2023
The human milk component myo-inositol promotes neuronal connectivity
Paquette A, Carbone B, Vogel S, Israel E, Maria S, Patil N, Sah S, Chowdhury D, Kondratiuk I, Labhart B, Morrow A, Phillips S, Kuang C, Hondmann D, Pandey N, Biederer T. The human milk component myo-inositol promotes neuronal connectivity. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2221413120. PMID: 37433002, PMCID: PMC10374161, DOI: 10.1073/pnas.2221413120.Peer-Reviewed Original ResearchConceptsHuman milkNeuronal connectionsInfant brainBreast milk componentsExcitatory synapse densityCultured rat neuronsMature brain tissueHuman milk samplesAbility of neuronsHuman excitatory neuronsDose-dependent mannerExcitatory postsynaptic sitesSlice culture systemSynapse densityExcitatory neuronsDietary supplementationPostsynaptic sitesRat neuronsNeuronal connectivityOrganotypic slicesBrain tissuePostsynaptic specializationsOrganotypic slice culture systemBrain developmentBrain connectivity
2019
Synaptic Connectivity and Cortical Maturation Are Promoted by the ω-3 Fatty Acid Docosahexaenoic Acid
Carbone BE, Abouleish M, Watters KE, Vogel S, Ribic A, Schroeder OH, Bader BM, Biederer T. Synaptic Connectivity and Cortical Maturation Are Promoted by the ω-3 Fatty Acid Docosahexaenoic Acid. Cerebral Cortex 2019, 30: 226-240. PMID: 31034037, DOI: 10.1093/cercor/bhz083.Peer-Reviewed Original ResearchConceptsVisual acuityDietary DHASynaptic connectivityFatty Acid Docosahexaenoic AcidVivo electrophysiological recordingsSize of synapsesEarly neuronal differentiationDose-dependent mannerFatty acid DHACortical maturationYoung miceAwake miceDendritic arborsCultured neuronsDHA's roleVisual cortexFunctional maturationPostsynaptic specializationsElectrophysiological recordingsCortical processingBrain developmentDocosahexaenoic acidAcid DHAPostnatal stagesNeuronal differentiation
2015
Topographic Mapping of the Synaptic Cleft into Adhesive Nanodomains
de Arce K, Schrod N, Metzbower SWR, Allgeyer E, Kong G, Tang AH, Krupp AJ, Stein V, Liu X, Bewersdorf J, Blanpied TA, Lucić V, Biederer T. Topographic Mapping of the Synaptic Cleft into Adhesive Nanodomains. Neuron 2015, 88: 1165-1172. PMID: 26687224, PMCID: PMC4687029, DOI: 10.1016/j.neuron.2015.11.011.Peer-Reviewed Original ResearchConceptsSynaptic cell adhesion molecule 1Trans-synaptic complexesEphB2 receptor tyrosine kinaseReceptor tyrosine kinasesCryo-ETSynaptic cleftCryoelectron tomographyTyrosine kinaseMolecular insightsSynCAM 1Macromolecular organizationImmunoglobulin proteinCell adhesion molecule-1Immunoelectron microscopyAdhesion molecule-1Super-resolution imagingPostsynaptic densityDistinct density profilesDepression paradigmExcitatory synapsesPostsynaptic areaMolecule-1Cleft edgesSynapsesCleft
2014
Activity-Dependent Regulation of Dendritic Complexity by Semaphorin 3A through Farp1
Cheadle L, Biederer T. Activity-Dependent Regulation of Dendritic Complexity by Semaphorin 3A through Farp1. Journal Of Neuroscience 2014, 34: 7999-8009. PMID: 24899721, PMCID: PMC4044256, DOI: 10.1523/jneurosci.3950-13.2014.Peer-Reviewed Original ResearchConceptsDendritic complexityTotal dendritic branch lengthActivity-dependent regulationDendritic shaftsDendritic arborizationDendritic arborsHippocampal neuronsSynaptic inputsNeuronal activityRat neuronsSemaphorin 3ANeuronal structuresSema3ADendrite differentiationNeuronsRac1 activatorDendritic morphologyComplex neuronal structuresPlexinA1Soluble cuesSignaling proteinsArborizationFARP1Coreceptor
