Search results for "ubiquitination"

showing 10 items of 39 documents

Tif1γ regulates the TGF-β1 receptor and promotes physiological aging of hematopoietic stem cells.

2014

The hematopoietic system declines with age. Myeloid-biased differentiation and increased incidence of myeloid malignancies feature aging of hematopoietic stem cells (HSCs), but the mechanisms involved remain uncertain. Here, we report that 4-mo-old mice deleted for transcription intermediary factor 1γ (Tif1γ) in HSCs developed an accelerated aging phenotype. To reinforce this result, we also show that Tif1γ is down-regulated in HSCs during aging in 20-mo-old wild-type mice. We established that Tif1γ controls TGF-β1 receptor (Tgfbr1) turnover. Compared with young HSCs, Tif1γ(-/-) and old HSCs are more sensitive to TGF-β signaling. Importantly, we identified two populations of HSCs specifical…

AgingMyeloidReceptor Transforming Growth Factor-beta Type IReceptors Cell SurfaceCell SeparationBiologyProtein Serine-Threonine KinasesTransforming Growth Factor beta1MiceSignaling Lymphocytic Activation Molecule Family Member 1Antigens CDmedicineAnimalsMyeloid CellsRNA MessengerPolyubiquitinTranscription factorCellular SenescenceRegulation of gene expressionMultidisciplinaryUbiquitinationhemic and immune systemsBiological SciencesHematopoietic Stem CellsCell biologyHematopoiesisHaematopoiesismedicine.anatomical_structurePhysiological AgingPhenotypeGene Expression RegulationSignal transductionStem cellCell agingReceptors Transforming Growth Factor betaSignal TransductionTranscription FactorsProceedings of the National Academy of Sciences of the United States of America
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Temporal quantitative phosphoproteomics of ADP stimulation reveals novel central nodes in platelet activation and inhibition

2017

Adenosine diphosphate (ADP) enhances platelet activation by virtually any other stimulant to complete aggregation. It binds specifically to the G-protein-coupled membrane receptors P2Y1 and P2Y12, stimulating intracellular signaling cascades, leading to integrin aIIbb3 activation, a process antagonized by endothelial prostacyclin. P2Y12 inhibitors are among the most successful antiplatelet drugs, however, show remarkable variability in efficacy. We reasoned whether a more detailed molecular understanding of ADP-induced protein phosphorylation could identify (1) critical hubs in platelet signaling toward aggregation and (2) novel molecular targets for antiplatelet treatment strategies. We ap…

0301 basic medicineBlood PlateletsPHOSPHATASEImmunologyBlotting WesternUBIQUITINATIONBINDING PROTEIN STXBP5Biochemistry03 medical and health scienceschemistry.chemical_compoundGTP-binding protein regulatorsP2Y12HumansProtein phosphorylationPlatelet activationIloprostPHOSPHORYLATIONCOMBINATIONChemistryPhosphoproteomicsPATHWAYSCell BiologyHematologyPlatelet ActivationSIGNALING REVEALSCell biologyAdenosine DiphosphateAdenosine diphosphate030104 developmental biologyCLOPIDOGRELPhosphorylationPROTEOMICSSECRETIONSignal transductionPlatelet Aggregation InhibitorsSignal TransductionBlood
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Ubiquitin ligase Rsp5p is involved in the gene expression changes during nutrient limitation inSaccharomyces cerevisiae

2009

Rsp5p is an essential ubiquitin ligase involved in many different cellular events, including amino acid transporters degradation, transcription initiation and mRNA export. It plays important role in both stress resistance and adaptation to the change of nutrients. We have found that ubiquitination machinery is necessary for the correct induction of the stress response SPI1 gene at the entry of the stationary phase. SPI1 is a gene whose expression is regulated by the nutritional status of the cell and whose deletion causes hypersensitivity to various stresses, such as heat shock, alkaline stress and oxidative stress. Its regulation is mastered by Rsp5p, as mutations in this gene lead to a lo…

Saccharomyces cerevisiae ProteinsTranscription GeneticBioengineeringSaccharomyces cerevisiaemedicine.disease_causeApplied Microbiology and BiotechnologyBiochemistryDDB1UbiquitinStress PhysiologicalGene Expression Regulation FungalGene expressionP-bodiesGeneticsmedicineGeneMutationMembrane GlycoproteinsSPI1Endosomal Sorting Complexes Required for TransportbiologyUbiquitinationUbiquitin-Protein Ligase ComplexesUbiquitin ligaseBiochemistryProtein Biosynthesisbiology.proteinBiotechnologyYeast
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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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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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Ubiquitin-Dependent And Independent Signals In Selective Autophagy.

