2021
NogoA-expressing astrocytes limit peripheral macrophage infiltration after ischemic brain injury in primates
Boghdadi AG, Spurrier J, Teo L, Li M, Skarica M, Cao B, Kwan WC, Merson TD, Nilsson SK, Sestan N, Strittmatter SM, Bourne JA. NogoA-expressing astrocytes limit peripheral macrophage infiltration after ischemic brain injury in primates. Nature Communications 2021, 12: 6906. PMID: 34824275, PMCID: PMC8617297, DOI: 10.1038/s41467-021-27245-0.Peer-Reviewed Original ResearchConceptsBrain injuryPeripheral macrophage infiltrationIschemic brain injuryAnti-inflammatory responseMajority of astrocytesNeurite outgrowth inhibitory proteinIschemic strokePeripheral macrophagesReactive astrocytesMacrophage infiltrationStroke recoveryAstrocyte clustersMarmoset monkeysVisual cortexAstrocytesNogoASingle-nucleus transcriptomicsInhibitory proteinInjuryStrokeHuman brainInfiltrationCritical rolePrecise functionOligodendrocytes
1998
GAP‐43 Augmentation of G Protein‐Mediated Signal Transduction Is Regulated by Both Phosphorylation and Palmitoylation
Nakamura F, Strittmatter P, Strittmatter S. GAP‐43 Augmentation of G Protein‐Mediated Signal Transduction Is Regulated by Both Phosphorylation and Palmitoylation. Journal Of Neurochemistry 1998, 70: 983-992. PMID: 9489717, DOI: 10.1046/j.1471-4159.1998.70030983.x.Peer-Reviewed Original ResearchConceptsG protein activationG-protein mediated signal transductionProtein kinase C phosphorylation sitesG-protein-coupled receptor stimulationKinase C phosphorylation sitesProtein activationG-protein-coupled signalsNeuronal protein GAP-43C phosphorylation sitesSignal transduction processesProtein kinase CGrowth cone membranePhosphorylation sitesSignal transductionXenopus laevis oocytesGAP-43Transduction processesKinase CResidues 41Second domainLaevis oocytesCone membraneCalmodulinProtein GAP-43Oocytes
1995
Neuronal pathfinding is abnormal in mice lacking the neuronal growth cone protein GAP-43
Strittmatter S, Fankhauser C, Huang P, Mashimo H, Fishman M. Neuronal pathfinding is abnormal in mice lacking the neuronal growth cone protein GAP-43. Cell 1995, 80: 445-452. PMID: 7859286, DOI: 10.1016/0092-8674(95)90495-6.Peer-Reviewed Original Research
1994
GAP-43 amino terminal peptides modulate growth cone morphology and neurite outgrowth
Strittmatter S, Igarashi M, Fishman M. GAP-43 amino terminal peptides modulate growth cone morphology and neurite outgrowth. Journal Of Neuroscience 1994, 14: 5503-5513. PMID: 8083750, PMCID: PMC6577098, DOI: 10.1523/jneurosci.14-09-05503.1994.Peer-Reviewed Original ResearchConceptsGAP-43G-protein activityPertussis toxinNeuronal growth-associated protein GAP-43Neurite outgrowthGrowth-associated protein GAP-43Dorsal root ganglion cellsG protein-mediated eventsGrowth cone membraneDorsal root gangliaProtein GAP-43N1E-115 neuroblastoma cellsChick dorsal root ganglion cellsChick dorsal root gangliaNeurite extensionCone membraneEmbryonic chick dorsal root gangliaRoot gangliaGanglion cellsRetinal neuronsPeptide stimulationGrowth cone collapseGrowth cone morphologyNeuroblastoma cellsPotential modulatorsAn 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
GAP-43 augments G protein-coupled receptor transduction in Xenopus laevis oocytes.
