Search results for "Z domain"

showing 10 items of 37 documents

NG2-expressing cells in the nervous system: role of the proteoglycan in migration and glial–neuron interaction

2005

The NG2 glycoprotein is a type I membrane protein expressed in the developing and adult central nervous system (CNS) by subpopulations of glia including oligodendroglial precursor cells (OPCs), and in the developing CNS additionally by pericytes. In the mouse CNS, expression of NG2 protein is already observed at embryonic day 13 and peaks between postnatal days 8 and 12. NG2+ cells persist in grey and white matter in adult mouse brain: cells in the developing and adult brain show clear differences in migration, cell-cycle length and lineage restriction. Several groups have provided evidence that subpopulations of NG2+ cells can generate neurons in vivo. Neuronal stimulation in the developin…

Nervous systemHistologyPDZ domainNeurexinAMPA receptorReviewCell CommunicationBiologyCell MovementmedicineCell AdhesionAnimalsHumansAntigensMolecular BiologyEcology Evolution Behavior and SystematicsNeuronsNG2 proteoglycanStem CellsGlutamate receptorBrainCell BiologyCell biologyOligodendrogliamedicine.anatomical_structurenervous systemImmunologyProteoglycansNeuronAnatomyNeurogliaDevelopmental BiologyAstrocyte
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NG2 cells: Properties, progeny and origin

2010

The NG2 proteoglycan is a type 1-transmembrane protein expressed by a range of cell types within and outside the mammalian nervous system. NG2-expressing (NG2) cells are found in grey and white matter tracts of the developing and adult CNS and have previously been assumed to represent oligodendrocyte precursor cells: new work using transgenic mice has shown that NG2 cells generate oligodendrocytes, protoplasmic astrocytes and in some instances neurons in vivo. NG2 cells express GABAA receptors and the AMPA subtype of glutamate receptors. They make intimate contact to neurons prior to myelinating axons and also form electron-dense synaptic specialisations with axons in the cerebellum, cortex…

NeuronsCerebellumCell typeStem CellsGeneral NeuroscienceModels NeurologicalPDZ domainGlutamate receptorAMPA receptorBiologyArticlemedicine.anatomical_structurenervous systemSynapsesmedicineAnimalsHumansProteoglycansNeurology (clinical)AntigensReceptorLong-term depressionNeurogliaNeuroscienceIon channel linked receptorsBrain Research Reviews
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Lipschitz continuity of Cheeger-harmonic functions in metric measure spaces

2003

Abstract We use the heat equation to establish the Lipschitz continuity of Cheeger-harmonic functions in certain metric spaces. The metric spaces under consideration are those that are endowed with a doubling measure supporting a (1,2)-Poincare inequality and in addition supporting a corresponding Sobolev–Poincare-type inequality for the modification of the measure obtained via the heat kernel. Examples are given to illustrate the necessity of our assumptions on these spaces. We also provide an example to show that in the general setting the best possible regularity for the Cheeger-harmonic functions is Lipschitz continuity.

Pure mathematicsMathematical analysisLipschitz continuityModulus of continuityCheeger-harmonicConvex metric spaceUniform continuityMetric spaceLipschitz domainPoincaré inequalityheat kerneldoubling measureMetric mapLipschitz regularitylogarithmic Sobolev inequalityMetric differentialhypercontractivityAnalysisNewtonian spaceMathematicsJournal of Functional Analysis
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Weighted Hardy inequalities beyond Lipschitz domains

2014

It is a well-known fact that in a Lipschitz domain \Omega\subset R^n a p-Hardy inequality, with weight d(x,\partial\Omega)^\beta, holds for all u\in C_0^\infty(\Omega) whenever \beta<p-1. We show that actually the same is true under the sole assumption that the boundary of the domain satisfies a uniform density condition with the exponent \lambda=n-1. Corresponding results also hold for smaller exponents, and, in fact, our methods work in general metric spaces satisfying standard structural assumptions.