2012
The novel synaptogenic protein Farp1 links postsynaptic cytoskeletal dynamics and transsynaptic organization
Cheadle L, Biederer T. The novel synaptogenic protein Farp1 links postsynaptic cytoskeletal dynamics and transsynaptic organization. Journal Of Cell Biology 2012, 199: 985-1001. PMID: 23209303, PMCID: PMC3518221, DOI: 10.1083/jcb.201205041.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsCell Adhesion Molecule-1Cell Adhesion MoleculesCytoskeletal ProteinsCytoskeletonDendritic SpinesGuanine Nucleotide Exchange FactorsHEK293 CellsHippocampusHumansImmunoglobulinsMiceMice, KnockoutNeurogenesisNeuronsNeuropeptidesProtein BindingProtein Structure, TertiaryProteomicsRac GTP-Binding ProteinsRac1 GTP-Binding ProteinRho Guanine Nucleotide Exchange FactorsSignal TransductionSynapsesConceptsSynCAM 1Synapse developmentF-actin assemblyCytoskeletal dynamicsGTPase Rac1Retrograde signalsSynaptic adhesionFARP1Transsynaptic interactionsFilopodial dynamicsProtein 1Synapse formationSynaptic complexImmature neuronsSpine densitySpine morphologySynapse numberPathwayKnockout miceSynaptic membranesPleckstrinFERMRac1
2010
SynCAM 1 participates in axo-dendritic contact assembly and shapes neuronal growth cones
Stagi M, Fogel AI, Biederer T. SynCAM 1 participates in axo-dendritic contact assembly and shapes neuronal growth cones. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 107: 7568-7573. PMID: 20368431, PMCID: PMC2867738, DOI: 10.1073/pnas.0911798107.Peer-Reviewed Original Research
2007
Mixed-culture assays for analyzing neuronal synapse formation
Biederer T, Scheiffele P. Mixed-culture assays for analyzing neuronal synapse formation. Nature Protocols 2007, 2: 670-676. PMID: 17406629, DOI: 10.1038/nprot.2007.92.Peer-Reviewed Original ResearchConceptsVertebrate central nervous systemIndividual cell surface proteinsSynaptic adhesion complexesCell biological mechanismsPostsynaptic membrane domainsCell surface proteinsAssembly of synapsesAdhesion complexesMembrane domainsNeuronal synapse formationIndividual proteinsSynaptogenic activityGenetic studiesBidirectional signalingPrimary neuronal culturesSynapse formationSynaptic differentiationMixed culture assayBiological mechanismsSynaptic structureProteinNew insightsSynaptic cleftNeuronal culturesAssay system
2002
SynCAM, a Synaptic Adhesion Molecule That Drives Synapse Assembly
Biederer T, Sara Y, Mozhayeva M, Atasoy D, Liu X, Kavalali ET, Südhof T. SynCAM, a Synaptic Adhesion Molecule That Drives Synapse Assembly. Science 2002, 297: 1525-1531. PMID: 12202822, DOI: 10.1126/science.1072356.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBrainBrain ChemistryCell Adhesion MoleculesCell Adhesion Molecules, NeuronalCell LineCoculture TechniquesExocytosisHumansImmunoglobulinsMolecular Sequence DataNeuronsProsencephalonProtein Structure, TertiaryRatsReceptors, AMPARecombinant Fusion ProteinsSequence Homology, Amino AcidSynapsesSynaptic TransmissionTransfectionTumor Suppressor ProteinsConceptsSynapse assemblyHomophilic cell adhesion moleculeDomain-containing proteinsPDZ domain proteinsNonneuronal cellsAdhesion moleculesSynaptic adhesion moleculesImmunoglobulin domain-containing proteinsGlutamate receptorsCoordinated assemblyCytoplasmic tailCell adhesion moleculeGlutamatergic synaptic transmissionSynapse formationPostsynaptic specializationsPostsynaptic responsesHippocampal neuronsSynaptic transmissionProteinNerve cellsAssemblyCellsExpressionTight attachmentNeurons