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
N-Glycosylation at the SynCAM (Synaptic Cell Adhesion Molecule) Immunoglobulin Interface Modulates Synaptic Adhesion*
Fogel AI, Li Y, Giza J, Wang Q, Lam TT, Modis Y, Biederer T. N-Glycosylation at the SynCAM (Synaptic Cell Adhesion Molecule) Immunoglobulin Interface Modulates Synaptic Adhesion*. Journal Of Biological Chemistry 2010, 285: 34864-34874. PMID: 20739279, PMCID: PMC2966101, DOI: 10.1074/jbc.m110.120865.Peer-Reviewed Original ResearchConceptsN-glycosylationTrans-synaptic interactionsN-glycansSite-specific N-glycansSynaptic cell adhesion molecule 1Site-specific N-glycosylationTrans-synaptic adhesionPost-translational modificationsSelect adhesion moleculesMutational studiesSynaptic adhesionGlycosylation sitesHeterophilic interactionsIg1 domainSynapse inductionPostsynaptic membraneAdhesion moleculesNeurobiological questionsSynaptic cleftStructural modelingPresynaptic terminalsDifferential mannerSialic acidCell adhesion molecule-1Adhesion
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