2017
Protein Tyrosine Phosphatase δ Mediates the Sema3A-Induced Cortical Basal Dendritic Arborization through the Activation of Fyn Tyrosine Kinase
Nakamura F, Okada T, Shishikura M, Uetani N, Taniguchi M, Yagi T, Iwakura Y, Ohshima T, Goshima Y, Strittmatter SM. Protein Tyrosine Phosphatase δ Mediates the Sema3A-Induced Cortical Basal Dendritic Arborization through the Activation of Fyn Tyrosine Kinase. Journal Of Neuroscience 2017, 37: 7125-7139. PMID: 28637841, PMCID: PMC6705738, DOI: 10.1523/jneurosci.2519-16.2017.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCells, CulturedCerebral CortexDendritesEnzyme ActivationFemaleGene Expression Regulation, EnzymologicMaleMiceMice, Inbred C57BLMice, KnockoutMice, TransgenicNeuronal PlasticityProtein-Tyrosine KinasesProto-Oncogene Proteins c-fynReceptor-Like Protein Tyrosine Phosphatases, Class 2Semaphorin-3AConceptsCortical dendritic growthBasal dendritesCultured dorsal root ganglion neuronsCortical layer V neuronsPrimary cultured dorsal root ganglion (DRG) neuronsDorsal root ganglion neuronsWild-type cortical neuronsBasal dendritic arborizationLayer V neuronsAxon guidanceDouble heterozygous mutantsSpecific guidance cuesProtein tyrosine phosphatase δAxon guidance cuesPoor arborizationV neuronsGuidance cuesGanglion neuronsDendritic arborizationCortical neuronsMutant miceSemaphorin 3ASrc kinaseActivation of FynGrowth cone collapse response
2008
Release of MICAL Autoinhibition by Semaphorin-Plexin Signaling Promotes Interaction with Collapsin Response Mediator Protein
Schmidt EF, Shim SO, Strittmatter SM. Release of MICAL Autoinhibition by Semaphorin-Plexin Signaling Promotes Interaction with Collapsin Response Mediator Protein. Journal Of Neuroscience 2008, 28: 2287-2297. PMID: 18305261, PMCID: PMC2846290, DOI: 10.1523/jneurosci.5646-07.2008.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsCell Adhesion MoleculesCell Line, TransformedChick EmbryoCytoskeletal ProteinsFlavin-Adenine DinucleotideGanglia, SpinalGenetic VectorsHIVHumansImmunoprecipitationIntracellular Signaling Peptides and ProteinsLIM Domain ProteinsMembrane GlycoproteinsMicrofilament ProteinsMixed Function OxygenasesMutationNerve Tissue ProteinsNeuritesNeuronsPeptide FragmentsProtein BindingSemaphorin-3ASemaphorinsSignal TransductionTransfectionConceptsCollapsin response mediator proteinsMediator proteinsCytoplasmic proteinsEnzymatic domainsCatalytic domainPlexin functionPlexin receptorsTerminal domainMICALPromotes interactionAxon guidanceNeuronal developmentAxonal guidanceEnzymatic activityProteinAutoinhibitionDomainPlexinsSignalingSemaphorinsActivatorAssociatesInteractionActivityActivation
2007
The CRMP Family of Proteins and Their Role in Sema3A Signaling
Schmidt EF, Strittmatter SM. The CRMP Family of Proteins and Their Role in Sema3A Signaling. Advances In Experimental Medicine And Biology 2007, 600: 1-11. PMID: 17607942, PMCID: PMC2853248, DOI: 10.1007/978-0-387-70956-7_1.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAxonsGrowth ConesHumansNerve Tissue ProteinsProtein IsoformsSemaphorin-3ASignal TransductionConceptsMonomeric G proteinsLarge intracellular domainNeuropilin-1Class A plexinsRepulsive axon guidance cuesCurrent knowledgeSema3A signalingVertebrate semaphorinsAxon guidance cuesCellular processesSignal transductionBinding partnerIntracellular domainMediator proteinsProtein turnoverCRMP proteinsF-actinCellular responsesCytosolic phosphoproteinG proteinsNeuronal differentiationRedox proteinsReceptor complexCellular effectsCell membrane
