Search results for "PDZ domain"

showing 10 items of 23 documents

PTEN recruitment controls synaptic and cognitive function in Alzheimer's models

2016

Dyshomeostasis of amyloid-β peptide (Aβ) is responsible for synaptic malfunctions leading to cognitive deficits ranging from mild impairment to full-blown dementia in Alzheimer's disease. Aβ appears to skew synaptic plasticity events toward depression. We found that inhibition of PTEN, a lipid phosphatase that is essential to long-term depression, rescued normal synaptic function and cognition in cellular and animal models of Alzheimer's disease. Conversely, transgenic mice that overexpressed PTEN displayed synaptic depression that mimicked and occluded Aβ-induced depression. Mechanistically, Aβ triggers a PDZ-dependent recruitment of PTEN into the postsynaptic compartment. Using a PTEN kno…

0301 basic medicinePrimary Cell CulturePDZ DomainsMice TransgenicMolecular neuroscienceBiologyNeurotransmissionSynaptic TransmissionMice03 medical and health sciences0302 clinical medicineAlzheimer DiseasePostsynaptic potentialmedicineAnimalsPTENGene Knock-In TechniquesAmyloid beta-PeptidesGeneral NeurosciencePTEN PhosphohydrolaseLong-term potentiationmedicine.diseaseRatsDisease Models Animal030104 developmental biologySynaptic fatigueSynaptic plasticitybiology.proteinAlzheimer's diseaseCognition DisordersNeuroscience030217 neurology & neurosurgeryNature Neuroscience
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The CFTR associated protein CAP70 interacts with the apical Cl-/HCO3- exchanger DRA in rabbit small intestinal mucosa.

2005

DRA (down regulated in adenoma) is an intestinal anion exchanger, acting in parallel with NHE3 to facilitate ileal and colonic NaCl absorption. Furthermore it is involved in small intestinal bicarbonate secretion. Because DRA has a PDZ interaction motif, which may influence its properties, we searched for DRA-interacting PDZ adapter proteins in the small intestine. Using an overlay assay with the recombinant DRA C-terminus as a ligand, a 70 kDa protein was labeled, which was restricted to the brush border membrane in rabbit duodenal and ileal mucosa and was not detected in the colon. Destruction of the C-terminal PDZ interaction motif abolished this band, suggesting a specific protein-prote…

Brush borderColonPDZ domainAmino Acid MotifsMolecular Sequence DataCystic Fibrosis Transmembrane Conductance RegulatorIleumBiologyBiochemistryAntiportersCell LineIntestine SmallmedicineAnimalsHumansSecretionAmino Acid SequenceChloride-Bicarbonate AntiportersRNA MessengerIntestinal MucosaMessenger RNAHEK 293 cellsSignal transducing adaptor proteinMembrane ProteinsMolecular biologySmall intestinePeptide Fragmentsmedicine.anatomical_structureSulfate TransportersRabbitsCarrier ProteinsBiochemistry
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The Functional Role of the Second NPXY Motif of the LRP1 β-Chain in Tissue-type Plasminogen Activator-mediated Activation of N-Methyl-D-aspartate Rec…

2008

The low density lipoprotein receptor-related protein 1 (LRP1) emerges to play fundamental roles in cellular signaling pathways in the brain. One of its prominent ligands is the serine proteinase tissue-type plasminogen activator (tPA), which has been shown to act as a key activator of neuronal mitogen-activated protein kinase pathways via the N-methyl-D-aspartate (NMDA) receptor. However, here we set out to examine whether LRP1 and the NMDA receptor might eventually act in a combined fashion to mediate tPA downstream signaling. By blocking tPA from binding to LRP1 using the receptor-associated protein, we were able to completely inhibit NMDA receptor activation. Additionally, inhibition of …

Cell signalingAmino Acid MotifsPDZ domainIntracellular SpaceBiologyReceptors N-Methyl-D-AspartateBiochemistryProtein Structure SecondaryCell LineRats Sprague-DawleyMiceStructure-Activity RelationshipAnimalsHumansAmino Acid SequencePhosphorylationRNA Small InterferingReceptorProtein kinase AMolecular BiologyMitogen-Activated Protein Kinase 1NeuronsMitogen-Activated Protein Kinase 3Activator (genetics)Intracellular Signaling Peptides and ProteinsMembrane ProteinsReceptor Cross-TalkCell BiologyLRP1RatsCell biologyEnzyme ActivationBiochemistryTissue Plasminogen ActivatorDisks Large Homolog 4 ProteinCalciumDisks Large Homolog 4 ProteinGuanylate KinasesPlasminogen activatorLow Density Lipoprotein Receptor-Related Protein-1PlasmidsSignal TransductionJournal of Biological Chemistry
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NG2-positive cells in CNS function and the pathological role of antibodies against NG2 in demyelinating diseases

2005

NG2 is expressed by a variety of immature glia in the CNS including oligodendrocyte progenitor cells, paranodal astrocytes and perisynaptic glia. The protein has a large extracellular domain with two LNS/Lam G domains at the N-terminus and a short intracellular tail with a PDZ-recognition domain at the C-terminus. Experiments suggest that the protein plays a role in migration. The PDZ protein GRIP was identified as an intracellular binding partner of NG2 in immature glial cells. A complex is formed between GRIP, NG2 and the AMPA class of glutamate receptors: this may position these glial receptors towards sites of neuronal glutamate release at synapses and during myelination. Identification…

