Search results for "Two-Hybrid System Techniques"

showing 10 items of 27 documents

Regulation of reactive oxygen species production by a 14-3-3 protein in elicited tobacco cells.

2007

International audience; The regulation of the system responsible for the production of reactive oxygen species (ROS) during plant–microorganism interaction is still largely unknown. The protein NtrbohD has been recently demonstrated as the plasma membrane oxidase responsible for ROS production in elicited tobacco cells. Here, its C-terminus part was used as a bait in a two-hybrid screen in order to identify putative regulators of this system. This led to the isolation of a cDNA coding for a member of the 14-3-3 protein family. The corresponding transcript was induced after infiltration of tobacco leaves with the fungal elicitor cryptogein. Tobacco cells transformed with an antisense constru…

0106 biological sciencesSIGNALLINGDNA ComplementaryProtein familyPhysiologyMolecular Sequence DataContext (language use)Plant ScienceBiology01 natural sciences03 medical and health sciencesTwo-Hybrid System TechniquesTobaccoNADPH OXIDASEAmino Acid Sequence14-3-3 protein030304 developmental biologychemistry.chemical_classification[SDV.EE]Life Sciences [q-bio]/Ecology environment0303 health sciencesReactive oxygen speciesOxidase testCRYPTOGEINNADPH oxidaseSequence Homology Amino AcidElicitorchemistryBiochemistry14-3-3 ProteinsNAD(P)H oxidasebiology.proteinReactive Oxygen Species010606 plant biology & botanyPlant, cellenvironment
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The Cytoskeletal Adaptor Obscurin-Like 1 Interacts with the Human Papillomavirus 16 (HPV16) Capsid Protein L2 and Is Required for HPV16 Endocytosis.

2016

ABSTRACT The human papillomavirus (HPV) capsid protein L2 is essential for viral entry. To gain a deeper understanding of the role of L2, we searched for novel cellular L2-interacting proteins. A yeast two-hybrid analysis uncovered the actin-depolymerizing factor gelsolin, the membrane glycoprotein dysadherin, the centrosomal protein 68 (Cep68), and the cytoskeletal adaptor protein obscurin-like 1 protein (OBSL1) as putative L2 binding molecules. Pseudovirus (PsV) infection assays identified OBSL1 as a host factor required for gene transduction by three oncogenic human papillomavirus types, HPV16, HPV18, and HPV31. In addition, we detected OBSL1 expression in cervical tissue sections and no…

0301 basic medicineKeratinocytesvirusesImmunologyEndocytic cycleEndocytosisMicrobiologyClathrinCell Line03 medical and health sciencesTransduction (genetics)TetraspaninViral entryVirologyTwo-Hybrid System TechniquesCaveolinHumansHuman papillomavirus 16biologyPapillomavirus InfectionsSignal transducing adaptor proteinOncogene Proteins ViralVirus InternalizationEndocytosisCell biologyVirus-Cell InteractionsCytoskeletal Proteins030104 developmental biologyInsect ScienceGene Knockdown TechniquesHost-Pathogen Interactionsbiology.proteinCapsid ProteinsHeLa CellsJournal of virology
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Search for variants of the gene-promoter and the potential phosphotyrosine encoding sequence of the insulin receptor substrate-2 gene: evaluation of …

1999

Aims/hypothesis. The aim of this study was to screen part of the putative promoter sequence in addition to 14 potential phosphotyrosine residues of human IRS-2 for genetic variability which might cause changes in protein expression or function. Furthermore, the potential impact on insulin secretion and sensitivity of a previously identified IRS-2 variant (Gly1057Asp) was analysed Methods. The screenings were carried out by the SSCP-heteroduplex technique on DNA from Type II (non-insulin-dependent) diabetic patients. The impact of the Gly1057Asp variant was analysed in four glucose-tolerant Scandinavian study groups. Results. The results showed no nucleotide substitutions in the promoter seq…

