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
1997
A 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
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 componentsNeuronsAn 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
An intrinsic guanine nucleotide exchange inhibitor in Gi2 alpha. Significance of G-protein self-suppression which antagonizes receptor signal.
Okamoto T, Murayama Y, Strittmatter SM, Katada T, Asano S, Ogata E, Nishimoto I. An intrinsic guanine nucleotide exchange inhibitor in Gi2 alpha. Significance of G-protein self-suppression which antagonizes receptor signal. Journal Of Biological Chemistry 1994, 269: 13756-13759. PMID: 8188651, DOI: 10.1016/s0021-9258(17)36711-x.Peer-Reviewed Original ResearchConceptsIntrinsic guanineHeterotrimeric G-protein familyG proteinsReceptor signalsGi2 alphaG protein familyProto-oncogene productProtein familyC-terminusResidues 338Alpha subunitReceptor polypeptideBasal activityAlpha activationPolypeptideGuanineReceptor stimulationAlphaExchange inhibitorInhibitorsReceptorsTerminusSubunitsProteinGi2Activated 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 mutationsSubunits
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 levelsAgonistsMediation by G Proteins of Signals That Cause Collapse of Growth Cones
Igarashi M, Strittmatter S, Vartanian T, Fishman M. Mediation by G Proteins of Signals That Cause Collapse of Growth Cones. Science 1993, 259: 77-79. PMID: 8418498, DOI: 10.1126/science.8418498.Peer-Reviewed Original Research
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