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
1996
Signal Transduction at the Neuronal Growth Cone
Strittmatter S. Signal Transduction at the Neuronal Growth Cone. The Neuroscientist 1996, 2: 83-86. DOI: 10.1177/107385849600200208.Peer-Reviewed Original ResearchSignal transductionG-protein-mediated transductionG proteinsHeterotrimeric G proteinsCell adhesion molecule familyGrowth conesNervous system developmentAdhesion molecule familyGrowth cone membraneNeuronal growth conesLigand-receptor interactionsGrowth cone motilityCadherin familyIntracellular proteinsCytoskeletal changesExtracellular moleculesMolecular understandingIntegrin familyTransductionMolecules inhibitoryDiffusible messengerMolecule familyCone motilityIntracellular eventsCone membrane
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
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
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 extensionGAP-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
Growth 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