AdultMalemedicine.medical_specialtyAdolescentInsulin Receptor Substrate ProteinsEndocrinology Diabetes and Metabolismmedicine.medical_treatmentMolecular Sequence Datamedicine.disease_causeGene FrequencyTwo-Hybrid System TechniquesInternal medicineDiabetes mellitusInsulin SecretionInternal MedicinemedicineHumansInsulinGenetic TestingProspective StudiesPhosphotyrosinePromoter Regions GeneticPolymorphism Single-Stranded ConformationalPancreatic hormoneAgedMutationGlucose tolerance testBase Sequencebiologymedicine.diagnostic_testGenetic Carrier ScreeningInsulinIntracellular Signaling Peptides and ProteinsGlucose Tolerance TestMiddle AgedPhosphoproteinsmedicine.diseaseIRS2PedigreeInsulin receptorEndocrinologyAmino Acid SubstitutionDiabetes Mellitus Type 2Insulin Receptor Substrate Proteinsbiology.proteinDiabetologia
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RPGR ORF15 isoform co-localizes with RPGRIP1 at centrioles and basal bodies and interacts with nucleophosmin

2005

The ORF15 isoform of RPGR (RPGR(ORF15)) and RPGR interacting protein 1 (RPGRIP1) are mutated in a variety of retinal dystrophies but their functions are poorly understood. Here, we show that in cultured mammalian cells both RPGR(ORF15) and RPGRIP1 localize to centrioles. These localizations are resistant to the microtubule destabilizing drug nocodazole and persist throughout the cell cycle. RPGR and RPGRIP1 also co-localize at basal bodies in cells with primary cilia. The C-terminal (C2) domain of RPGR(ORF15) (ORF15(C2)) is highly conserved across 13 mammalian species, suggesting that it is a functionally important domain. Using matrix-assisted laser desorption ionization time-of-flight mas…

CentrioleFluorescent Antibody TechniqueMicechemistry.chemical_compoundChlorocebus aethiopsGuanine Nucleotide Exchange FactorsProtein IsoformsBasal bodyConserved SequenceGenetics (clinical)CentriolesGlutathione Transferaseintegumentary systemNuclear ProteinsExonsGeneral MedicineRetinitis pigmentosa GTPase regulatorImmunohistochemistryNocodazoleCOS CellsNucleophosminCell NucleolusRecombinant Fusion ProteinsMolecular Sequence DataBiologyOpen Reading FramesMicrotubuleTwo-Hybrid System TechniquesGeneticsAnimalsHumansAmino Acid SequenceEye ProteinsMolecular BiologyNucleophosminSequence Homology Amino AcidProteinsPrecipitin TestsMolecular biologyeye diseasesProtein Structure TertiaryMice Inbred C57BLCytoskeletal ProteinschemistryCentrosomeCytoplasmSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationMutationCattleHeLa CellsHuman Molecular Genetics
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Myosin VIIa, harmonin and cadherin 23, three Usher I gene products that cooperate to shape the sensory hair cell bundle

2002

Deaf-blindness in three distinct genetic forms of Usher type I syndrome (USH1) is caused by defects in myosin VIIa, harmonin and cadherin 23. Despite being critical for hearing, the functions of these proteins in the inner ear remain elusive. Here we show that harmonin, a PDZ domain-containing protein, and cadherin 23 are both present in the growing stereocilia and that they bind to each other. Moreover, we demonstrate that harmonin b is an F-actin-bundling protein, which is thus likely to anchor cadherin 23 to the stereocilia microfilaments, thereby identifying a novel anchorage mode of the cadherins to the actin cytoskeleton. Moreover, harmonin b interacts directly with myosin VIIa, and i…