Strittmatter SM, Cannon SC, Ross EM, Higashijima T, Fishman MC. GAP-43 augments G protein-coupled receptor transduction in Xenopus laevis oocytes. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 5327-5331. PMID: 7685122, PMCID: PMC46709, DOI: 10.1073/pnas.90.11.5327.Peer-Reviewed Original ResearchMeSH KeywordsAcetylcholineAnimalsCalciumCattleChloride ChannelsFemaleGAP-43 ProteinGrowth SubstancesGTP-Binding ProteinsHumansInositol 1,4,5-TrisphosphateIon Channel GatingIon ChannelsKineticsMembrane GlycoproteinsMembrane PotentialsMembrane ProteinsNerve Tissue ProteinsOocytesReceptors, MuscarinicRecombinant ProteinsSignal TransductionXenopus laevisConceptsGAP-43Receptor transductionG protein-coupled receptor agonistsCalcium-activated chloride channelXenopus laevis oocytesProtein GAP-43Neuronal protein GAP-43Receptor agonistInjection of inositolLaevis oocytesReceptor stimulationOocyte responseGrowth cone motilityChloride channelsSignal transductionIntracellular regulatorsIntracellular signalsMolecular mechanismsTransductionOocytesHigh levelsAgonists
1992
GAP‐43 as a plasticity protein in neuronal form and repair
Strittmatter S, Vartanian T, Fishman M. GAP‐43 as a plasticity protein in neuronal form and repair. Developmental Neurobiology 1992, 23: 507-520. PMID: 1431834, DOI: 10.1002/neu.480230506.Peer-Reviewed Original ResearchConceptsGrowth cone membraneShort amino-terminal sequenceG proteinsCone membranePlasticity proteinsSpecific cellular domainsAmino-terminal sequenceMembrane localizationG-protein activityGAP-43Cellular domainsProtein activityCell shapeIntracellular proteinsActin filamentsBeta subunitRemarkable plasticityNeural developmentSuch plasticityTerminal sequenceProteinNeurite extensionGuanine nucleotidesNeurite growthAxonal extensionPalmitoylation alters protein activity: blockade of G(o) stimulation by GAP‐43.
Sudo Y, Valenzuela D, Beck‐Sickinger A, Fishman MC, Strittmatter SM. Palmitoylation alters protein activity: blockade of G(o) stimulation by GAP‐43. The EMBO Journal 1992, 11: 2095-2102. PMID: 1534749, PMCID: PMC556676, DOI: 10.1002/j.1460-2075.1992.tb05268.x.Peer-Reviewed Original ResearchConceptsHeterotrimeric G proteinsProtein-protein interactionsMembrane associationFatty acylationGAP-43Cysteine residuesHydrophobicity of proteinsN-terminusAddition of palmitateG proteinsPalmitoylationNeuronal proteinsProteinGAP-43 proteinTerminal peptidesActive poolResiduesPeptidesCysteineMembraneActivityActivationPoolGAP-43 as a modulator of G protein transduction in the growth cone.
Strittmatter SM. GAP-43 as a modulator of G protein transduction in the growth cone. Perspectives On Developmental Neurobiology 1992, 1: 13-9. PMID: 1364285.Peer-Reviewed Original ResearchConceptsGrowth cone membraneGrowth cone motilityMolecular mechanismsSame cellular functionCone motilityG protein-coupled transmembrane receptorsAmino acid stretchComplex cellular propertiesCone membraneGrowth conesNeurotransmitter releaseGrowth cone functionPossible molecular mechanismsCellular functionsGAP-43 functionHydrophilic proteinProtein transductionGAP-43Transmembrane receptorsGAP-43 regulationCysteine residuesTransduction systemSynaptic plasticityAmino terminusCell shape
1991
An intracellular guanine nucleotide release protein for G0. GAP-43 stimulates isolated alpha subunits by a novel mechanism.
