2023
Diverse p120RasGAP interactions with doubly phosphorylated partners EphB4, p190RhoGAP, and Dok1
Vish K, Stiegler A, Boggon T. Diverse p120RasGAP interactions with doubly phosphorylated partners EphB4, p190RhoGAP, and Dok1. Journal Of Biological Chemistry 2023, 299: 105098. PMID: 37507023, PMCID: PMC10470053, DOI: 10.1016/j.jbc.2023.105098.Peer-Reviewed Original ResearchConceptsSH2 domainSpatial-temporal regulationDual SH2 domainsProper vascular developmentKey binding partnerProtein familySH2 interactionsBinding partnerHuman proteinsDistinct binding interactionsWeakened affinityVascular developmentRasGAPConformational differencesP190RhoGAPSmall-angle X-ray scatteringBindingBinding interactionsAffinity measurementsEphB4DomainGTPaseDok1X-ray scatteringProtein
2022
Tandem engagement of phosphotyrosines by the dual SH2 domains of p120RasGAP
Stiegler A, Vish K, Boggon T. Tandem engagement of phosphotyrosines by the dual SH2 domains of p120RasGAP. Structure 2022, 30: 1603-1614.e5. PMID: 36417908, PMCID: PMC9722645, DOI: 10.1016/j.str.2022.10.009.Peer-Reviewed Original ResearchConceptsGTPase-activating proteinsSH2 domainSH2-SH3Src homology 2 domainDual SH2 domainsPhosphotyrosine residuesSH3 domainRho GTPasesPhosphotyrosine recognitionTarget proteinsSynergistic bindingPhosphotyrosineP120RasGAPConformational flexibilityProteinSelectivity mechanismAffinity measurementsDomainGTPasesClose proximityCassetteCrystal structureResiduesCompact arrangementBinding
2001
G-Protein Signaling Through Tubby Proteins
Santagata S, Boggon T, Baird C, Gomez C, Zhao J, Shan W, Myszka D, Shapiro L. G-Protein Signaling Through Tubby Proteins. Science 2001, 292: 2041-2050. PMID: 11375483, DOI: 10.1126/science.1061233.Peer-Reviewed Original ResearchMeSH KeywordsActive Transport, Cell NucleusAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsCell MembraneCell NucleusCells, CulturedCrystallography, X-RayGene Expression RegulationGTP-Binding Protein alpha Subunits, Gq-G11Heterotrimeric GTP-Binding ProteinsHumansIntercellular Signaling Peptides and ProteinsIntracellular Signaling Peptides and ProteinsIsoenzymesMembrane LipidsMiceModels, BiologicalMolecular Sequence DataNuclear Localization SignalsObesityPhosphatidylinositol 4,5-DiphosphatePhosphatidylinositol PhosphatesPhospholipase C betaPhosphorylationProtein Structure, TertiaryProteinsReceptor, Serotonin, 5-HT2CReceptors, MuscarinicReceptors, SerotoninRecombinant Fusion ProteinsSignal TransductionTranscription FactorsType C PhospholipasesConceptsTubby-like protein 3G protein signalingTubby proteinTubby domainTranscription regulatorsPlasma membranePhospholipase C-betaReceptor-mediated activationHeterotrimeric GTPSignal transductionGene expressionMolecular mechanismsTubbyC betaCarboxyl terminalCell nucleiMaturity-onset obesityProteinX-ray crystallographyProtein 3SignalingRegulatorMembranePhosphatidylinositolTransduction
1999
Implication of Tubby Proteins as Transcription Factors by Structure-Based Functional Analysis
Boggon T, Shan W, Santagata S, Myers S, Shapiro L. Implication of Tubby Proteins as Transcription Factors by Structure-Based Functional Analysis. Science 1999, 286: 2119-2125. PMID: 10591637, DOI: 10.1126/science.286.5447.2119.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAlternative SplicingAmino Acid SequenceAnimalsCell LineCell NucleusCrystallography, X-RayDNAEye ProteinsHumansIntercellular Signaling Peptides and ProteinsIntracellular Signaling Peptides and ProteinsModels, MolecularMolecular Sequence DataProtein ConformationProtein Structure, SecondaryProtein Structure, TertiaryProteinsRecombinant ProteinsSequence AlignmentTranscription FactorsTranscriptional ActivationConceptsTubby-like proteinsTubby proteinTranscription factorsBipartite transcription factorDisease phenotypeMulticellular organismsProtein familyBiochemical functionsBiological functionsFunctional analysisStructural cluesCore domainUnique familyProteinGenetic mutationsTubbyPhenotypeRetinal degenerationFamilyMammalsOrganismsVital roleCrystal structureMutationsBroad range