Search results for "Transducin"

showing 10 items of 169 documents

Contribution of Large Genomic Rearrangements in Italian Lynch Syndrome Patients: Characterization of a Novel Alu-Mediated Deletion

2012

Lynch syndrome is associated with germ-line mutations in the DNA mismatch repair (MMR) genes, mainlyMLH1andMSH2. Most of the mutations reported in these genes to date are point mutations, small deletions, and insertions. Large genomic rearrangements in the MMR genes predisposing to Lynch syndrome also occur, but the frequency varies depending on the population studied on average from 5 to 20%. The aim of this study was to examine the contribution of large rearrangements in theMLH1andMSH2genes in a well-characterised series of 63 unrelated Southern Italian Lynch syndrome patients who were negative for pathogenic point mutations in theMLH1,MSH2, andMSH6genes. We identified a large novel delet…

Malecongenital hereditary and neonatal diseases and abnormalitiesgenomic rearragementArticle SubjectPopulationlcsh:MedicineSettore BIO/11 - Biologia MolecolareBiologyMLH1General Biochemistry Genetics and Molecular Biologynovel Alu-mediated deletionAlu ElementsmedicineHumanseducationneoplasmsAdaptor Proteins Signal TransducingSequence DeletionGene RearrangementGeneticseducation.field_of_studyGeneral Immunology and MicrobiologyPoint mutationlcsh:RNuclear ProteinsLynch syndrome; genomic rearragements; novel Alu-mediated deletionnutritional and metabolic diseasesGeneral MedicineGene rearrangementmedicine.diseaseColorectal Neoplasms Hereditary NonpolyposisMolecular biologyLynch syndromedigestive system diseasesDNA-Binding ProteinsMSH6Settore MED/18 - Chirurgia GeneraleLynch syndromeMutS Homolog 2 ProteinItalyMSH2FemaleDNA mismatch repairMutL Protein Homolog 1Research ArticleBioMed Research International
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Germline deletion of Cetn1 causes infertility in male mice

2013

Centrins are calmodulin-like Ca2+-binding proteins that can be found in all ciliated eukaryotic cells from yeast to mammals. Expressed in male germ cells and photoreceptors, centrin 1 (CETN1) resides in the photoreceptor transition zone and connecting cilium. To identify its function in mammals, we deleted Cetn1 by homologous recombination. Cetn1−/− mice were viable and showed no sign of retina degeneration suggesting that CETN1 is nonessential for photoreceptor ciliogenesis or structural maintenance. Phototransduction components localized normally to the Cetn1−/− photoreceptor outer segments, and loss of CETN1 had no effect on light-induced translocation of transducin to the inner segment.…

Maleendocrine systemLight Signal TransductionCentrioleChromosomal Proteins Non-HistoneSpermiogenesisBiologyMice03 medical and health sciencesRetinal Rod Photoreceptor CellsCiliogenesismedicineAnimalsBasal bodyTransducinSpermatogenesisGerm-Line MutationInfertility MaleCentriolesSequence Deletion030304 developmental biologyMice KnockoutGenetics0303 health sciencesSpermatidCalcium-Binding ProteinsCell Cycle030302 biochemistry & molecular biologyCell DifferentiationCell BiologySpermatidsCell biologyMice Inbred C57BLmedicine.anatomical_structureCentrinFemalesense organsTransducinResearch ArticleVisual phototransductionJournal of Cell Science
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MORT1/FADD is involved in liver regeneration

2006

AIM: To explore the role of the adaptor molecule in liver regeneration after partial hepatectomy (PH). METHODS: We used transgenic mice expressing an N-terminal truncated form of MORT1/FADD under the control of the albumin promoter. As previously shown, this transgenic protein abrogated CD95- and CD120a-mediated apoptosis in the liver. Cyclin A expression was detected using Western blotting. ELISA and RT-PCR were used to detect IL-6 and IL-6 mRNA, respectively. DNA synthesis in liver tissue was measured by BrdU staining. RESULTS: Resection of 70% of the liver was followed by a reduced early regenerative response in the transgenic group at 36 h. Accordingly, 36 h after hepatectomy, cyclin A …

Malemedicine.medical_specialtyFas-Associated Death Domain Proteinmedicine.medical_treatmentTransgeneCyclin AApoptosisMice TransgenicCyclin AMiceInternal medicinemedicineAnimalsHepatectomyFADDAdaptor Proteins Signal TransducingCell ProliferationbiologyInterleukin-6GastroenterologyGeneral MedicineFas receptorMolecular biologyPeptide FragmentsLiver regenerationLiver RegenerationBlotBasic ResearchEndocrinologyApoptosisbiology.proteinHepatectomyWorld Journal of Gastroenterology
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Cannabinoid receptor 1 and acute resistance exercise – In vivo and in vitro studies in human skeletal muscle