2006
RanBPM Contributes to Semaphorin3A Signaling through Plexin-A Receptors
Togashi H, Schmidt EF, Strittmatter SM. RanBPM Contributes to Semaphorin3A Signaling through Plexin-A Receptors. Journal Of Neuroscience 2006, 26: 4961-4969. PMID: 16672672, PMCID: PMC2846289, DOI: 10.1523/jneurosci.0704-06.2006.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsCell Adhesion MoleculesCell DeathCell SizeCells, CulturedChick EmbryoCloning, MolecularCricetinaeCricetulusCytoskeletal ProteinsDose-Response Relationship, DrugDrug InteractionsEnzyme InhibitorsGanglia, SpinalGene ExpressionGreen Fluorescent ProteinsHumansImmunoprecipitationIn Situ Nick-End LabelingNerve Tissue ProteinsNeuritesNeuronsNeuropilin-1Nuclear ProteinsRan GTP-Binding ProteinSemaphorin-3ASignal TransductionTranscription Factor AP-1TransfectionTwo-Hybrid System TechniquesConceptsPlexin-A1Collapsin response mediator proteinsNervous system developmentReceptor complex consistingSignal transductionRanBPMMediator proteinsMicrotubule functionCell spreadingComplex consistingAxonal guidanceNeuronal cellsAxonal guidance cuesProteinGuidance cuesPlexinsAxonal outgrowthExpressionSema3ATransductionReceptorsDomainOverexpressionNeuropilinsSystem development
2003
Structural bases for CRMP function in plexin‐dependent semaphorin3A signaling
Deo RC, Schmidt EF, Elhabazi A, Togashi H, Burley SK, Strittmatter SM. Structural bases for CRMP function in plexin‐dependent semaphorin3A signaling. The EMBO Journal 2003, 23: 9-22. PMID: 14685275, PMCID: PMC1271659, DOI: 10.1038/sj.emboj.7600021.Peer-Reviewed Original ResearchMeSH KeywordsAlanineAmino Acid SequenceAmino Acid SubstitutionAnimalsCell Adhesion MoleculesCell LineChick EmbryoChlorocebus aethiopsCOS CellsCrystallography, X-RayGanglia, SpinalHumansHydrogen BondingImmunophilinsMiceModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedNerve Tissue ProteinsPhosphoproteinsProtein Structure, SecondaryProtein Structure, TertiaryReceptors, Cell SurfaceRecombinant Fusion ProteinsSemaphorin-3ASequence Homology, Amino AcidSignal TransductionStructure-Activity RelationshipConceptsCollapsin response mediator proteinsStructure-based mutagenesisCOS-7 cellsSurface-exposed residuesTetrameric assemblyPhysical complexAxonal specificationMediator proteinsStructural basisFunctional domainsAlanine substitutionsActive proteinCytosolic phosphoproteinNeuronal differentiationAxonal repulsionAxonal guidanceReceptor componentsProteinStructural viewX-ray crystal structureCRMP1Sema3ACell contractionCellsNP1
2000
Molecular basis of semaphorin‐mediated axon guidance
Nakamura F, Kalb R, Strittmatter S. Molecular basis of semaphorin‐mediated axon guidance. Developmental Neurobiology 2000, 44: 219-229. PMID: 10934324, DOI: 10.1002/1097-4695(200008)44:2<219::aid-neu11>3.0.co;2-w.Peer-Reviewed Original ResearchConceptsGrowth cone collapseSemaphorin guidance cuesMonomeric G proteinsSignal transduction cascadeGuidance cuesAxon guidance eventsCone collapseGrowth cone motilityCaenorhabditis elegansActin cytoskeletonTransmembrane proteinFilopodial tipsNeuropilin-1Transduction cascadeMolecular basisComplex interactsIntracellular domainPrototypic memberGrowth cone turningRac1 activityAxon guidanceG proteinsRepulsive guidance cuesNeuronal proteinsAxonal guidanceSemaphorin3a Enhances Endocytosis at Sites of Receptor–F-Actin Colocalization during Growth Cone Collapse