Strittmatter SM, Valenzuela D, Sudo Y, Linder ME, Fishman MC. An intracellular guanine nucleotide release protein for G0. GAP-43 stimulates isolated alpha subunits by a novel mechanism. Journal Of Biological Chemistry 1991, 266: 22465-22471. PMID: 1834672, DOI: 10.1016/s0021-9258(18)54595-6.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBrainCattleGAP-43 ProteinGTP-Binding ProteinsGuanine NucleotidesGuanosine 5'-O-(3-Thiotriphosphate)Guanosine DiphosphateGuanosine TriphosphateKineticsLiposomesMacromolecular SubstancesMembrane GlycoproteinsNADNerve Tissue ProteinsPertussis ToxinPhosphatidylcholinesPhosphoproteinsProtein BindingRatsRecombinant ProteinsVirulence Factors, BordetellaConceptsG proteinsMembrane-associated G proteinsGAP-43Novel mechanismG protein-coupled receptorsG protein-coupled membrane receptorsIntracellular guanine nucleotidesGuanine nucleotidesProtein-coupled receptorsCytosolic faceGTP gamma S bindingRegions of neuronsGTPase activityGDP releaseAlpha s.Alpha subunitAlpha i1Alpha oMembrane receptorsNeuronal proteinsBeta gammaGTP gamma SProteinGamma S bindingGrowth conesThe neuronal growth cone as a specialized transduction system
Strittmatter S, Fishman M. The neuronal growth cone as a specialized transduction system. BioEssays 1991, 13: 127-134. PMID: 1831353, DOI: 10.1002/bies.950130306.Peer-Reviewed Original ResearchConceptsGene programGrowth conesNeuronal growth conesExtracellular stimuliEnvironmental signalsExtracellular signalsMembrane proteinsTransduction systemCell shapeGrowth cone behaviorExtracellular matrixGrowth cone activityCone behaviorGrowth programMechanical forcesNeuronal growthProteinTransduction devicesIntrinsic factorsGAP-43Molecular sitesGTPPossible componentsSitesCone activityGrowth cone transduction: Go and GAP-43
STRITTMATTER S, VALENZUELA D, VARTANIAN T, SUDO Y, ZUBER M, FISHMAN M. Growth cone transduction: Go and GAP-43. Journal Of Cell Science. Supplement 1991, 1991: 27-33. PMID: 1840457, DOI: 10.1242/jcs.1991.supplement_15.5.Peer-Reviewed Original ResearchConceptsGrowth cone membraneExtracellular signalsIntracellular proteinsGrowth cone targetingNon-cytoskeletal proteinsG protein familyG-protein-linked receptorsAppropriate synaptic targetsComplex brain architectureCone membraneGrowth conesProtein-linked receptorsGrowth cone functionNeuronal growth conesMembrane associationProtein familyNon-neuronal cellsGAP-43Filopodial formationAmino terminusCell shapeExtrinsic cluesSecond messengerGrowth proteinsProtein
1990
G0 is a major growth cone protein subject to regulation by GAP-43
Strittmatter S, Valenzuela D, Kennedy T, Neer E, Fishman M. G0 is a major growth cone protein subject to regulation by GAP-43. Nature 1990, 344: 836-841. PMID: 2158629, DOI: 10.1038/344836a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBrain ChemistryCell MembraneGAP-43 ProteinGrowth SubstancesGTP-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)Guanosine TriphosphateMembrane GlycoproteinsMolecular Sequence DataMolecular WeightNerve Tissue ProteinsPeptide FragmentsProtein BindingRatsReceptors, Cell SurfaceReceptors, NeurotransmitterSequence Homology, Nucleic AcidSignal TransductionThionucleotidesConceptsTransmembrane receptorsNeuronal growth cone membraneAmino-terminal domainGTP-binding proteinsGrowth cone membraneExtracellular signalsGrowth cone proteinGAP-43Cone membraneGrowth conesCone proteinNeuronal growthProteinS bindingMajor componentG0ReceptorsGTPRegulationIntracellularBindingMembraneDomain
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