2015

Selective autophagy regulates the abundance of specific cellular components via a specialized arsenal of factors, termed autophagy receptors, that target protein complexes, aggregates, and whole organelles into lysosomes. Autophagy receptors bind to LC3/GABARAP proteins on phagophore and autophagosome membranes, and recognize signals on cargoes to deliver them to autophagy. Ubiquitin (Ub), a well-known signal for the degradation of polypeptides in the proteasome, also plays an important role in the recognition of cargoes destined for selective autophagy. In addition, a variety of cargoes are committed to selective autophagy pathways by Ub-independent mechanisms employing protein-protein int…

0301 basic medicineAutophagosomebiologyUbiquitinGABARAPAutophagyUbiquitinationCell BiologyBAG3BioinformaticsCell biology03 medical and health sciences030104 developmental biologyProteasomeUbiquitinProteolysisbiology.proteinAutophagyAnimalsHumansTarget proteinATG16L1Signal TransductionTrends in cell biology
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BAG2 Interferes with CHIP-Mediated Ubiquitination of HSP72

2016

The maintenance of cellular proteostasis is dependent on molecular chaperones and protein degradation pathways. Chaperones facilitate protein folding, maturation, and degradation, and the particular fate of a misfolded protein is determined by the interaction of chaperones with co-chaperones. The co-factor CHIP (C-terminus of HSP70-inteacting protein, STUB1) ubiquitinates chaperone substrates and directs proteins to the cellular degradation systems. The activity of CHIP is regulated by two co-chaperones, BAG2 and HSPBP1, which are potent inhibitors of the E3 ubiquitin ligase activity. Here, we examined the functional correlation of HSP72, CHIP, and BAG2, employing human primary fibroblasts.…

0301 basic medicineTime FactorsUbiquitin-Protein LigasesImmunoblottingHSP72 Heat-Shock ProteinsUbiquitin-conjugating enzymeProtein degradationArticleCatalysisCell Linelcsh:ChemistryInorganic Chemistry03 medical and health sciencesUbiquitinddc:570Humansaging; BAG2; CHIP; HSP72; proteostasis; ubiquitinationPhysical and Theoretical ChemistryHSP72lcsh:QH301-705.5Molecular BiologyCellular SenescenceSpectroscopySTUB1proteostasisBAG2biologyCHIPagingOrganic ChemistryUbiquitinationGeneral MedicineComputer Science ApplicationsUbiquitin ligaseCell biology030104 developmental biologyProteostasislcsh:Biology (General)lcsh:QD1-999Chaperone (protein)biology.proteinRNA InterferenceProtein foldingMolecular ChaperonesInternational Journal of Molecular Sciences
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Aging of the musculoskeletal system: How the loss of estrogen impacts muscle strength.

2019

Skeletal muscle weakness occurs with aging and in females this is compounded by the loss of estrogen with ovarian failure. Estrogen deficiency mediates decrements in muscle strength from both inadequate preservation of skeletal muscle mass and decrements in the quality of the remaining skeletal muscle. Processes and components of skeletal muscle that are affected by estrogens are beginning to be identified. This review focuses on mechanisms that contribute to the loss of muscle force generation when estrogen is low in females, and conversely the maintenance of strength by estrogen. Evidence is accumulating that estrogen deficiency induces apoptosis in skeletal muscle contributing to loss of…

estrogeenit0301 basic medicinemedicine.medical_specialtyAgingProteasome Endopeptidase ComplexHistologyPhysiologymedicine.drug_classEndocrinology Diabetes and Metabolism030209 endocrinology & metabolismApoptosisArticle03 medical and health sciences0302 clinical medicineInternal medicineestrogenmedicineHumansMuscle Strengthskeletal muscleta315Muscle SkeletalMuscle forcebusiness.industryagingOvarian failureUbiquitinationSkeletal muscleta3141Estrogensmedicine.diseaseGenerating capacityikääntyminen030104 developmental biologymedicine.anatomical_structureEndocrinologyEstrogenSarcopeniaMuscle strengthEstrogenic EffectsFemalestrengthbusinesshormones hormone substitutes and hormone antagonistslihasvoimaBone
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HSP27 controls GATA-1 protein level during erythroid cell differentiation.

