2021
Structural basis for ligand reception by anaplastic lymphoma kinase
Li T, Stayrook SE, Tsutsui Y, Zhang J, Wang Y, Li H, Proffitt A, Krimmer SG, Ahmed M, Belliveau O, Walker IX, Mudumbi KC, Suzuki Y, Lax I, Alvarado D, Lemmon MA, Schlessinger J, Klein DE. Structural basis for ligand reception by anaplastic lymphoma kinase. Nature 2021, 600: 148-152. PMID: 34819665, PMCID: PMC8639777, DOI: 10.1038/s41586-021-04141-7.Peer-Reviewed Original ResearchROR 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
2020
Structural Insights into Pseudokinase Domains of Receptor Tyrosine Kinases
Sheetz JB, Mathea S, Karvonen H, Malhotra K, Chatterjee D, Niininen W, Perttilä R, Preuss F, Suresh K, Stayrook SE, Tsutsui Y, Radhakrishnan R, Ungureanu D, Knapp S, Lemmon MA. Structural Insights into Pseudokinase Domains of Receptor Tyrosine Kinases. Molecular Cell 2020, 79: 390-405.e7. PMID: 32619402, PMCID: PMC7543951, DOI: 10.1016/j.molcel.2020.06.018.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBaculoviridaeBinding SitesCell Adhesion MoleculesCell LineCloning, MolecularCrystallography, X-RayGene ExpressionHumansMiceModels, MolecularPrecursor Cells, B-LymphoidProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsProtein Kinase InhibitorsReceptor Protein-Tyrosine KinasesReceptor Tyrosine Kinase-like Orphan ReceptorsReceptors, Eph FamilyRecombinant ProteinsSf9 CellsSmall Molecule LibrariesSpodopteraStructural Homology, ProteinSubstrate SpecificityConceptsInsulin receptor kinasePseudokinase domainReceptor tyrosine kinasesTyrosine kinaseNon-catalytic functionsATP-binding pocketType II inhibitorsDomain plasticityActivation loopReceptor kinaseInactive conformationStructural insightsPseudokinasesATP siteStructural comparisonAromatic residuesKinaseAlternative interactionsApparent lackImportant roleDomainWntMotifROR1Residues
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
2007
Prevalence of the EH1 Groucho interaction motif in the metazoan Fox family of transcriptional regulators
Yaklichkin S, Vekker A, Stayrook S, Lewis M, Kessler D. Prevalence of the EH1 Groucho interaction motif in the metazoan Fox family of transcriptional regulators. BMC Genomics 2007, 8: 201. PMID: 17598915, PMCID: PMC1939712, DOI: 10.1186/1471-2164-8-201.Peer-Reviewed Original ResearchConceptsEh1-like motifsFox gene familyFox family proteinsFox proteinsGroucho interaction motifEh1 motifGene familyTranscriptional regulationFOX familyFamily proteinsInteraction motifsStructure predictionWinged helix DNA-binding domainFamily of transcriptional regulatorsSecondary structure predictionDNA-binding domainN-terminal motifSwiss protein databaseManual sequence alignmentFOX family genesDivergent speciesSequence alignmentProtein sequencesProtein databaseTranscriptional corepressor
1998
Steroidogenic Acute Regulatory Protein (StAR) Is A Sterol Transfer Protein*
Kallen C, Billheimer J, Summers S, Stayrook S, Lewis M, Strauss J. Steroidogenic Acute Regulatory Protein (StAR) Is A Sterol Transfer Protein*. Journal Of Biological Chemistry 1998, 273: 26285-26288. PMID: 9756854, DOI: 10.1074/jbc.273.41.26285.Peer-Reviewed Original ResearchConceptsSterol carrier protein-2Steroidogenic acute regulatory proteinStAR proteinRegulatory proteinsSterol transferCholesterol side-chain cleavage enzyme systemMitochondrial targeting sequenceSterol transfer activityTransfer proteinSterol transfer proteinsOuter mitochondrial membraneTrypsin-treated mitochondriaAmino acid residuesLipid transfer proteinsTransfer of cholesterolDonor membranesSubstrate cholesterolInner membraneMitochondrial membraneIsolated mitochondriaTarget sequenceN-terminalTemperature-dependent mannerAcid residuesPhosphatidylcholine transferThe Mechanism of Action of Steroidogenic Acute Regulatory Protein (StAR) StAR ACTS ON THE OUTSIDE OF MITOCHONDRIA TO STIMULATE STEROIDOGENESIS*
Arakane F, Kallen C, Watari H, Foster J, Sepuri N, Pain D, Stayrook S, Lewis M, Gerton G, Strauss J. The Mechanism of Action of Steroidogenic Acute Regulatory Protein (StAR) StAR ACTS ON THE OUTSIDE OF MITOCHONDRIA TO STIMULATE STEROIDOGENESIS*. Journal Of Biological Chemistry 1998, 273: 16339-16345. PMID: 9632696, DOI: 10.1074/jbc.273.26.16339.Peer-Reviewed Original ResearchConceptsCOS-1 cellsMitochondrial targeting sequenceWild-type StARSteroidogenic acute regulatory proteinStAR preproteinHis-tagMitochondrial membraneIsolated mitochondriaNH2-terminal mitochondrial targeting sequenceCOS-1Target sequenceRegulatory proteinsMechanism of StAR's actionIn vitro import assayStAR proteinStAR's actionCytoplasm of transfected COS-1 cellsProteins associated with mitochondriaCholesterol side-chain cleavage systemLipoid congenital adrenal hyperplasiaSide-chain cleavage systemLocalized to mitochondriaN-62 StARHis-tagged proteinsAbsence of cytosolSteroidogenic acute regulatory protein (StAR) acts on the outside of mitochondria to stimulate steroidogenesis
Arakane F, Kallen C, Watari H, Stayrook S, Lewis M, Strauss J. Steroidogenic acute regulatory protein (StAR) acts on the outside of mitochondria to stimulate steroidogenesis. Endocrine Research 1998, 24: 463-468. PMID: 9888526, DOI: 10.3109/07435809809032634.Peer-Reviewed Original ResearchConceptsCOS-1 cellsMitochondrial targeting sequenceWild-type StARSteroidogenic acute regulatory proteinHis-tagMitochondrial membraneIsolated mitochondriaN-terminal mitochondrial targeting sequenceTarget sequenceCOS-1Regulatory proteinsCytoplasm of transfected COS-1 cellsCholesterol side-chain cleavage systemLipoid congenital adrenal hyperplasiaSide-chain cleavage systemLocalized to mitochondriaInner mitochondrial membraneHis-tagged proteinsDelivery of cholesterolMitochondrial importPoint mutantsN-terminalStAR proteinCleavage systemE. coli