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
2018
Mapping the Proteome of the Synaptic Cleft through Proximity Labeling Reveals New Cleft Proteins
Cijsouw T, Ramsey AM, Lam TT, Carbone BE, Blanpied TA, Biederer T. Mapping the Proteome of the Synaptic Cleft through Proximity Labeling Reveals New Cleft Proteins. Proteomes 2018, 6: 48. PMID: 30487426, PMCID: PMC6313906, DOI: 10.3390/proteomes6040048.Peer-Reviewed Original ResearchProximity labelingLabel-free quantitation mass spectrometryReceptor-type tyrosine-protein phosphatase zetaProximity labeling approachCell-cell contactSynaptic cleftPost-synaptic specializationsProteomic contentSynapse heterogeneitySynCAM 1Confocal microcopySurface proteinsCell surfaceProteomeSuper-resolution imagingCultured cortical neuronsMammalian brainLabeling approachMolecular compositionReporterProteinCortical neuronsFunctional organizationExcitatory synapsesDiverse set
2015
Key Molecules: SynCAM Proteins☆
Biederer T, Shrestha N. Key Molecules: SynCAM Proteins☆. 2015 DOI: 10.1016/b978-0-12-801238-3.04784-x.Peer-Reviewed Original ResearchSynaptic cell adhesion moleculesPostsynaptic neurotransmitter receptorsPresynaptic release machineryCell adhesion moleculeAdhesion proteinsPost-synaptic specializationsInstructive signalsContact sitesSynaptic contact sitesRelease machinerySynapse inductionCentral nervous systemAdhesion moleculesNeurotransmitter receptorsProteinSynaptic specializationsNervous systemAsymmetric sitesSpecializationMachinerySitesConcomitant formationAssemblyInductionFamily
2012
Specific N‐glycans on SynCAM Ig proteins regulate synaptic adhesion and synapse development
Biederer T. Specific N‐glycans on SynCAM Ig proteins regulate synaptic adhesion and synapse development. The FASEB Journal 2012, 26: 232.2-232.2. DOI: 10.1096/fasebj.26.1_supplement.232.2.Peer-Reviewed Original ResearchTrans-synaptic interactionsSynapse developmentN-glycansSite-specific N-glycosylationSpecialized cell junctionsSpecific N-glycansProtein complexesFirst Ig domainN-glycosylationBinding interfaceSynaptic adhesionIg domainsFunctional analysisSynCAM 1Cell junctionsIg1 domainImmunoglobulin proteinNovel mechanismIg proteinGlycosylationProteinAdhesive interactionsSynCAMSynaptic cleftExcitatory synapses
2009
SynCAMs
Fogel A, Biederer T. SynCAMs. 2009, 823-828. DOI: 10.1016/b978-008045046-9.01352-8.Peer-Reviewed Original ResearchSynaptic cell adhesion molecule 1Nectin-like molecule-2Functional presynaptic terminalsVertebrate phylumProtein interactionsPlasma membraneAdhesive cuesExpression patternsCentral nervous systemFunctional roleSynaptic plasma membranesProteinCADM-1Adhesion moleculesPresynaptic terminalsCell adhesion molecule-1CofractionatesInvertebratesSuch cuesPhylaMolecule 2Recent progressAdhesion molecule-1Nervous systemSynCAM
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 synapsesMixed-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
2006
SynCAM in Formation and Function of Synaptic Specializations
Biederer T. SynCAM in Formation and Function of Synaptic Specializations. 2006, 125-135. DOI: 10.1007/978-0-387-32562-0_9.Peer-Reviewed Original ResearchInteraction motifsSynCAM 1Short cytosolic tailProtein interaction motifsSingle transmembrane regionIg-like domainsCytosolic tailActin cytoskeletonTransmembrane regionIntracellular sequencesExtracellular sequencesAdaptor moleculeGeneral roleMembrane differentiationSynaptic differentiationCentral nervous systemPostsynaptic membraneAdhesion moleculesProteinSynaptic cleftMotifPresynaptic terminalsDifferentiationSequenceFamily members
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
2001
CASK and Protein 4.1 Support F-actin Nucleation on Neurexins*
Biederer T, Südhof T. CASK and Protein 4.1 Support F-actin Nucleation on Neurexins*. Journal Of Biological Chemistry 2001, 276: 47869-47876. PMID: 11604393, DOI: 10.1074/jbc.m105287200.Peer-Reviewed Original ResearchMeSH KeywordsActinsAmino Acid SequenceAnimalsBinding SitesCalcium-Calmodulin-Dependent Protein KinasesCytoplasmCytoskeletal ProteinsGlycophorinsGuanylate KinasesMembrane ProteinsMolecular Sequence DataNerve Tissue ProteinsNeuropeptidesNucleoside-Phosphate KinaseProtein BindingRatsSequence Homology, Amino AcidSpectrinConceptsProtein 4.1Actin cytoskeletonActin filamentsBrain-enriched isoformF-actin nucleationCytosolic C-terminusClass of proteinsCell surface proteinsCytosolic tailPDZ domainAdaptor proteinCellular processesMembrane organizationC-terminusNeurexinsProtein p55Glycophorin CCell surfaceRat brain extractsIntercellular junctionsSpectrin filamentsErythrocyte isoformsCytoskeletonProteinLocomotion of cells
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