2016
Kv3.3 Channels Bind Hax-1 and Arp2/3 to Assemble a Stable Local Actin Network that Regulates Channel Gating
Zhang Y, Zhang XF, Fleming MR, Amiri A, El-Hassar L, Surguchev AA, Hyland C, Jenkins DP, Desai R, Brown MR, Gazula VR, Waters MF, Large CH, Horvath TL, Navaratnam D, Vaccarino FM, Forscher P, Kaczmarek LK. Kv3.3 Channels Bind Hax-1 and Arp2/3 to Assemble a Stable Local Actin Network that Regulates Channel Gating. Cell 2016, 165: 434-448. PMID: 26997484, PMCID: PMC4826296, DOI: 10.1016/j.cell.2016.02.009.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActin-Related Protein 2Actin-Related Protein 2-3 ComplexActin-Related Protein 3Adaptor Proteins, Signal TransducingAmino Acid SequenceCell MembraneMolecular Sequence DataMutationNeuronsPluripotent Stem CellsRac GTP-Binding ProteinsShaw Potassium ChannelsSignal TransductionSpinocerebellar AtaxiasConceptsCytoplasmic C-terminusProline-rich domainPlasma membraneHAX-1Actin nucleationC-terminusCortical actin filament networkLocal actin networkStem cell-derived neuronsActin filament networkCell-derived neuronsAnti-apoptotic proteinsActin cytoskeletonKv3.3 potassium channelActin assemblyActin structuresActin networkArp2/3Channel gatingFilament networkGrowth conesCerebellar neurodegenerationKv3.3TerminusPotassium channels
2013
Antibodies to cannabinoid type 1 receptor co‐react with stomatin‐like protein 2 in mouse brain mitochondria
Morozov YM, Dominguez MH, Varela L, Shanabrough M, Koch M, Horvath TL, Rakic P. Antibodies to cannabinoid type 1 receptor co‐react with stomatin‐like protein 2 in mouse brain mitochondria. European Journal Of Neuroscience 2013, 38: 2341-2348. PMID: 23617247, PMCID: PMC3902808, DOI: 10.1111/ejn.12237.Peer-Reviewed Original ResearchConceptsStomatin-like protein 2Type 1 receptorPresence of CB1Protein 2Anti-CB1 antibodySynthetic cannabinoid WINMouse brain mitochondriaCerebral cortexEndocannabinoid signalingBrain cellsCannabinoid WINNeuronal mitochondriaBrain mitochondriaAntibodiesMitochondrial functionCB1Polyclonal antibodiesCortexMitochondrial preparationsSerumReceptors
2004
CPG2 A brain- and synapse-specific protein that regulates the endocytosis of glutamate receptors
Cottrell JR, Borok E, Horvath TL, Nedivi E. CPG2 A brain- and synapse-specific protein that regulates the endocytosis of glutamate receptors. Neuron 2004, 44: 677-690. PMID: 15541315, PMCID: PMC3065105, DOI: 10.1016/j.neuron.2004.10.025.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceBlotting, NorthernBlotting, WesternBrainCells, CulturedClathrin-Coated VesiclesEndocytosisHumansIn Situ HybridizationMicroscopy, ElectronMolecular Sequence DataNerve Tissue ProteinsNeuronal PlasticityNeuronsReceptors, AMPAReceptors, GlutamateReceptors, N-Methyl-D-AspartateReverse Transcriptase Polymerase Chain ReactionSynapsesConceptsGlutamate receptorsClathrin-coated vesiclesBrain-specific splice variantSynapse-specific proteinsExcitatory synapsesReceptor endocytosisSYNE-1 geneConstitutive internalizationEndocytic mechanismsSynaptic AMPA receptorsDendritic spine sizeMembrane transportSplice variantsSynaptic proteinsNMDA receptorsAMPA receptorsProteinPostsynaptic plasticityNeurotransmitter receptorsEndocytosisSynaptic strengthLong-term maintenanceReceptorsSpine sizeInternalization
2003
Mitochondrial Uncoupling Proteins: Regulators of Retinal Cell Death
Barnstable CJ, Li M, Reddy R, Horvath TL. Mitochondrial Uncoupling Proteins: Regulators of Retinal Cell Death. Advances In Experimental Medicine And Biology 2003, 533: 269-275. PMID: 15180273, DOI: 10.1007/978-1-4615-0067-4_33.Peer-Reviewed Original ResearchConceptsOxidative stressElevated levelsOptic nerve disordersGanglion cell deathCell deathRetinal cell deathSuch elevated levelsNerve disordersInner retinaNeuronal degenerationReactive oxygen radicalsMetabolic conditionsNeural componentsApoptotic cell deathOxygen radicalsIntracellular metabolismDeathSpecific mutationsCell typesExtensive evidenceIrreversible cascadeGlaucomaDegenerationRetinaGhrelin as a potential anti-obesity target.
Horvath TL, Castañeda T, Tang-Christensen M, Pagotto U, Tschöp MH. Ghrelin as a potential anti-obesity target. Current Pharmaceutical Design 2003, 9: 1383-95. PMID: 12769730, DOI: 10.2174/1381612033454748.Peer-Reviewed Original ResearchConceptsPositive energy balancePotential anti-obesity targetEndogenous growth hormone secretagogueEffective pharmacological treatmentAnti-obesity targetGrowth hormone secretagoguesNumerous target tissuesPeptide hormone ghrelinGhrelin antagonistGhrelin actionPharmacological treatmentHormone ghrelinFood intakeHormone secretagoguesPharmacological approachesGhrelinPleiotropic hormoneFat oxidationNeuroendocrine regulationCompensatory mechanismsEnergy homeostasisBlood streamTarget tissuesExact mechanismObesity