2015

Abstract Aim This study aimed to determine whether Cannabinoid receptor 1 (CB1) is involved in mammalian target of rapamycin (mTOR) signaling and skeletal muscle protein synthesis. Methods This study used human vastus lateralis skeletal muscle biopsies obtained before and after a resistance exercise (RE) bout in young men (n = 18). The signaling mechanisms were studied in vitro in human myotubes. Protein expression was determined by Western blot and confocal microscopy, and gene expression by quantitative PCR. Protein synthesis was measured in vitro using puromycin-based SuNSET technique. Results In human skeletal muscle, an anabolic stimulus in the form of RE down-regulated CB1 expression.…

Malemedicine.medical_specialtyPhysiologyMAP Kinase Signaling SystemMuscle Fibers SkeletalGene ExpressionSkeletal muscleP70-S6 Kinase 1Cell Cycle ProteinsBiochemistryCell LineCellular and Molecular NeuroscienceYoung AdultEndocrinologyPiperidinesReceptor Cannabinoid CB1Internal medicinemedicineCannabinoid receptor type 2HumansCannabinoid receptor 1PhosphorylationMuscle Skeletalta315PI3K/AKT/mTOR pathwayAdaptor Proteins Signal TransducingChemistryMyogenesista1184Eukaryotic initiation factor 4E bindingSkeletal muscleRibosomal Protein S6 Kinases 70-kDaResistance TrainingPhosphoproteinsResistance exerciseCell biologymedicine.anatomical_structureEndocrinologyRibosomal protein s6Protein BiosynthesismTOR signalingPhosphorylationPyrazolesProtein synthesisProtein Processing Post-TranslationalPeptides
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The Leber congenital amaurosis protein AIPL1 and EB proteins co-localize at the photoreceptor cilium.

2014

Purpose The aim of this study was to investigate the interaction and co-localization of novel interacting proteins with the Leber congenital amaurosis (LCA) associated protein aryl hydrocarbon receptor interacting protein-like 1 (AIPL1). Methods The CytoTrapXR yeast two-hybrid system was used to screen a bovine retinal cDNA library. A novel interaction between AIPL1 and members of the family of EB proteins was confirmed by directed yeast two-hybrid analysis and co-immunoprecipitation assays. The localization of AIPL1 and the EB proteins in cultured cells and in retinal cryosections was examined by immunofluorescence microscopy and cryo-immunogold electron microscopy. Results Yeast two-hybri…

MiceLeber Congenital AmaurosisAnimalsHumansPhotoreceptor Cellsmacromolecular substancesCarrier ProteinsEye ProteinsMicrotubule-Associated ProteinsMicrotubulesCells CulturedAdaptor Proteins Signal TransducingResearch ArticlePloS one
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Flexible Structure of Peptide-Bound Filamin A Mechanosensor Domain Pair 20-21.

2015

Filamins (FLNs) are large, multidomain actin cross-linking proteins with diverse functions. Besides regulating the actin cytoskeleton, they serve as important links between the extracellular matrix and the cytoskeleton by binding cell surface receptors, functioning as scaffolds for signaling proteins, and binding several other cytoskeletal proteins that regulate cell adhesion dynamics. Structurally, FLNs are formed of an amino terminal actin-binding domain followed by 24 immunoglobulin-like domains (IgFLNs). Recent studies have demonstrated that myosin-mediated contractile forces can reveal hidden protein binding sites in the domain pairs IgFLNa18-19 and 20-21, enabling FLNs to transduce me…

Models MolecularDIMERIZATIONMagnetic Resonance SpectroscopyFilaminsProtein domainlcsh:MedicinePlasma protein bindingmacromolecular substancesBiologyMyosinsFilaminCrystallography X-RayLigandsfilaminsFORCEProtein structureAUTO-INHIBITIONBINDINGEscherichia coliCytoskeletonPHOSPHORYLATIONlcsh:ScienceCytoskeletonFRAGMENTMultidisciplinaryBinding Siteslcsh:Rta1182Signal transducing adaptor proteinfilamiinitSMALL-ANGLE SCATTERINGActin cytoskeletonActinsRecombinant ProteinsCell biologyProtein Structure TertiaryMODELBIOLOGICAL MACROMOLECULESCytoskeletal Proteinspeptiditpeptides1182 Biochemistry cell and molecular biologylcsh:QPeptidesINTEGRINBinding domainProtein BindingResearch ArticlePloS one
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Assembly of a Filamin Four-domain Fragment and the Influence of Splicing Variant-1 on the Structure

2011

Filamins are scaffold proteins that bind to various proteins, including the actin cytoskeleton, integrin adhesion receptors, and adaptor proteins such as migfilin. Alternative splicing of filamin, largely constructed from 24 Ig-like domains, is thought to have a role in regulating its interactions with other proteins. The filamin A splice variant-1 (FLNa var-1) lacks 41 amino acids, including the last β-strand of domain 19, FLNa(19), and the first β-strand of FLNa(20) that was previously shown to mask a key binding site on FLNa(21). Here, we present a structural characterization of domains 18-21, FLNa(18-21), in the FLNa var-1 as well as its nonspliced counterpart. A model of nonspliced FLN…

Models MolecularFilaminsProtein domainBiologyFilaminBiochemistryProtein Structure SecondaryStructure-Activity RelationshipContractile ProteinsProtein structureHumansFLNANuclear Magnetic Resonance BiomolecularMolecular BiologyMicrofilament ProteinsAlternative splicingta1182Signal transducing adaptor proteinCell BiologyActin cytoskeletonMolecular biologyProtein Structure TertiaryCell biologyAlternative SplicingProtein Structure and FoldingRNA splicingJournal of Biological Chemistry
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Structural basis of the migfilin-filamin interaction and competition with integrin beta tails.

