Search results for "Ubiquitination"

showing 9 items of 39 documents

Protein Kinase C-dependent Ubiquitination and Clathrin-mediated Endocytosis of the Cationic Amino Acid Transporter CAT-1*

2011

Cationic amino acid transporter 1 (CAT-1) is responsible for the bulk of the uptake of cationic amino acids in most mammalian cells. Activation of protein kinase C (PKC) leads to down-regulation of the cell surface CAT-1. To examine the mechanisms of PKC-induced down-regulation of CAT-1, a functional mutant of CAT-1 (CAT-1-HA-GFP) was generated in which a hemagglutinin antigen (HA) epitope tag was introduced into the second extracellular loop and GFP was attached to the carboxyl terminus. CAT-1-HA-GFP was stably expressed in porcine aorthic endothelial and human epithelial kidney (HEK) 293 cells. Using the HA antibody internalization assay we have demonstrated that PKC-dependent endocytosis…

Swinemedia_common.quotation_subjectNedd4 Ubiquitin Protein LigasesUbiquitin-Protein LigasesUbiquitin-conjugating enzymeEndocytosisBiochemistryClathrinProtein Structure SecondaryMembrane BiologyAnimalsHumansAmino acid transporterInternalizationMolecular BiologyProtein kinase CProtein Kinase Cmedia_commonCationic Amino Acid Transporter 1biologyEndosomal Sorting Complexes Required for TransportUbiquitinationClathrin-Coated VesiclesCell BiologyReceptor-mediated endocytosisClathrinEndocytosisCell biologyUbiquitin ligaseHEK293 CellsBiochemistrybiology.protein
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UbcD1 is a Histone H2B Ubiquitin-Conjugating Enzyme Essential for Global Chromatin Structure and Gene Expression Regulation

2014

UbcD1 ubiquitination chromatin drosophila
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Alix protein is substrate of Ozz-E3 ligase and modulates actin remodeling in skeletal muscle

2012

Alix/AIP1 is a multifunctional adaptor protein that participates in basic cellular processes, including membrane trafficking and actin cytoskeleton assembly, by binding selectively to a variety of partner proteins. However, the mechanisms regulating Alix turnover, subcellular distribution, and function in muscle cells are unknown. We now report that Alix is expressed in skeletal muscle throughout myogenic differentiation. In myotubes, a specific pool of Alix colocalizes with Ozz, the substrate-binding component of the muscle-specific ubiquitin ligase complex Ozz-E3. We found that interaction of the two endogenous proteins in the differentiated muscle fibers changes Alix conformation and pro…

Ubiquitin-Protein LigasesMuscle Fibers Skeletalmacromolecular substancesBiochemistryCell LineMiceCell MovementTwo-Hybrid System TechniquesmedicineCell AdhesionAnimalsProtein Interaction Domains and MotifsPseudopodiaMuscle SkeletalMolecular BiologyActinMice KnockoutbiologyMyogenesisSettore BIO/16 - Anatomia UmanaCalcium-Binding ProteinsUbiquitinationActin remodelingSkeletal muscleUbiquitin-Protein Ligase ComplexesCell BiologyActin cytoskeletonUbiquitin ligaseCell biologyRepressor ProteinsActin CytoskeletonProtein Transportmedicine.anatomical_structureUbiquitin ligase complexbiology.proteinCell Migration Myogenesis Skeletal Muscle Ubiquitin Ligase Ubiquitination Alix F-actin Ozz-E3 Ubiquitin Ligase Skeletal Muscle CellsCortactinCortactinProtein Binding
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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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dsRNA induces apoptosis through an atypical death complex associating TLR3 to caspase-8

2012

Toll-like receptor 3 (TLR3) is a pattern-recognition receptor known to initiate an innate immune response when stimulated by double-stranded RNA (dsRNA). Components of TLR3 signaling, including TIR domain-containing adapter inducing IFN-α (TRIF), have been demonstrated to contribute to dsRNA-induced cell death through caspase-8 and receptor interacting protein (RIP)1 in various human cancer cells. We provide here a detailed analysis of the caspase-8 activating machinery triggered in response to Poly(I:C) dsRNA. Engagement of TLR3 by dsRNA in both type I and type II lung cancer cells induces the formation of an atypical caspase-8-containing complex that is devoid of classical death receptors…