Fournier A, Nakamura F, Kawamoto S, Goshima Y, Kalb R, Strittmatter S. Semaphorin3a Enhances Endocytosis at Sites of Receptor–F-Actin Colocalization during Growth Cone Collapse. Journal Of Cell Biology 2000, 149: 411-422. PMID: 10769032, PMCID: PMC2175148, DOI: 10.1083/jcb.149.2.411.Peer-Reviewed Original ResearchDendrites go up, axons go down
Strittmatter S. Dendrites go up, axons go down. Nature 2000, 404: 557-559. PMID: 10766224, DOI: 10.1038/35007181.Peer-Reviewed Original Research
1999
Growth cone neuropilin‐1 mediates collapsin‐1/sema III facilitation of antero‐ and retrograde axoplasmic transport
Goshima Y, Hori H, Sasaki Y, Yang T, Maezono M, Li C, Takenaka T, Nakamura F, Takahashi T, Strittmatter S, Misu Y, Kawakami T. Growth cone neuropilin‐1 mediates collapsin‐1/sema III facilitation of antero‐ and retrograde axoplasmic transport. Developmental Neurobiology 1999, 39: 579-589. PMID: 10380079, DOI: 10.1002/(sici)1097-4695(19990615)39:4<579::aid-neu11>3.0.co;2-9.Peer-Reviewed Original Research
1998
Neuropilin-1 Extracellular Domains Mediate Semaphorin D/III-Induced Growth Cone Collapse
Nakamura F, Tanaka M, Takahashi T, Kalb R, Strittmatter S. Neuropilin-1 Extracellular Domains Mediate Semaphorin D/III-Induced Growth Cone Collapse. Neuron 1998, 21: 1093-1100. PMID: 9856464, DOI: 10.1016/s0896-6273(00)80626-1.Peer-Reviewed Original ResearchSemaphorins A and E act as antagonists of neuropilin-1 and agonists of neuropilin-2 receptors
Takahashi T, Nakamura F, Jin Z, Kalb R, Strittmatter S. Semaphorins A and E act as antagonists of neuropilin-1 and agonists of neuropilin-2 receptors. Nature Neuroscience 1998, 1: 487-493. PMID: 10196546, DOI: 10.1038/2203.Peer-Reviewed Original Research
1997
Neuronal and Non-Neuronal Collapsin-1 Binding Sites in Developing Chick Are Distinct from Other Semaphorin Binding Sites
Takahashi T, Nakamura F, Strittmatter S. Neuronal and Non-Neuronal Collapsin-1 Binding Sites in Developing Chick Are Distinct from Other Semaphorin Binding Sites. Journal Of Neuroscience 1997, 17: 9183-9193. PMID: 9364065, PMCID: PMC6573609, DOI: 10.1523/jneurosci.17-23-09183.1997.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAvian ProteinsAxonsBinding SitesCells, CulturedCentral Nervous SystemChick EmbryoDNA, ComplementaryFetal ProteinsGanglia, SpinalGlycoproteinsLungMembrane ProteinsMesodermMiceMotor NeuronsMultigene FamilyNerve Growth FactorsNerve Tissue ProteinsNeuronsNeurotrophin 3Organ SpecificityRatsRats, Sprague-DawleyReceptors, Cell SurfaceRecombinant Fusion ProteinsSemaphorin-3AConceptsFusion proteinBinding sitesGrowth conesDRG neuronsNon-neuronal tissuesExtracellular proteinsF fusion proteinSemaphorin familyDRG growth conesProteinLow nanomolar affinityMajor blood vesselsLigand familyBrainstem neuronsSympathetic neuronsNanomolar affinityNervous systemAxonal pathsBiological activityBlood vesselsNeuronsFamilySitesMesenchymeSemaphorinsBrain CRMP Forms Heterotetramers Similar to Liver Dihydropyrimidinase
Wang L, Strittmatter S. Brain CRMP Forms Heterotetramers Similar to Liver Dihydropyrimidinase. Journal Of Neurochemistry 1997, 69: 2261-2269. PMID: 9375656, DOI: 10.1046/j.1471-4159.1997.69062261.x.Peer-Reviewed Original ResearchA novel action of collapsin: Collapsin‐1 increases antero‐ and retrograde axoplasmic transport independently of growth cone collapse