DNA ComplementaryCadherin Related ProteinsCell Cycle Proteinsmacromolecular substancesMyosinsBiologyTransfectionMicrofilamentGeneral Biochemistry Genetics and Molecular BiologyCell LineMiceCDH23Two-Hybrid System TechniquesHair Cells Auditoryotorhinolaryngologic diseasesmedicineAnimalsHumansProtein IsoformsRats WistarMolecular BiologyActinAdaptor Proteins Signal TransducingGene LibraryGeneral Immunology and MicrobiologyCadherinGeneral NeuroscienceStereociliaDyneinsCell DifferentiationArticlesCadherinsActin cytoskeletonActinsProtein Structure TertiaryRatsCell biologyCytoskeletal ProteinsMicroscopy Electronmedicine.anatomical_structureMicroscopy FluorescenceMyosin VIIasense organsCarrier ProteinsTip linkPCDH15HeLa CellsProtein BindingThe EMBO Journal
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Goodpasture antigen-binding protein, the kinase that phosphorylates the goodpasture antigen, is an alternatively spliced variant implicated in autoim…

2000

The non-collagenous C-terminal domain of the alpha(3) chain of collagen IV is the autoantigen in Goodpasture disease, an autoimmune disorder described only in humans. Specific N-terminal phosphorylation is a biological feature unique to the human domain when compared with other homologous domains lacking immunopathogenic potential. We have recently cloned from a HeLa-derived cDNA library a novel serine/threonine kinase (Goodpasture antigen-binding protein (GPBP)) that phosphorylates the N-terminal region of the human domain (Raya, A. Revert, F, Navarro, S. and Saus J. (1999) J. Biol. Chem. 274, 12642-12649). We show here that the pre-mRNA of GPBP is alternatively spliced in human tissues an…

Gene isoformCollagen Type IVMolecular Sequence DataBiologyProtein Serine-Threonine KinasesBiochemistryAutoantigensSerinePathogenesisTwo-Hybrid System TechniquesHumansAmino Acid SequencePhosphorylationMolecular BiologyCeramide Transfer ProteinBase SequenceKinasecDNA libraryCell BiologyDNACeramide transportMolecular biologyRecombinant ProteinsAlternative SplicingBiochemistryPhosphorylationCollagenThe Journal of biological chemistry
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The b1 isoform of protocadherin-gamma (Pcdhgamma) interacts with the microtubule-destabilizing protein SCG10.

2004

Due to their structural characteristics and their diversity, the 22 members of the protocadherin-gamma (Pcdhgamma) family have been suggested to contribute to the establishment of specific connections in the nervous system. Here, we focus on a single isoform, Pcdhgamma-b1. Its expression is found in different brain regions and in developing spinal cord it is restricted to scattered cells, whereas all cells are labeled using an antibody that recognizes all Pcdhgamma isoforms. As a first step to understanding the signaling mechanisms downstream of Pcdhgamma, we identify the microtubule-destabilizing protein SCG10 as a cytoplasmic interactor for Pcdhgamma-b1 and other isoforms of the Pcdhgamma…

Gene isoformNervous systemSubfamilyRecombinant Fusion ProteinsBiophysicsTwo-hybridProtocadherinCadherin Related ProteinsBiologyBiochemistryMicrotubulesMiceProtocadherinStructural BiologyMicrotubuleTwo-Hybrid System TechniquesChlorocebus aethiopsGeneticsmedicineAnimalsProtein IsoformsInteractorNerve Growth FactorsGrowth coneMolecular BiologyNeuronsProtocadherin-gammaCalcium-Binding ProteinsIntracellular Signaling Peptides and ProteinsBrainCell BiologySCGIOCadherinsMolecular biologyCell biologySCG10medicine.anatomical_structureCytoplasmCOS CellsStathminGrowth coneSignal TransductionFEBS letters
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Usher syndrome and Leber congenital amaurosis are molecularly linked via a novel isoform of the centrosomal ninein-like protein.