Ubiquitin-Protein LigasesvirusesApoptosischemical and pharmacologic phenomenaInhibitor of Apoptosis ProteinsCell Line TumorHumansFADDMolecular BiologyRNA Double-StrandedDeath domainCaspase 8Original PaperbiologyUbiquitinationRNA-Binding Proteinshemic and immune systemsMDA5Cell BiologyTNF Receptor-Associated Factor 2Fas receptorTRADDBaculoviral IAP Repeat-Containing 3 ProteinTNF Receptor-Associated Death Domain ProteinToll-Like Receptor 3Cell biologyNuclear Pore Complex ProteinsUbiquitin ligase complexDeath-inducing signaling complexTLR3biology.proteinSignal TransductionCell Death & Differentiation
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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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Echovirus 1 infectious entry via novel multivesicular bodies

2011

integriinitmakropinosytoosiviruksetmacropinocytosisα2β1 integriiniubiquitinationmonirakkulaiset solurakenteetinfektiotmultivesicular bodyESCRTenteroviruksetubikitinaatioα2β1 integrinEV1integrinsendocytosisECHO-viruksetEchovirus 1endosytoosi
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The deubiquitinating enzyme CYLD regulates the differentiation and maturation of thymic medullary epithelial cells.

2014

The cross talk between thymocytes and the thymic epithelium is critical for T-cell development and the establishment of central tolerance. Medullary thymic epithelial cells (mTECs) are located in the thymic medulla and mediate the elimination of self-reactive thymocytes, thereby preventing the onset of autoimmunity. Previous studies identified the deubiquitinating enzyme CYLD as a critical regulator of T-cell development by activating proximal T-cell receptor signaling during the transition of double-positive to single-positive thymocytes. Here we evaluated the impact of the naturally occurring short-splice variant of the cyld gene (sCYLD) on the development and maturation of mTECs. We foun…

medicine.medical_specialtyMedullary cavityImmunologyReceptors Antigen T-CellCell CountThymus GlandBiologyDeubiquitinating Enzyme CYLDImmunophenotypingMiceInternal medicinemedicineImmunology and AllergyAnimalsMice KnockoutThymocytesUbiquitinationCell DifferentiationEpithelial CellsCell BiologyCell biologyDeubiquitinating Enzyme CYLDCysteine EndopeptidasesEndocrinologyPhenotypeAntigens SurfaceMutationFemaleSignal TransductionImmunology and cell biology
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The E3 Ubiquitin Ligase MID1 Catalyzes Ubiquitination and Cleavage of Fu

2014

Sonic Hedgehog (SHH)-GLI signalling plays an important role during embryogenesis and in tumorigenesis. The survival and growth of several types of cancer depend on autonomously activated SHH-GLI signalling. A protein complex containing the ubiquitin-ligase MID1 and protein phosphatase 2A (PP2A) regulates the nuclear localization and transcriptional activity of GLI3, a transcriptional effector molecule of SHH, in cancer cell lines with autonomously activated SHH signalling. However, the exact molecular mechanisms that mediate the interaction between MID1 and GLI3 remained unknown. Here, we show that MID1 catalyses the ubiquitination and proteasomal cleavage of the GLI3-regulator Fu. Our data…

metabolism [Microtubule Proteins]Ubiquitin-conjugating enzymeBiochemistrymetabolism [Protein Serine-Threonine Kinases]Ubiquitinmetabolism [Transcription Factors]Nuclear proteinSonic hedgehogbiologymetabolism [Protein-Serine-Threonine Kinases]Nuclear Proteinsrespiratory systemProtein-Serine-Threonine KinasesUbiquitin ligaseGene Expression Regulation NeoplasticGLI3 protein humanBiochemistryddc:540embryonic structuresMicrotubule Proteinsmetabolism [Hedgehog Proteins]Function and Dysfunction of the Nervous Systemmetabolism [Nuclear Proteins]Signal Transductionmetabolism [Kruppel-Like Transcription Factors]Proteasome Endopeptidase Complexanimal structuresSTK36 protein humanUbiquitin-Protein LigasesKruppel-Like Transcription FactorsNerve Tissue ProteinsProtein Serine-Threonine Kinaseschemistry [Ubiquitin-Protein Ligases]CatalysisZinc Finger Protein Gli3Cell Line TumorGLI3HumansHedgehog Proteinsmetabolism [Proteasome Endopeptidase Complex]metabolism [Cell Nucleus]Molecular Biologychemistry [Lysine]DNA PrimersCell Nucleusmetabolism [Nerve Tissue Proteins]UbiquitinLysineUbiquitinationCell BiologyProtein phosphatase 2chemistry [Ubiquitin]Proteasomebiology.proteinSHH protein humanhuman activitiesMid1 protein humanHeLa CellsTranscription FactorsJournal of Biological Chemistry
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