2020
Insulin and epidermal growth factor receptor family members share parallel activation mechanisms
Ferguson KM, Hu C, Lemmon MA. Insulin and epidermal growth factor receptor family members share parallel activation mechanisms. Protein Science 2020, 29: 1331-1344. PMID: 32297376, PMCID: PMC7255510, DOI: 10.1002/pro.3871.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsReceptor tyrosine kinasesEpidermal growth factor receptorLigand-binding moduleInsulin receptorAutoinhibitory interactionsRecent cryo-electron microscopy structuresCryo-electron microscopy structureFirst receptor tyrosine kinasesRecent cryo-EM structureEGFR activation mechanismsEpidermal growth factor receptor family membersActivated insulin receptorIntramolecular autoinhibitory interactionCryo-EM structureActivation mechanismCysteine-rich domainFibronectin type III domainReceptor family membersEGFR family membersType III domainMicroscopy structureDomain compositionTransmembrane regionGrowth factor receptorLike domain
2017
Dimerization of Tie2 mediated by its membrane-proximal FNIII domains
Moore JO, Lemmon MA, Ferguson KM. Dimerization of Tie2 mediated by its membrane-proximal FNIII domains. Proceedings Of The National Academy Of Sciences Of The United States Of America 2017, 114: 4382-4387. PMID: 28396397, PMCID: PMC5410832, DOI: 10.1073/pnas.1617800114.Peer-Reviewed Original ResearchConceptsExtracellular regionFNIII domainsResolution X-ray crystal structureMembrane-proximal fibronectin type III domainsDomain-mediated interactionsDifferent cellular contextsLigand-binding regionHigher-order oligomersTie2 activationFibronectin type III domainReceptor tyrosine kinasesTyrosine kinase familyEGF-homology domainThird FNIII domainType III domainPrevious structural studiesStructural studiesHomology domainCellular contextKinase familyDimer interfaceDimerization modeReceptor dimerizationTyrosine kinasePrimary activator