Pure mathematicsMathematics::Functional AnalysisHausdorff-sisältöApplied MathematicsGeneral Mathematicsmetric spaceBoundary (topology)LambdaLipschitz continuityOmega46E35 26D15Domain (mathematical analysis)Functional Analysis (math.FA)Mathematics - Functional AnalysisMetric spacemetrinen avaruusHardyn epäyhtälöuniform fatnessLipschitz domainHardy inequalityHausdorff contenttasainen paksuusExponentFOS: MathematicsMathematics
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Relaxation of Quasilinear Elliptic SystemsviaA-quasiconvex Envelopes

2002

We consider the weak closure WZof the set Z of all feasible pairs (solution, flow) of the family of potential elliptic systems div s0 s=1 s(x)F 0 s(ru(x )+ g(x)) f(x) =0i n; u =( u1;:::;um)2 H 1 0 (; R m ) ; =( 1;:::;s 0 )2 S; where R n is a bounded Lipschitz domain, Fs are strictly convex smooth functions with quadratic growth and S =f measurable j s(x )=0o r 1 ;s =1 ;:::;s0 ;1(x )+ +s0 (x )=1 g .W e show that WZis the zero level set for an integral functional with the integrand QF being the A-quasiconvex envelope for a certain functionF and the operator A = (curl,div) m . If the functions Fs are isotropic, then on the characteristic cone (dened by the operator A) QF coincides with the A-p…

Quadratic growthCurl (mathematics)Pure mathematicsControl and OptimizationElliptic systemsIsotropyMathematical analysisComputational MathematicsQuasiconvex functionLipschitz domainControl and Systems EngineeringBounded functionConvex functionMathematicsESAIM: Control, Optimisation and Calculus of Variations
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The Proteoglycan NG2 Is Complexed with α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors by the PDZ Glutamate Receptor Interactio…

2003

The proteoglycan NG2 is expressed by immature glial cells in the developing and adult central nervous system. Using the COOH-terminal region of NG2 as bait in a yeast two-hybrid screen, we identified the glutamate receptor interaction protein GRIP1, a multi-PDZ domain protein, as an interacting partner. NG2 exhibits a PDZ binding motif at the extreme COOH terminus which binds to the seventh PDZ domain of GRIP1. In addition to the published expression in neurons, GRIP1 is expressed by immature glial cells. GRIP1 is known to bind to the GluRB subunit of the AMPA glutamate receptor expressed by subpopulations of neurons and immature glial cells. In cultures of primary oligodendrocytes, cells c…

Receptor complexbiologyProtein subunitPDZ domainProtein domainGlutamate receptorCell BiologyAMPA receptorTransfectionBiochemistryMolecular biologynervous systemProteoglycanbiology.proteinMolecular BiologyJournal of Biological Chemistry
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Zasp/Cypher internal ZM-motif containing fragments are sufficient to co-localize with α-actinin—Analysis of patient mutations

2005

Z-band alternatively spliced PDZ-containing protein (ZASP/Cypher) has an important role in maintaining Z-disc stability in striated and cardiac muscle. ZASP/Cypher interacts through its PDZ domain with the major Z-disc actin cross-linker, alpha-actinin. ZASP/Cypher also has a conserved sequence called the ZM-motif, and it is found in two alternatively spliced exons 4 and 6. We have shown earlier that the ZM-motif containing internal regions of two related proteins ALP and CLP36 interact with alpha-actinin rod region, and that the ZM-motif is important in targeting ALP to the alpha-actinin containing structures in cell. Here, we show that the ZASP/Cypher internal fragments containing either …

SarcomeresAmino Acid MotifsPDZ domainCHO Cellsmacromolecular substancesBiologyConserved sequenceStress fiber assemblyMyoblastsMiceExonCricetinaeStress FibersmedicineAnimalsHumansMyocyteActininMuscle SkeletalActinAdaptor Proteins Signal TransducingOrganellesGeneticsMyocardiumPoint mutationCardiac muscleExonsIntracellular MembranesCell BiologyLIM Domain Proteinsmusculoskeletal systemPeptide FragmentsCell biologymedicine.anatomical_structureMutationCardiomyopathiesProtein BindingExperimental Cell Research
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Gene-based treatment options for Usher type 1C by translational read-through of a nonsense mutation