Central Nervous SystemCentral nervous systemPDZ domainGlutamate receptorAMPA receptorBiologyModels BiologicalAntibodiesOligodendrocytemedicine.anatomical_structurenervous systemNeurologySynapsesmedicineAnimalsHumansNeurogliaProteoglycansNeurology (clinical)AntigensRemyelinationReceptorNeurogliaNeuroscienceDemyelinating DiseasesJournal of the Neurological Sciences
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The evolutionary history and tissue mapping of GPR123: specific CNS expression pattern predominantly in thalamic nuclei and regions containing large …

2007

The Adhesion family of G protein-coupled receptors (GPCRs) includes 33 receptors and is the second largest GPCR family. Most of these proteins are still orphans and fairly little is known of their tissue distribution and evolutionary context. We report the evolutionary history of the Adhesion family protein GPR123 as well as mapping of GPR123 mRNA expression in mouse and rat using in situ hybridization and real-time PCR, respectively. GPR123 was found to be well conserved within the vertebrate lineage, especially within the transmembrane regions and in the distal part of the cytoplasmic tail, containing a potential PDZ binding domain. The real-time PCR data indicates that GPR123 is predomin…

Central Nervous SystemMaleModels MolecularNeuronal signal transductionPDZ domainGene ExpressionContext (language use)In situ hybridizationBiologyBiochemistryReceptors G-Protein-CoupledMiceCellular and Molecular NeuroscienceAnimalsHumansTissue DistributionRNA MessengerNeural Cell Adhesion MoleculesIn Situ HybridizationPhylogenyG protein-coupled receptorReverse Transcriptase Polymerase Chain ReactionPyramidal CellsSubiculumRatsCell biologySignal transductionSequence AlignmentNeuroscienceBinding domainJournal of Neurochemistry
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Characterization of the interaction between Actinin-Associated LIM Protein (ALP) and the rod domain of α-actinin

2009

Abstract Background The PDZ-LIM proteins are a family of signalling adaptors that interact with the actin cross-linking protein, α-actinin, via their PDZ domains or via internal regions between the PDZ and LIM domains. Three of the PDZ-LIM proteins have a conserved 26-residue ZM motif in the internal region, but the structure of the internal region is unknown. Results In this study, using circular dichroism and nuclear magnetic resonance (NMR), we showed that the ALP internal region (residues 107–273) was largely unfolded in solution, but was able to interact with the α-actinin rod domain in vitro, and to co-localize with α-actinin on stress fibres in vivo. NMR analysis revealed that the ti…

Circular dichroismPDZ domaineducationAmino Acid MotifsMolecular Sequence DataPlasma protein bindingActininmacromolecular substancesBiology03 medical and health sciences0302 clinical medicineCell Line TumorHumansActininAmino Acid Sequencelcsh:QH573-671Peptide sequenceActin030304 developmental biologyLIM domainFluorescent Dyes0303 health scienceslcsh:CytologyMicrofilament ProteinsCell BiologyLIM Domain ProteinsSurface Plasmon Resonancemusculoskeletal systemRecombinant ProteinsCell biologyProtein Structure TertiaryLHX3Peptides030217 neurology & neurosurgeryResearch ArticleProtein BindingBMC Cell Biology
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Mpdz is a quantitative trait gene for drug withdrawal seizures

2004

Physiological dependence and associated withdrawal episodes can constitute a powerful motivational force that perpetuates drug use and abuse. Using robust behavioral models of drug physiological dependence in mice, positional cloning, and sequence and expression analyses, we identified an addiction-relevant quantitative trait gene, Mpdz. Our findings provide a framework to define the protein interactions and neural circuit by which this gene's product (multiple PDZ domain protein) affects drug dependence, withdrawal and relapse.

DrugGenotypePositional cloningmedia_common.quotation_subjectMolecular Sequence DataQuantitative Trait LociPDZ domainGene ExpressionQuantitative trait locusBiologyProtein–protein interactionMiceMice CongenicDrug withdrawalSeizuresmedicineAnimalsGenetic Predisposition to DiseaseCloning MolecularGenemedia_commonGeneticsBehavior AnimalEthanolGeneral NeuroscienceChromosome MappingMembrane ProteinsEmbryo Mammalianmedicine.diseaseSubstance Withdrawal SyndromeMice Inbred C57BLCarrier ProteinsNeuroscienceNature Neuroscience
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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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Molecular Analysis of the Supramolecular Usher Protein Complex in the Retina

2007

Human Usher syndrome (USH) is the most common form of deaf-blindness and also the most frequent case of recessive retinitis pigmentosa. According to the degree of the clinical symptoms, three different types of the Usher syndrome are distinguished: USH1, USH2 and USH3 (Davenport and Omenn, 1977). USH is genetically heterogeneous with eleven chromosomal loci, which can be assigned to the three USH types (USH1A-G, USH2A-C, USH3A) (Petit, 2001). Out of these, USH1 is the most severe form, characterized by profound congenital deafness, constant vestibular dysfunction and prepubertal-onset retinitis pigmentosa. USH2 patients show a milder congenital deafness, a slightly later onset of retinitis …

GeneticsScaffold proteinGenetic heterogeneityHearing lossUsher syndromePDZ domainLate onsetBiologymedicine.diseasePhenotypeRetinitis pigmentosaotorhinolaryngologic diseasesmedicinemedicine.symptom
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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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