseCell biologybiology.proteinProtein BindingJournal of Biological Chemistry
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