2003
Structural bases for CRMP function in plexin‐dependent semaphorin3A signaling
Deo RC, Schmidt EF, Elhabazi A, Togashi H, Burley SK, Strittmatter SM. Structural bases for CRMP function in plexin‐dependent semaphorin3A signaling. The EMBO Journal 2003, 23: 9-22. PMID: 14685275, PMCID: PMC1271659, DOI: 10.1038/sj.emboj.7600021.Peer-Reviewed Original ResearchMeSH KeywordsAlanineAmino Acid SequenceAmino Acid SubstitutionAnimalsCell Adhesion MoleculesCell LineChick EmbryoChlorocebus aethiopsCOS CellsCrystallography, X-RayGanglia, SpinalHumansHydrogen BondingImmunophilinsMiceModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedNerve Tissue ProteinsPhosphoproteinsProtein Structure, SecondaryProtein Structure, TertiaryReceptors, Cell SurfaceRecombinant Fusion ProteinsSemaphorin-3ASequence Homology, Amino AcidSignal TransductionStructure-Activity RelationshipConceptsCollapsin response mediator proteinsStructure-based mutagenesisCOS-7 cellsSurface-exposed residuesTetrameric assemblyPhysical complexAxonal specificationMediator proteinsStructural basisFunctional domainsAlanine substitutionsActive proteinCytosolic phosphoproteinNeuronal differentiationAxonal repulsionAxonal guidanceReceptor componentsProteinStructural viewX-ray crystal structureCRMP1Sema3ACell contractionCellsNP1
1999
A PDZ Protein Regulates the Distribution of the Transmembrane Semaphorin, M-SemF*
Wang L, Kalb R, Strittmatter S. A PDZ Protein Regulates the Distribution of the Transmembrane Semaphorin, M-SemF*. Journal Of Biological Chemistry 1999, 274: 14137-14146. PMID: 10318831, DOI: 10.1074/jbc.274.20.14137.Peer-Reviewed Original ResearchConceptsPDZ proteinsG-protein signal transduction pathwaySingle PDZ domainDetergent-resistant aggregatesSignal transduction pathwaysAxon guidance signalsPDZ domainCytoplasmic domainProtein interactionsTransduction pathwaysTransmembrane semaphorinsExpression studiesFour residuesGAIPSubcellular distributionHEK293 cellsSemaphorin familyCell surfaceProteinNeural proteinsGuidance signalsInteractsGIPCPDZSemaphorins
1992
Palmitoylation 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