2014
Lysosome size, motility and stress response regulated by fronto-temporal dementia modifier TMEM106B
Stagi M, Klein ZA, Gould TJ, Bewersdorf J, Strittmatter SM. Lysosome size, motility and stress response regulated by fronto-temporal dementia modifier TMEM106B. Molecular And Cellular Neuroscience 2014, 61: 226-240. PMID: 25066864, PMCID: PMC4145808, DOI: 10.1016/j.mcn.2014.07.006.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBasic Helix-Loop-Helix Leucine Zipper Transcription FactorsCells, CulturedChlorocebus aethiopsEmbryo, MammalianGreen Fluorescent ProteinsHumansLuminescent ProteinsLysosomal-Associated Membrane Protein 1LysosomesMembrane ProteinsMiceMice, Inbred C57BLMicrotubule-Associated ProteinsNerve Tissue ProteinsProtein TransportRNA, MessengerRNA, Small InterferingStress, PhysiologicalTransfection
2009
An Unbiased Expression Screen for Synaptogenic Proteins Identifies the LRRTM Protein Family as Synaptic Organizers
Linhoff MW, Laurén J, Cassidy RM, Dobie FA, Takahashi H, Nygaard HB, Airaksinen MS, Strittmatter SM, Craig AM. An Unbiased Expression Screen for Synaptogenic Proteins Identifies the LRRTM Protein Family as Synaptic Organizers. Neuron 2009, 61: 734-749. PMID: 19285470, PMCID: PMC2746109, DOI: 10.1016/j.neuron.2009.01.017.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell DifferentiationCells, CulturedCloning, MolecularCricetinaeCricetulusDisks Large Homolog 4 ProteinEmbryo, MammalianGene ExpressionGene Expression RegulationGene LibraryGenetic TestingGuanylate KinasesHippocampusHumansIntracellular Signaling Peptides and ProteinsLuminescent ProteinsMembrane PotentialsMembrane ProteinsMiceMice, KnockoutNeuronsPatch-Clamp TechniquesPDZ DomainsPresynaptic TerminalsRatsSynapsesTransfectionVesicular Glutamate Transport Protein 1ConceptsExpression screenSynaptogenic proteinsTrans-synaptic signalingDomain proteinsProtein familyTransmembrane proteinCDNA libraryMolecular basisSynaptogenic activityPresynaptic differentiationVesicular glutamate transporter VGLUT1Postsynaptic differentiationSynaptic organizersSynapse developmentPositive clonesCocultures of neuronsReported linkageLRRTMsCellular basisProteinGlutamate transporter VGLUT1LRRTM1Synaptic functionCurrent understandingAltered distribution
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
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
2002
Myelin-Associated Glycoprotein as a Functional Ligand for the Nogo-66 Receptor
Liu BP, Fournier A, GrandPré T, Strittmatter SM. Myelin-Associated Glycoprotein as a Functional Ligand for the Nogo-66 Receptor. Science 2002, 297: 1190-1193. PMID: 12089450, DOI: 10.1126/science.1073031.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAxonsBinding SitesChick EmbryoCloning, MolecularCOS CellsGanglia, SpinalGene LibraryGPI-Linked ProteinsLigandsMiceMyelin ProteinsMyelin-Associated GlycoproteinNerve RegenerationNeuritesNeuronsNogo ProteinsNogo Receptor 1Peptide FragmentsPhosphatidylinositol Diacylglycerol-LyaseProtein Structure, TertiaryReceptors, Cell SurfaceRecombinant Fusion ProteinsSialic AcidsTransfectionType C PhospholipasesSmall Proline-Rich Repeat Protein 1A Is Expressed by Axotomized Neurons and Promotes Axonal Outgrowth
Bonilla IE, Tanabe K, Strittmatter SM. Small Proline-Rich Repeat Protein 1A Is Expressed by Axotomized Neurons and Promotes Axonal Outgrowth. Journal Of Neuroscience 2002, 22: 1303-1315. PMID: 11850458, PMCID: PMC6757578, DOI: 10.1523/jneurosci.22-04-01303.2002.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsAxonsAxotomyCell DifferentiationCell Surface ExtensionsCornified Envelope Proline-Rich ProteinsCOS CellsGanglia, SpinalMaleMembrane ProteinsMiceMice, Inbred C57BLNerve CrushNerve RegenerationNeuronsOligonucleotide Array Sequence AnalysisProtein BiosynthesisProteinsRNA, MessengerS100 ProteinsSciatic NerveSciatic NeuropathySpinal Cord InjuriesTransfectionConceptsSmall proline-rich repeat protein 1AProtein 1AAxonal outgrowthMembrane rufflesP21/WAFDifferentiation genesCDNA microarrayNerve regenerationF-actinEpithelial differentiation genesPeripheral axonal damageSciatic nerve regenerationSuccessful nerve regenerationAbility of neuronsSPRR1AGenesUninjured neuronsAxotomized neuronsRange of substratesAxonal damageSensory neuronsOutgrowthNeuronsRufflesAxons
1999
Plexin-Neuropilin-1 Complexes Form Functional Semaphorin-3A Receptors
Takahashi T, Fournier A, Nakamura F, Wang L, Murakami Y, Kalb R, Fujisawa H, Strittmatter S. Plexin-Neuropilin-1 Complexes Form Functional Semaphorin-3A Receptors. Cell 1999, 99: 59-69. PMID: 10520994, DOI: 10.1016/s0092-8674(00)80062-8.Peer-Reviewed Original ResearchGrowth 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
1995
An activated mutant of the a subunit of Go increases neurite outgrowth via protein kinase C