2012

The Usher syndrome (USH) is the most frequent cause of inherited combined deaf-blindness. The ciliopathy is clinically and genetically heterogeneous, assigned to three clinical USH types of which the most severe type is USH1. The USH1C gene encodes the PDZ containing scaffold protein harmonin which is expressed in form of numerous alternatively spliced variants. Hamonin binds directly to all USH1/2 proteins and is a key organizer of USH protein networks in photoreceptor cells. So far no effective treatment for the ophthalmic component of USH exists. Translational read-through was introduced as an innovative therapy option for several non-ocular diseases caused by nonsense mutations leading …

Scaffold proteinGeneticslcsh:CytologyUsher syndromePDZ domainNonsense mutationCell BiologyBiologymedicine.diseaseCiliopathiesPhotoreceptor cellCell biologyCiliopathymedicine.anatomical_structureotorhinolaryngologic diseasesmedicineOral Presentationlcsh:QH573-671GeneCilia
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Molecular basis of human Usher syndrome: deciphering the meshes of the Usher protein network provides insights into the pathomechanisms of the Usher …

2006

Usher syndrome (USH) is the most frequent cause of combined deaf-blindness in man. It is clinically and genetically heterogeneous and at least 12 chromosomal loci are assigned to three clinical USH types, namely USH1A-G, USH2A-C, USH3A (Davenport, S.L.H., Omenn, G.S., 1977. The heterogeneity of Usher syndrome. Vth Int. Conf. Birth Defects, Montreal; Petit, C., 2001. Usher syndrome: from genetics to pathogenesis. Annu. Rev. Genomics Hum. Genet. 2, 271-297). Mutations in USH type 1 genes cause the most severe form of USH. In USH1 patients, congenital deafness is combined with a pre-pubertal onset of retinitis pigmentosa (RP) and severe vestibular dysfunctions. Those with USH2 have moderate to…

Scaffold proteinModels MolecularUsher syndromePDZ domainProtocadherinCadherin Related ProteinsCell Cycle ProteinsNerve Tissue ProteinsBiologyDeafnessMyosinsCellular and Molecular NeuroscienceRetinitis pigmentosaotorhinolaryngologic diseasesmedicineAnimalsHumansAdaptor Proteins Signal TransducingGeneticsExtracellular Matrix ProteinsModels GeneticCadherinRetinal DegenerationSignal transducing adaptor proteinDyneinsMembrane Proteinsmedicine.diseaseCadherinsSensory SystemsOphthalmologyCytoskeletal ProteinsDisease Models AnimalMembrane proteinMyosin VIIaMutationMicrotubule ProteinsVestibule LabyrinthUsher SyndromesExperimental eye research
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The GRIP1/14-3-3 Pathway Coordinates Cargo Trafficking and Dendrite Development

2014

SummaryRegulation of cargo transport via adaptor molecules is essential for neuronal development. However, the role of PDZ scaffolding proteins as adaptors in neuronal cargo trafficking is still poorly understood. Here, we show by genetic deletion in mice that the multi-PDZ domain scaffolding protein glutamate receptor interacting protein 1 (GRIP1) is required for dendrite development. We identify an interaction between GRIP1 and 14-3-3 proteins that is essential for the function of GRIP1 as an adaptor protein in dendritic cargo transport. Mechanistically, 14-3-3 binds to the kinesin-1 binding region in GRIP1 in a phospho-dependent manner and detaches GRIP1 from the kinesin-1 motor protein …

Scaffold proteinPDZ domainKinesinsNerve Tissue ProteinsDendriteBiologyGeneral Biochemistry Genetics and Molecular BiologyMotor proteinGene Knockout TechniquesMiceMicrotubulemedicineAnimalsMolecular BiologyAdaptor Proteins Signal TransducingPoint mutationSignal transducing adaptor proteinDendritesCell BiologyCell biologyProtein Transportmedicine.anatomical_structure14-3-3 ProteinsMutationCarrier ProteinsFunction (biology)Protein BindingSignal TransductionTranscription FactorsDevelopmental BiologyDevelopmental Cell
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