2021
ROR and RYK extracellular region structures suggest that receptor tyrosine kinases have distinct WNT-recognition modes
Shi F, Mendrola JM, Sheetz JB, Wu N, Sommer A, Speer KF, Noordermeer JN, Kan ZY, Perry K, Englander SW, Stayrook SE, Fradkin LG, Lemmon MA. ROR and RYK extracellular region structures suggest that receptor tyrosine kinases have distinct WNT-recognition modes. Cell Reports 2021, 37: 109834. PMID: 34686333, PMCID: PMC8650758, DOI: 10.1016/j.celrep.2021.109834.Peer-Reviewed Original ResearchAnimalsDrosophila melanogasterDrosophila ProteinsModels, MolecularNerve Tissue ProteinsProtein BindingProtein ConformationProtein Interaction Domains and MotifsProtein-Tyrosine KinasesProto-Oncogene ProteinsReceptor Protein-Tyrosine KinasesSf9 CellsStructure-Activity RelationshipWnt ProteinsWnt Signaling Pathway
2008
Structural basis for EGFR ligand sequestration by Argos
Klein DE, Stayrook SE, Shi F, Narayan K, Lemmon MA. Structural basis for EGFR ligand sequestration by Argos. Nature 2008, 453: 1271-1275. PMID: 18500331, PMCID: PMC2526102, DOI: 10.1038/nature06978.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBinding SitesCell LineCrystallography, X-RayDrosophila melanogasterDrosophila ProteinsEpidermal Growth FactorErbB ReceptorsEye ProteinsHumansLigandsMembrane ProteinsModels, MolecularNerve Tissue ProteinsProtein Structure, TertiaryReceptors, Transforming Growth Factor betaSpodopteraConceptsEpidermal growth factor receptorLigand sequestrationEGFR ligand SpitzLigand SpitzMammalian counterpartsGrowth factor receptorStructural basisUrokinase plasminogen activatorStructural homologuesEGFR ligandsFactor receptorAnticancer therapeuticsStructural resemblanceHomologuesPlasminogen activatorReceptorsSequestrationProteinActivatorLigandsSpitzTGFTherapeuticsDomain
2006
Argos Mutants Define an Affinity Threshold for Spitz Inhibition in Vivo *
Alvarado D, Evans TA, Sharma R, Lemmon MA, Duffy JB. Argos Mutants Define an Affinity Threshold for Spitz Inhibition in Vivo *. Journal Of Biological Chemistry 2006, 281: 28993-29001. PMID: 16870613, DOI: 10.1074/jbc.m603782200.Peer-Reviewed Original Research
1998
Phosphatidylinositol-4,5-bisphosphate is required for endocytic coated vesicle formation
Jost M, Simpson F, Kavran J, Lemmon M, Schmid S. Phosphatidylinositol-4,5-bisphosphate is required for endocytic coated vesicle formation. Current Biology 1998, 8: 1399-1404. PMID: 9889104, DOI: 10.1016/s0960-9822(98)00022-0.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex 2Adaptor Proteins, Vesicular TransportBiotinCell MembraneClathrinEndocytosisEndosomesHumansIsoenzymesMutagenesisNeomycinNerve Tissue ProteinsPhosphatidylinositol 4,5-DiphosphatePhospholipase C deltaPhosphoproteinsProtein BindingTransferrinTumor Cells, CulturedType C PhospholipasesConceptsCoated vesicle formationEndocytic coated vesicle formationVesicle formationPleckstrin homology domainClathrin-coated vesiclesInvolvement of phosphatidylinositolReceptor-mediated endocytosisBind phosphatidylinositolGTPase dynaminAP2 complexProtein playersEndocytic motifEndocytic machineryHomology domainPH domainCoat assemblyInositol polyphosphateHigh-specificity probesGTPase activityInositol lipidsPhosphatidylinositolFirst direct evidenceDirect evidenceClathrinEndocytosis