2009

Contains fulltext : 80984.pdf (Publisher’s version ) (Closed access) Usher syndrome (USH) and Leber congenital amaurosis (LCA) are autosomal recessive disorders resulting in syndromic and non-syndromic forms of blindness. In order to gain insight into the pathogenic mechanisms underlying retinal degeneration, we searched for interacting proteins of USH2A isoform B (USH2A(isoB)) and the LCA5-encoded protein lebercilin. We identified a novel isoform of the centrosomal ninein-like protein, hereby named Nlp isoform B (Nlp(isoB)), as a common interactor. Although we identified the capacity of this protein to bind calcium with one of its three EF-hand domains, the interacton with USH2A(isoB) did …

Gene isoformRetinal degenerationCandidate geneGenetics and epigenetic pathways of disease [NCMLS 6]Usher syndromeMolecular Sequence DataOptic Atrophy Hereditary LeberBiologyIn Vitro TechniquesNeuroinformatics [DCN 3]CiliopathiesRetinaCell LineMiceCiliogenesisTwo-Hybrid System TechniquesGeneticsmedicineotorhinolaryngologic diseasesAnimalsHumansProtein IsoformsPhotoreceptor CellsAmino Acid SequenceNuclear proteinRats WistarEye ProteinsMolecular BiologyGenetics (clinical)GeneticsExtracellular Matrix ProteinsCiliumNuclear ProteinsGeneral MedicineArticlesmedicine.diseaseRatsMice Inbred C57BLMicrotubule-Associated ProteinsSequence AlignmentUsher SyndromesFunctional Neurogenomics [DCN 2]Protein BindingHuman Molecular Genetics
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Association of Whirlin with Cav1.3 (α1D) Channels in Photoreceptors, Defining a Novel Member of the Usher Protein Network

2010

Contains fulltext : 88383.pdf (Publisher’s version ) (Closed access) PURPOSE: Usher syndrome is the most common form of hereditary deaf-blindness. It is both clinically and genetically heterogeneous. The USH2D protein whirlin interacts via its PDZ domains with other Usher-associated proteins containing a C-terminal type I PDZ-binding motif. These proteins co-localize with whirlin at the region of the connecting cilium and at the synapse of photoreceptor cells. This study was undertaken to identify novel, Usher syndrome-associated, interacting partners of whirlin and thereby obtain more insights into the function of whirlin. METHODS: The database of ciliary proteins was searched for proteins…

Genetics and epigenetic pathways of disease [NCMLS 6]Calcium Channels L-TypeUsher syndromeProtein subunitImmunoelectron microscopyBlotting WesternPDZ domainRetinaCav1.3MiceTwo-Hybrid System TechniquesChlorocebus aethiopsmedicineAnimalsInner earRNA MessengerRats WistarDatabases ProteinMicroscopy ImmunoelectronPhotoreceptor Connecting CiliumIn Situ HybridizationRenal disorder [IGMD 9]RetinaVoltage-dependent calcium channelbiologyComputational BiologyMembrane Proteinsmedicine.diseaseeye diseasesRatsCell biologyMice Inbred C57BLmedicine.anatomical_structureCOS Cellsbiology.proteinsense organsFunctional Neurogenomics [DCN 2]Photoreceptor Cells VertebrateInvestigative Opthalmology & Visual Science
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Interaction of syntenin-1 and the NG2 proteoglycan in migratory oligodendrocyte precursor cells.

2008

Migration of oligodendrocyte precursors along axons is a necessary prerequisite for myelination, but little is known about underlying mechanisms. NG2 is a large membrane proteoglycan implicated in oligodendrocyte migration. Here we show that a PDZ domain protein termed syntenin-1 interacts with NG2 and that syntenin-1 is necessary for normal rates of migration. The association of syntenin-1 with NG2, identified in a yeast two-hybrid screen, was confirmed by colocalization of both proteins within processes of oligodendroglial precursor cells and by coimmunoprecipitation from cell extracts. Syntenin-1 also colocalizes with NG2 in "co-capping" assays, demonstrating a lateral association of bot…

ImmunoprecipitationSynteninsCellPDZ domainAmino Acid MotifsBiologyBiochemistryMiceCell MovementPrecursor cellTwo-Hybrid System TechniquesmedicineAnimalsHumansAntigensRNA Small InterferingMolecular BiologyCells CulturedNG2 proteoglycanColocalizationCell DifferentiationCell BiologyMolecular biologyOligodendrocyteCell biologyOligodendrogliamedicine.anatomical_structurenervous systemProteoglycanbiology.proteinProteoglycansNeurogliaProtein BindingThe Journal of biological chemistry
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