2008

A link between sites of cell adhesion and the cytoskeleton is essential for regulation of cell shape, motility, and signaling. Migfilin is a recently identified adaptor protein that localizes at cell-cell and cell-extracellular matrix adhesion sites, where it is thought to provide a link to the cytoskeleton by interacting with the actin cross-linking protein filamin. Here we have used x-ray crystallography, NMR spectroscopy, and protein-protein interaction studies to investigate the molecular basis of migfilin binding to filamin. We report that the N-terminal portion of migfilin can bind all three human filamins (FLNa, -b, or -c) and that there are multiple migfilin-binding sites in FLNa. H…

Models MolecularIntegrin beta ChainsMagnetic Resonance SpectroscopyFilaminsIntegrinMolecular ConformationPlasma protein bindingmacromolecular substancesBiologyFilaminLigandsBiochemistryMiceContractile ProteinsFLNAAnimalsHumansCytoskeletonCell adhesionMolecular BiologyActinCytoskeletonDose-Response Relationship DrugMicrofilament ProteinsMechanisms of Signal TransductionSignal transducing adaptor proteinCell BiologyCell biologyCytoskeletal Proteinsbiology.proteinNIH 3T3 CellsCell Adhesion MoleculesProtein BindingThe Journal of biological chemistry
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Mona/Gads SH3C binding to hematopoietic progenitor kinase 1 (HPK1) combines an atypical SH3 binding motif, R/KXXK, with a classical PXXP motif embedd…

2004

Hematopoietic progenitor kinase 1 (HPK1) is implicated in signaling downstream of the T cell receptor. Its non-catalytic, C-terminal half contains several prolinerich motifs, which have been shown to interact with different SH3 domain-containing adaptor proteins in vitro. One of these, Mona/Gads, was also shown to bind HPK1 in mouse T cells in vivo. The region of HPK1 that binds to the Mona/Gads C-terminal SH3 domain has been mapped and shows only very limited similarity to a recently identified high affinity binding motif in SLP-76, another T-cell adaptor. Using isothermal titration calorimetry and x-ray crystallography, the binding of the HPK1 motif to Mona/Gads SH3C has now been characte…

Models MolecularTime FactorsProtein ConformationAmino Acid MotifsMolecular Sequence DataPlasma protein bindingBiologyCalorimetryProtein Serine-Threonine KinasesCrystallography X-RayBiochemistrySH3 domainProtein Structure Secondarysrc Homology DomainsMiceProtein structureAnimalsHumansAmino Acid SequenceMolecular BiologyPeptide sequencePolyproline helixAdaptor Proteins Signal TransducingSequence Homology Amino AcidSignal transducing adaptor proteinIsothermal titration calorimetryCell BiologyPhosphoproteinsCell biologyProtein Structure TertiaryCrystallographyKineticsPXXP MotifCarrier ProteinsPeptidesProtein BindingThe Journal of biological chemistry
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The genetic contribution of the NO system at the glutamatergic post-synapse to schizophrenia: Further evidence and meta-analysis

2013

NO is a pleiotropic signaling molecule and has an important role in cognition and emotion. In the brain, NO is produced by neuronal nitric oxide synthase (NOS-I, encoded by NOS1) coupled to the NMDA receptor via PDZ interactions; this protein-protein interaction is disrupted upon binding of NOS1 adapter protein (encoded by NOS1AP) to NOS-I. As both NOS1 and NOS1AP were associated with schizophrenia, we here investigated these genes in greater detail by genotyping new samples and conducting a meta-analysis of our own and published data. In doing so, we confirmed association of both genes with schizophrenia and found evidence for their interaction in increasing risk towards disease. Our stron…

NOS1Glutamic AcidNitric Oxide Synthase Type IPolymorphism Single NucleotidePrefrontal cortexNitric oxideAssociationSynapsechemistry.chemical_compoundGlutamatergicSDG 3 - Good Health and Well-beingmedicineAnimalsHumansGenetic Predisposition to DiseasePharmacology (medical)Promoter Regions GeneticPrefrontal cortexBiological PsychiatryAdaptor Proteins Signal TransducingPharmacologyGlutamate receptorComputational BiologyNitric oxideCognitionmedicine.diseasePsychiatry and Mental healthPost-synapseNeurologychemistrySchizophreniaSynapsesRC0321SchizophreniaNeurology (clinical)GlutamatePsychologyRC0321 Neuroscience. Biological psychiatry. NeuropsychiatryNeuroscienceSignal TransductionEuropean Neuropsychopharmacology
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