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