2024
A complex of the lipid transport ER proteins TMEM24 and C2CD2 with band 4.1 at cell–cell contacts
Johnson B, Iuliano M, Lam T, Biederer T, De Camilli P. A complex of the lipid transport ER proteins TMEM24 and C2CD2 with band 4.1 at cell–cell contacts. Journal Of Cell Biology 2024, 223: e202311137. PMID: 39158698, PMCID: PMC11334333, DOI: 10.1083/jcb.202311137.Peer-Reviewed Original ResearchConceptsPlasma membraneNon-vesicular lipid transferSites of cell contactC-terminus motifsCell contact-dependent signalsContact-dependent signalingCell-cell contactER/PM junctionsTMEM24ER proteinsPM proteinsSynCAM 1Cell adhesion moleculesCellular functionsLipid transferC2CD2Phospholipid transportLipid transportCell contactProteinAdhesion moleculesCalcium homeostasisCellsFamily membersParalogs
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
2021
Synaptic recognition molecules in development and disease
Chowdhury D, Watters K, Biederer T. Synaptic recognition molecules in development and disease. Current Topics In Developmental Biology 2021, 142: 319-370. PMID: 33706921, PMCID: PMC8632550, DOI: 10.1016/bs.ctdb.2020.12.009.ChaptersConceptsSingle-cell expression studiesRecognition moleculesRecognition factorsKey protein familiesPost-translational modificationsLeucine-rich repeatsCell expression studiesSemaphorin/PlexinAlternative splicingProtein familyProteomic approachCombinatorial actionMolecular playersPartner recognitionExpression studiesMolecular themesSpecific expressionDisease relevanceSynapse specificationVertebrate brainImmunoglobulin SuperfamilyRich repertoireAppropriate brain regionsNeuron type-specific expressionSynaptic wiring
2019
SynGO: An Evidence-Based, Expert-Curated Knowledge Base for the Synapse
Koopmans F, van Nierop P, Andres-Alonso M, Byrnes A, Cijsouw T, Coba M, Cornelisse L, Farrell R, Goldschmidt H, Howrigan D, Hussain N, Imig C, de Jong A, Jung H, Kohansalnodehi M, Kramarz B, Lipstein N, Lovering R, MacGillavry H, Mariano V, Mi H, Ninov M, Osumi-Sutherland D, Pielot R, Smalla K, Tang H, Tashman K, Toonen R, Verpelli C, Reig-Viader R, Watanabe K, van Weering J, Achsel T, Ashrafi G, Asi N, Brown T, De Camilli P, Feuermann M, Foulger R, Gaudet P, Joglekar A, Kanellopoulos A, Malenka R, Nicoll R, Pulido C, de Juan-Sanz J, Sheng M, Südhof T, Tilgner H, Bagni C, Bayés À, Biederer T, Brose N, Chua J, Dieterich D, Gundelfinger E, Hoogenraad C, Huganir R, Jahn R, Kaeser P, Kim E, Kreutz M, McPherson P, Neale B, O'Connor V, Posthuma D, Ryan T, Sala C, Feng G, Hyman S, Thomas P, Smit A, Verhage M. SynGO: An Evidence-Based, Expert-Curated Knowledge Base for the Synapse. Neuron 2019, 103: 217-234.e4. PMID: 31171447, PMCID: PMC6764089, DOI: 10.1016/j.neuron.2019.05.002.Peer-Reviewed Original Research
2017
Transcellular Nanoalignment of Synaptic Function
Biederer T, Kaeser PS, Blanpied TA. Transcellular Nanoalignment of Synaptic Function. Neuron 2017, 96: 680-696. PMID: 29096080, PMCID: PMC5777221, DOI: 10.1016/j.neuron.2017.10.006.Peer-Reviewed Original Research
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
2011
Lateral assembly of the immunoglobulin protein SynCAM 1 controls its adhesive function and instructs synapse formation
Fogel AI, Stagi M, Perez de Arce K, Biederer T. Lateral assembly of the immunoglobulin protein SynCAM 1 controls its adhesive function and instructs synapse formation. The EMBO Journal 2011, 30: 4728-4738. PMID: 21926970, PMCID: PMC3243608, DOI: 10.1038/emboj.2011.336.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell AdhesionCell Adhesion Molecule-1Cell Adhesion MoleculesCell Adhesion Molecules, NeuronalCell DifferentiationCells, CulturedChlorocebus aethiopsCoculture TechniquesCOS CellsFluorescence Resonance Energy TransferHEK293 CellsHippocampusHumansImmunoglobulinsImmunohistochemistryMiceNeuritesProtein Structure, QuaternarySynapsesConceptsSynCAM 1Specialized adhesion sitesSynapse formationTrans-synaptic interactionsSynaptic cleftCI assemblyProtein complexesSynaptic cell adhesion molecule SynCAM 1Adhesion sitesSynaptogenic activityAdhesive functionSynapse developmentStructural organizationNovel insightsSynapse inductionLateral assemblyAdhesive capacityAdhesion moleculesSynaptic morphologyAdhesive mechanismsOligomerizationAssemblyAxo-dendritic contactsCleftLater stages
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
2007
SynCAMs Organize Synapses through Heterophilic Adhesion
Fogel AI, Akins MR, Krupp AJ, Stagi M, Stein V, Biederer T. SynCAMs Organize Synapses through Heterophilic Adhesion. Journal Of Neuroscience 2007, 27: 12516-12530. PMID: 18003830, PMCID: PMC6673342, DOI: 10.1523/jneurosci.2739-07.2007.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell AdhesionCell Adhesion MoleculesCell Adhesion Molecules, NeuronalCell DifferentiationCell LineCells, CulturedCoculture TechniquesHippocampusHumansImmunoglobulinsMacromolecular SubstancesMiceNeural PathwaysPresynaptic TerminalsProtein IsoformsRatsRats, Sprague-DawleySynapsesSynaptic MembranesSynaptic TransmissionTumor Suppressor ProteinsConceptsAdhesion complexesDivergent expression profilesImmunoglobulin superfamily memberHeterophilic complexesProtein familyPosttranslational modificationsHeterophilic adhesionSuperfamily membersCell adhesion moleculeSynapse organizationExpression profilesSynapse developmentSynCAM 1Cell junctionsActive presynaptic terminalsPostsynaptic sideMolecular compositionAdhesion moleculesAdhesive patternsProteinSynaptic cleftPresynaptic terminalsComplexesExcitatory neurotransmissionFunctional synapses
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
2000
Mints as Adaptors DIRECT BINDING TO NEUREXINS AND RECRUITMENT OF Munc18*
Biederer T, Südhof T. Mints as Adaptors DIRECT BINDING TO NEUREXINS AND RECRUITMENT OF Munc18*. Journal Of Biological Chemistry 2000, 275: 39803-39806. PMID: 11036064, DOI: 10.1074/jbc.c000656200.Peer-Reviewed Original ResearchConceptsAdaptor proteinPDZ domain-mediated interactionsDomain-mediated interactionsSynaptic vesicle exocytosisCell surface proteinsNeuronal adaptor proteinMultiprotein complexesProtein essentialCytoplasmic tailMunc18-1Vesicle exocytosisPlasma membraneMunc18NeurexinsDirect bindingPossible functionsSurface proteinsProteinExocytosisMINT1RecruitmentComplexesMint2BindsMint