Xie R, Li L, Goshima Y, Strittmatter S. An activated mutant of the a subunit of Go increases neurite outgrowth via protein kinase C. Brain Research 1995, 87: 77-86. PMID: 7554235, DOI: 10.1016/0165-3806(95)00061-h.Peer-Reviewed Original ResearchMeSH KeywordsAlkaloidsAnimalsCalciumCalcium Channel BlockersCalcium-Transporting ATPasesDose-Response Relationship, DrugEnzyme InhibitorsEthers, CyclicGallic AcidGTP-Binding ProteinsMutationNeuritesOkadaic AcidPC12 CellsProtein Kinase CRatsSecond Messenger SystemsStaurosporineTerpenesThapsigarginTransfectionConceptsProtein kinase CAlpha oKinase CNeurite outgrowthNeuronal growth cone membraneProtein phosphatase inhibitorSignal transduction cascadeDifferent signal transduction cascadesNeurite extensionGrowth cone membranePhorbol ester treatmentPhosphatase inhibitorTransduction cascadeOkadaic acidEster treatmentPhorbol esterCone membraneNeurite elongationMutantsIntracellular mechanismsKinase inhibitorsOutgrowthSubunitsIntracellular calcium levelsPresence of agents
1994
Activated mutants of the alpha subunit of G(o) promote an increased number of neurites per cell
Strittmatter S, Fishman M, Zhu X. Activated mutants of the alpha subunit of G(o) promote an increased number of neurites per cell. Journal Of Neuroscience 1994, 14: 2327-2338. PMID: 8158271, PMCID: PMC6577129, DOI: 10.1523/jneurosci.14-04-02327.1994.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCell LineChlorocebus aethiopsDNA PrimersDose-Response Relationship, DrugGTP-Binding ProteinsIntercellular Signaling Peptides and ProteinsKineticsMacromolecular SubstancesMolecular Sequence DataMutagenesis, Site-DirectedNeuritesNeuroblastomaPC12 CellsPeptidesPertussis ToxinPoint MutationTransfectionTumor Cells, CulturedVirulence Factors, BordetellaWasp VenomsConceptsAlpha oNumber of neuritesPertussis toxin-sensitive G proteinToxin-sensitive G proteinGrowth conesAlpha subunitG proteinsNeurite outgrowthTotal neurite lengthN1E-115 cellsAlpha i2Activated alpha subunitNeuroblastoma cellsNeurite numberNeurite lengthNeuronal growth conesAlpha sOncogenic mutationsActivation stateO mutantsActivationNeuritesCellsPoint mutationsSubunitsAn amino-terminal domain of the growth-associated protein gap-43 mediates its effects on filopodial formation and cell spreading
Strittmatter S, Valenzuela D, Fishman M. An amino-terminal domain of the growth-associated protein gap-43 mediates its effects on filopodial formation and cell spreading. Journal Of Cell Science 1994, 107: 195-204. PMID: 8175908, DOI: 10.1242/jcs.107.1.195.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCarcinoma, Squamous CellCell LineCell MembraneCell MovementChlorocebus aethiopsColforsinCyclic AMPGAP-43 ProteinGene ExpressionGenetic VectorsGrowth SubstancesHumansMembrane GlycoproteinsMolecular Sequence DataNerve Tissue ProteinsNeuronsPlasmidsSequence DeletionStructure-Activity RelationshipTransfectionTumor Cells, CulturedConceptsAmino-terminal domainCell shapeAmino terminusFusion proteinA431 cellsCell shape changesCOS-7 cellsProtein kinase CGrowth cone membraneCell surface activityLevel of forskolinMutant proteinsHeterotrimeric GTPNon-neuronal cellsG protein stimulationProtein mutantsChimeric geneGAP-43Filopodial formationFunctional domainsCell spreadingBind calmodulinKinase CMajor substratePeptide stretch
1993
Functional expression of sodium channel mutations identified in families with periodic paralysis
Cannon S, Strittmatter S. Functional expression of sodium channel mutations identified in families with periodic paralysis. Neuron 1993, 10: 317-326. PMID: 8382500, DOI: 10.1016/0896-6273(93)90321-h.Peer-Reviewed Original ResearchConceptsSodium channel alpha subunitChannel alpha subunitAlpha subunitFunctional expressionMammalian cell linesSame functional defectSodium channel mutationsBenign polymorphismsSingle-channel conductanceMutationsChannel mutationsCell linesSubunitsMyotubesFunctional defectsPeriodic paralysisProcess of inactivationPotassium dependenceNoninactivating componentNew regionsInactivationExpressionPolymorphismSodium currentFamily
1989
A membrane-targeting signal in the amino terminus of the neuronal protein GAP-43
Zuber M, Strittmatter S, Fishman M. A membrane-targeting signal in the amino terminus of the neuronal protein GAP-43. Nature 1989, 341: 345-348. PMID: 2797153, DOI: 10.1038/341345a0.Peer-Reviewed Original ResearchConceptsGrowth cone membraneN-terminusNeuronal protein GAP-43Membrane-targeting signalMembrane-binding abilityTargeting signalsGAP-43Plasma membraneTransduction systemAmino terminusMutational analysisProminent proteinsParticular proteinFusion proteinShort stretchesMembrane distributionLaser scanning confocal microscopyRegulated growthProteinConfocal microscopyEpithelial cellsProtein GAP-43MembraneModification correlatesDiscrete domains