Goshima Y, Kawakami T, Hori H, Sugiyama Y, Takasawa S, Hashimoto Y, Kagoshima‐Maezono M, Takenaka T, Misu Y, Strittmatter S. A novel action of collapsin: Collapsin‐1 increases antero‐ and retrograde axoplasmic transport independently of growth cone collapse. Developmental Neurobiology 1997, 33: 316-328. PMID: 9298768, DOI: 10.1002/(sici)1097-4695(199709)33:3<316::aid-neu9>3.0.co;2-4.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAxonal TransportCells, CulturedDose-Response Relationship, DrugGanglia, SpinalGlycoproteinsGTP-Binding ProteinsIntercellular Signaling Peptides and ProteinsMiceMice, Inbred C57BLMyelin ProteinsNerve Growth FactorsNeuritesOrganellesPeptidesPertussis ToxinSemaphorin-3AVirulence Factors, BordetellaWasp VenomsRac1 Mediates Collapsin-1-Induced Growth Cone Collapse
Jin Z, Strittmatter SM. Rac1 Mediates Collapsin-1-Induced Growth Cone Collapse. Journal Of Neuroscience 1997, 17: 6256-6263. PMID: 9236236, PMCID: PMC6568359, DOI: 10.1523/jneurosci.17-16-06256.1997.Peer-Reviewed Original ResearchADP Ribose TransferasesAnimalsBotulinum ToxinsCdc42 GTP-Binding ProteinCell Cycle ProteinsCells, CulturedChick EmbryoGanglia, SpinalGlycoproteinsGTP-Binding ProteinsLysophospholipidsMyelin ProteinsNerve Growth FactorsNeuritesRac GTP-Binding ProteinsRecombinant ProteinsRho GTP-Binding ProteinsSemaphorin-3ASensitivity and SpecificityThrombin
1996
A Family of Rat CRMP Genes Is Differentially Expressed in the Nervous System
Wang LH, Strittmatter SM. A Family of Rat CRMP Genes Is Differentially Expressed in the Nervous System. Journal Of Neuroscience 1996, 16: 6197-6207. PMID: 8815901, PMCID: PMC6579169, DOI: 10.1523/jneurosci.16-19-06197.1996.Peer-Reviewed Original ResearchMeSH KeywordsAgingAmino Acid SequenceAnimalsAnimals, NewbornEmbryonic and Fetal DevelopmentGanglia, SensoryGanglia, SympatheticGene ExpressionHumansIntercellular Signaling Peptides and ProteinsIsomerismMolecular Sequence DataMultigene FamilyNerve Tissue ProteinsNervous System Physiological PhenomenaProsencephalonRatsSemaphorin-3ASpinal Cord
1995
Collapsin-induced growth cone collapse mediated by an intracellular protein related to UNC-33
Goshima Y, Nakamura F, Strittmatter P, Strittmatter S. Collapsin-induced growth cone collapse mediated by an intracellular protein related to UNC-33. Nature 1995, 376: 509-514. PMID: 7637782, DOI: 10.1038/376509a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBrainCaenorhabditis elegans ProteinsCell LineCell MembraneChick EmbryoGanglia, SpinalGlycoproteinsGTP-Binding ProteinsHelminth ProteinsIntercellular Signaling Peptides and ProteinsMolecular Sequence DataNerve Growth FactorsNerve Tissue ProteinsNeuritesNeuronsOocytesRecombinant Fusion ProteinsSemaphorin-3ASignal TransductionVirulence Factors, BordetellaXenopus laevisConceptsGrowth cone collapseDorsal root ganglion neuronsCollapsin response mediator proteinsCone collapseXenopus laevis oocyte expression systemChick nervous systemGanglion neuronsNervous systemOocyte expression systemUNC-33Inward currentsNeuronal proteinsAxonal pathfindingNeural developmentX. laevis oocytesGrowth conesLaevis oocytesIntracellular proteinsHeterotrimeric GTPMediator proteinsProteinIntracellular componentsNeurons