Search results for "Two-Hybrid System Techniques"

showing 7 items of 27 documents

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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LaXp180, a mammalian ActA-binding protein, identified with the yeast two-hybrid system, co-localizes with intracellular Listeria monocytogenes

2001

The Listeria monocytogenes surface protein ActA is an important virulence factor required for listerial intracellular movement by inducing actin polymerization. The only host cell protein known that directly interacts with ActA is the phosphoprotein VASP, which binds to the central proline-rich repeat region of ActA. To identify additional ActA-binding proteins, we applied the yeast two-hybrid system to search for mouse proteins that interact with ActA. A mouse cDNA library was screened for ActA-interacting proteins (AIPs) using ActA from strain L. monocytogenes EGD as bait. Three different AIPs were identified, one of which was identical to the human protein LaXp180 (also called CC1). Bind…

Two-hybrid screeningImmunologyMolecular Sequence DataAutophagy-Related ProteinsFluorescent Antibody TechniqueStathminmacromolecular substancesmedicine.disease_causeMicrobiologylaw.inventionCell LineMicefluids and secretionsListeria monocytogenesBacterial ProteinslawVirologyTwo-Hybrid System TechniquesmedicineAnimalsHumansListeriosisAmino Acid SequencebiologyReverse Transcriptase Polymerase Chain ReactionBinding proteintechnology industry and agricultureIntracellular Signaling Peptides and ProteinsMembrane ProteinsProteinsListeria monocytogenesActinsBiochemistryPhosphoproteinembryonic structuresCOS CellsRecombinant DNAbiology.proteinbacteriaSignal transductionCarrier ProteinsIntracellularPlasmids
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NOSIP, a novel modulator of endothelial nitric oxide synthase activity.

2001

Production of nitric oxide (NO) in endothelial cells is regulated by direct interactions of endothelial nitric oxide synthase (eNOS) with effector proteins such as Ca2+-calmodulin, by posttranslational modifications such as phosphorylation via protein kinase B, and by translocation of the enzyme from the plasma membrane caveolae to intracellular compartments. Reversible acylation of eNOS is thought to contribute to the intracellular trafficking of the enzyme; however, protein factor(s) that govern the translocation of the enzyme are still unknown. Here we have used the yeast two-hybrid system and identified a novel 34 kDa protein, termed NOSIP (eNOS interacting protein), which avidly binds …

Ubiquitin-Protein LigasesMolecular Sequence DataCHO CellsCaveolaeBiochemistryNitric oxideSubstrate Specificitychemistry.chemical_compoundEnosCaveolaeCricetinaeTwo-Hybrid System TechniquesGeneticsAnimalsHumansAmino Acid SequenceRNA MessengerMolecular BiologyProtein kinase BCalcimycinBinding SitesbiologyAkt/PKB signaling pathwayGene Expression Profilingbiology.organism_classificationImmunohistochemistryPrecipitin TestsTransport proteinCell biologyNitric oxide synthaseProtein TransportchemistryBiochemistrybiology.proteinEndothelium VascularNitric Oxide SynthaseCarrier ProteinsSequence AlignmentIntracellularBiotechnologyProtein BindingFASEB journal : official publication of the Federation of American Societies for Experimental Biology
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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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The Cth2 ARE-binding protein recruits the Dhh1 helicase to promote the decay of succinate dehydrogenase SDH4 mRNA in response to iron deficiency

2008

Iron is an essential nutrient that participates as a redox co-factor in a broad range of cellular processes. In response to iron deficiency, the budding yeast Saccharomyces cerevisiae induces the expression of the Cth1 and Cth2 mRNA-binding proteins to promote a genome-wide remodeling of cellular metabolism that contributes to the optimal utilization of iron. Cth1 and Cth2 proteins bind to specific AU-rich elements within the 3'-untranslated region of many mRNAs encoding proteins involved in iron-dependent pathways, thereby promoting their degradation. Here, we show that the DEAD box Dhh1 helicase plays a crucial role in the mechanism of Cth2-mediated mRNA turnover. Yeast two-hybrid experim…

Untranslated regionCytoplasmSaccharomyces cerevisiae ProteinsDEAD boxIronSaccharomyces cerevisiaeSaccharomyces cerevisiaeRNA-Mediated Regulation and Noncoding RnasModels BiologicalBiochemistryDEAD-box RNA HelicasesTristetraprolinGene Expression Regulation FungalTwo-Hybrid System TechniquesP-bodiesRNA MessengerMolecular BiologyMessenger RNAbiologySuccinate dehydrogenaseBinding proteinGalactoseHelicaseCell Biologybiology.organism_classificationProtein Structure TertiarySuccinate DehydrogenaseGlucoseBiochemistryMutationbiology.proteinPlasmids
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Interactions in the network of Usher syndrome type 1 proteins

2004

International audience; Defects in myosin VIIa, harmonin (a PDZ domain protein), cadherin 23, protocadherin 15 and sans (a putative scaffolding protein), underlie five forms of Usher syndrome type I (USH1). Mouse mutants for all these proteins exhibit disorganization of their hair bundle, which is the mechanotransduction receptive structure of the inner ear sensory cells, the cochlear and vestibular hair cells. We have previously demonstrated that harmonin interacts with cadherin 23 and myosin VIIa. Here we address the extent of interactions between the five known USH1 proteins. We establish the previously suggested sans-harmonin interaction and find that sans also binds to myosin VIIa. We …

[SDV]Life Sciences [q-bio]Hearing Loss SensorineuralStereocilia (inner ear)PDZ domainCadherin Related ProteinsProtocadherinCell Cycle ProteinsNerve Tissue ProteinsCuticular plateMyosinsBiologyMiceTwo-Hybrid System TechniquesHair Cells AuditoryBone plateMyosinotorhinolaryngologic diseasesGeneticsAnimalsHumansProtein PrecursorsMolecular BiologyGenetics (clinical)GeneticsStereociliumDyneinsSyndromeGeneral MedicineCadherinsCell biologyCytoskeletal ProteinsMyosin VIIaMutationsense organsCarrier ProteinsRetinitis PigmentosaPCDH15HeLa CellsProtein BindingHuman Molecular Genetics
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In vivo evaluation of the interaction between the Escherichia coli IGP synthase subunits using the Bacterial Two-Hybrid system

2020

ABSTRACT Histidine biosynthesis is one of the most characterized metabolic routes for its antiquity and its central role in cellular metabolism; indeed, it represents a cross-road between nitrogen metabolism and de novo synthesis of purines. This interconnection is due to the activity of imidazole glycerol phosphate synthase, a heterodimeric enzyme constituted by the products of two his genes, hisH and hisF, encoding a glutamine amidotransferase and a cyclase, respectively. Despite their interaction was suggested by several in vitro experiments, their in vivo complex formation has not been demonstrated. On the contrary, the analysis of the entire Escherichia coli interactome performed using…

medicine.disease_causeMicrobiologyInteractomeCyclase03 medical and health scienceschemistry.chemical_compoundBiosynthesisAminohydrolasesTwo-Hybrid System TechniquesEscherichia coliGeneticsmedicineHistidineAmino Acid SequencePurine metabolismMolecular BiologyEscherichia coliHistidine030304 developmental biologyGlutamine amidotransferase0303 health sciencesATP synthasebiologyEscherichia coli Proteins030302 biochemistry & molecular biologyProtein SubunitschemistryBiochemistrybiology.proteinProtein BindingFEMS Microbiology Letters
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