2010

AbstractHeat shock protein 27 (HSP27) is a chaperone whose cellular expression increases in response to various stresses and protects the cell either by inhibiting apoptotic cell death or by promoting the ubiquitination and proteasomal degradation of specific proteins. Here, we show that globin transcription factor 1 (GATA-1) is a client protein of HSP27. In 2 models of erythroid differentiation; that is, in the human erythroleukemia cell line, K562 induced to differentiate into erythroid cells on hemin exposure and CD34+ human cells ex vivo driven to erythroid differentiation in liquid culture, depletion of HSP27 provokes an accumulation of GATA-1 and impairs terminal maturation. More spec…

LeupeptinsPyridines[SDV]Life Sciences [q-bio]Cellular differentiationCellHSP27 Heat-Shock ProteinsAntigens CD34Biochemistryp38 Mitogen-Activated Protein Kinases0302 clinical medicineTransforming Growth Factor betahemic and lymphatic diseasesChlorocebus aethiopsGATA1 Transcription FactorPhosphorylationComputingMilieux_MISCELLANEOUSCells CulturedHeat-Shock Proteins0303 health sciencesbiologyImidazolesCell DifferentiationHematology[SDV] Life Sciences [q-bio]medicine.anatomical_structure030220 oncology & carcinogenesisembryonic structuresCOS CellsRNA InterferenceSignal transductionProteasome InhibitorsProtein BindingProteasome Endopeptidase ComplexImmunologyImmunoblotting03 medical and health sciencesHsp27Erythroid CellsHeat shock proteinmedicineAnimalsHumansTranscription factor030304 developmental biologyCell NucleusInterleukin-6UbiquitinationCell BiologyTransforming growth factor betaMolecular biologyChaperone (protein)biology.proteinK562 CellsHeLa CellsMolecular ChaperonesBlood
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OTUB1 inhibits CNS autoimmunity by preventing IFN-γ-induced hyperactivation of astrocytes.

2019

Astrocytes are critical regulators of neuroinflammation in multiple sclerosis (MS) and its animal model experimental autoimmune encephalomyelitis (EAE). Growing evidence indicates that ubiquitination of signaling molecules is an important cell‐intrinsic mechanism governing astrocyte function during MS and EAE. Here, we identified an upregulation of the deubiquitinase OTU domain, ubiquitin aldehyde binding 1 (OTUB1) in astrocytes during MS and EAE. Mice with astrocyte‐specific OTUB1 ablation developed more severe EAE due to increased leukocyte accumulation, proinflammatory gene transcription, and demyelination in the spinal cord as compared to control mice. OTUB1‐deficient astrocytes were hy…

Central Nervous SystemEncephalomyelitis Autoimmune ExperimentalNeuroimmunomodulationmedicine.medical_treatmentexperimental autoimmune encephalomyelitisAutoimmunityBiologymultiple sclerosisubiquitinationGeneral Biochemistry Genetics and Molecular BiologyProinflammatory cytokineneuroinflammationInterferon-gammaMice03 medical and health sciences0302 clinical medicineastrocytemedicineAnimalsMolecular BiologyCells CulturedNeuroinflammation030304 developmental biologyMice Knockout0303 health sciencesGeneral Immunology and MicrobiologySuppressor of cytokine signaling 1General NeuroscienceExperimental autoimmune encephalomyelitisArticlesmedicine.disease3. Good healthCell biologyMice Inbred C57BLCysteine EndopeptidasesCytokinemedicine.anatomical_structureAnimals NewbornAstrocytesSTAT proteinOTUB1FemaleNeurogenic InflammationJanus kinase030217 neurology & neurosurgeryAstrocyte
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