2007
The CRMP Family of Proteins and Their Role in Sema3A Signaling
Schmidt EF, Strittmatter SM. The CRMP Family of Proteins and Their Role in Sema3A Signaling. Advances In Experimental Medicine And Biology 2007, 600: 1-11. PMID: 17607942, PMCID: PMC2853248, DOI: 10.1007/978-0-387-70956-7_1.Peer-Reviewed Original ResearchConceptsMonomeric G proteinsLarge intracellular domainNeuropilin-1Class A plexinsRepulsive axon guidance cuesCurrent knowledgeSema3A signalingVertebrate semaphorinsAxon guidance cuesCellular processesSignal transductionBinding partnerIntracellular domainMediator proteinsProtein turnoverCRMP proteinsF-actinCellular responsesCytosolic phosphoproteinG proteinsNeuronal differentiationRedox proteinsReceptor complexCellular effectsCell membrane
2001
Semaphorin-mediated axonal guidance via Rho-related G proteins
Liu B, Strittmatter S. Semaphorin-mediated axonal guidance via Rho-related G proteins. Current Opinion In Cell Biology 2001, 13: 619-626. PMID: 11544032, DOI: 10.1016/s0955-0674(00)00260-x.Peer-Reviewed Original Research
2000
Molecular basis of semaphorin‐mediated axon guidance
Nakamura F, Kalb R, Strittmatter S. Molecular basis of semaphorin‐mediated axon guidance. Developmental Neurobiology 2000, 44: 219-229. PMID: 10934324, DOI: 10.1002/1097-4695(200008)44:2<219::aid-neu11>3.0.co;2-w.Peer-Reviewed Original ResearchConceptsGrowth cone collapseSemaphorin guidance cuesMonomeric G proteinsSignal transduction cascadeGuidance cuesAxon guidance eventsCone collapseGrowth cone motilityCaenorhabditis elegansActin cytoskeletonTransmembrane proteinFilopodial tipsNeuropilin-1Transduction cascadeMolecular basisComplex interactsIntracellular domainPrototypic memberGrowth cone turningRac1 activityAxon guidanceG proteinsRepulsive guidance cuesNeuronal proteinsAxonal guidance
1999
Go protein-dependent survival of primary accessory olfactory neurons
Tanaka M, Treloar H, Kalb R, Greer C, Strittmatter S. Go protein-dependent survival of primary accessory olfactory neurons. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 14106-14111. PMID: 10570206, PMCID: PMC24198, DOI: 10.1073/pnas.96.24.14106.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisCell Adhesion Molecules, NeuronalCell SurvivalCells, CulturedFemaleGTP-Binding Protein alpha Subunit, Gi2GTP-Binding Protein alpha SubunitsGTP-Binding Protein alpha Subunits, Gi-GoHeterotrimeric GTP-Binding ProteinsHumansMaleMiceMice, Inbred C57BLMice, KnockoutNeural Cell Adhesion MoleculesNeuronsProto-Oncogene ProteinsProto-Oncogene Proteins c-fosRatsSynaptophysinVomeronasal OrganConceptsPosterior accessory olfactory bulbCell survivalAccessory olfactory bulbG proteinsOlfactory systemAccessory olfactory systemG protein-independent processReceptor-coupled G proteinsG protein-coupled receptor familyProtein-coupled receptor familyVNO neuronsAxonal targetingSensory functionAxonal guidanceReceptor familyAnterior accessory olfactory bulbTargeted deletionOlfactory neuronsReceptor neuronsC-Fos immunoreactivityProteinApoptotic neuronsNeurons decreasesOlfactory bulbSensory activation
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
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
Mediation 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 poolResiduesPeptidesCysteineMembraneActivityActivationPool
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 cones