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
2009
N-terminal Domains Elicit Formation of Functional Pmel17 Amyloid Fibrils*
Watt B, van Niel G, Fowler DM, Hurbain I, Luk KC, Stayrook SE, Lemmon MA, Raposo G, Shorter J, Kelly JW, Marks MS. N-terminal Domains Elicit Formation of Functional Pmel17 Amyloid Fibrils*. Journal Of Biological Chemistry 2009, 284: 35543-35555. PMID: 19840945, PMCID: PMC2790984, DOI: 10.1074/jbc.m109.047449.Peer-Reviewed Original ResearchConceptsFibril formationFormation of melanosomesMultivesicular compartmentsImperfect repeatsRPT domainTransmembrane proteinMelanosome maturationTerminal domainIntracellular traffickingMultivesicular bodiesAmyloid foldPrecursor organellesAmyloid-like fibrilsDownstream domainSubcellular organellesAmyloid conversionRegulatory rolePmel17RepeatsEarly stepsStructural coreAmyloid formationProteolytic fragmentsRecombinant fragmentsOrganelles
2001
Crystal Structure of Human Type III 3α-Hydroxysteroid Dehydrogenase/Bile Acid Binding Protein Complexed with NADP+ and Ursodeoxycholate † , ‡
Jin Y, Stayrook S, Albert R, Palackal N, Penning T, Lewis M. Crystal Structure of Human Type III 3α-Hydroxysteroid Dehydrogenase/Bile Acid Binding Protein Complexed with NADP+ and Ursodeoxycholate † , ‡. Biochemistry 2001, 40: 10161-10168. PMID: 11513593, DOI: 10.1021/bi010919a.Peer-Reviewed Original ResearchMeSH KeywordsAllosteric RegulationAllosteric SiteAmino Acid SequenceBinding SitesCloning, MolecularComputer SimulationCrystallography, X-RayEscherichia coliFluoxetineHumansHydroxysteroid DehydrogenasesModels, MolecularMolecular ConformationMolecular Sequence DataNADPProtein BindingProtein Structure, SecondaryRecombinant ProteinsSequence AlignmentSequence Homology, Amino AcidUrsodeoxycholic AcidConceptsRat 3alpha-HSDAldo-keto reductase superfamilyBinding protein complexSteroid binding pocketAlpha/beta barrelBound NADP(+Human typeProtein complexesThree-dimensional structureOxyanion holeAndrogen 5alpha-dihydrotestosteroneBinding proteinStructural basisTransport of bile acidsAKR1C2Ternary complexRat isoformsNADP(+SuperfamilyExtended conformationProstatic productionActive siteIsoformsCrystal structureBile acids
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 ResearchMeSH KeywordsAnimalsBiological TransportCattleCholesterolHumansMembrane ProteinsMiceMicrosomes, LiverPhosphatidylcholinesPhosphoproteinsRatsRecombinant ProteinsConceptsSterol 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