2014
Angiotensin II signaling via protein kinase C phosphorylates Kelch-like 3, preventing WNK4 degradation
Shibata S, Arroyo JP, Castañeda-Bueno M, Puthumana J, Zhang J, Uchida S, Stone KL, Lam TT, Lifton RP. Angiotensin II signaling via protein kinase C phosphorylates Kelch-like 3, preventing WNK4 degradation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 15556-15561. PMID: 25313067, PMCID: PMC4217463, DOI: 10.1073/pnas.1418342111.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceAngiotensin IIAnimalsCarrier ProteinsCell LineHumansKidneyMice, Inbred C57BLMicrofilament ProteinsMolecular Sequence DataPhosphorylationPhosphoserineProtein BindingProtein Kinase CProtein Serine-Threonine KinasesProteolysisSignal TransductionConceptsRenal salt reabsorptionAngiotensin IIVolume depletionSalt reabsorptionNormal physiologic responseProtein kinase CAII administrationBlood pressureCardiovascular diseaseGlobal burdenPhysiologic responsesCullin 3Kinase CNaCl cotransporterReabsorptionHuman genetic studiesSecretionHypertensionNormal mechanismsWNK4 degradationMissense mutationsSerine 433WNK4Inverse relationshipCultured cellsInhibitor of the Tyrosine Phosphatase STEP Reverses Cognitive Deficits in a Mouse Model of Alzheimer's Disease
Xu J, Chatterjee M, Baguley TD, Brouillette J, Kurup P, Ghosh D, Kanyo J, Zhang Y, Seyb K, Ononenyi C, Foscue E, Anderson GM, Gresack J, Cuny GD, Glicksman MA, Greengard P, Lam TT, Tautz L, Nairn AC, Ellman JA, Lombroso PJ. Inhibitor of the Tyrosine Phosphatase STEP Reverses Cognitive Deficits in a Mouse Model of Alzheimer's Disease. PLOS Biology 2014, 12: e1001923. PMID: 25093460, PMCID: PMC4122355, DOI: 10.1371/journal.pbio.1001923.Peer-Reviewed Original ResearchMeSH KeywordsAlzheimer DiseaseAmino Acid SequenceAnimalsBenzothiepinsCatalytic DomainCell DeathCerebral CortexCognition DisordersCysteineDisease Models, AnimalEnzyme InhibitorsHigh-Throughput Screening AssaysHumansMaleMice, Inbred C57BLMice, KnockoutMolecular Sequence DataNeuronsPhosphorylationPhosphotyrosineProtein Tyrosine Phosphatases, Non-ReceptorSubstrate SpecificityConceptsInhibitors of stepsSpecificity of inhibitorsIsoxazolepropionic acid receptor (AMPAR) traffickingCatalytic cysteinePTP inhibitorsTyrosine phosphataseTyrosine phosphorylationSecondary assaysSTEP KO miceReceptor traffickingFirst large-scale effortN-methyl-D-aspartate receptorsPyk2 activitySTEP inhibitorLarge-scale effortsNovel therapeutic targetSynaptic functionAlzheimer's diseaseNeurodegenerative disordersCortical cellsTherapeutic targetERK1/2Specificity experimentsPhosphataseInhibitors
2012
Endothelial Cell Palmitoylproteomic Identifies Novel Lipid-Modified Targets and Potential Substrates for Protein Acyl Transferases
Marin EP, Derakhshan B, Lam TT, Davalos A, Sessa WC. Endothelial Cell Palmitoylproteomic Identifies Novel Lipid-Modified Targets and Potential Substrates for Protein Acyl Transferases. Circulation Research 2012, 110: 1336-1344. PMID: 22496122, PMCID: PMC3428238, DOI: 10.1161/circresaha.112.269514.Peer-Reviewed Original ResearchMeSH KeywordsAcetyltransferasesAcyltransferasesAmino Acid SequenceAnimalsChlorocebus aethiopsCOS CellsEndothelial CellsHEK293 CellsHuman Umbilical Vein Endothelial CellsHumansLipoylationMolecular Sequence DataPlatelet Endothelial Cell Adhesion Molecule-1ProteomicsRNA, Small InterferingSubstrate SpecificitySuperoxide DismutaseSuperoxide Dismutase-1ConceptsProtein acyl transferasesAcyl-biotinyl exchangeProtein S-palmitoylationPlatelet endothelial cell adhesion molecule-1Posttranslational lipid modificationRole of palmitoylationEndothelial cell adhesion molecule-1Acyl transferaseEndothelial cell biologyPalmitoyl proteinsS-palmitoylationPosttranslational attachmentProtein localizationCysteine side chainsCell biologyNuclear localizationPalmitoylationLipid modificationEC biologyThioester bondCell adhesion molecule-1Superoxide dismutase 1Functional roleCell surfacePotential substratesInteraction of the Histone mRNA Hairpin with Stem–Loop Binding Protein (SLBP) and Regulation of the SLBP–RNA Complex by Phosphorylation and Proline Isomerization
Zhang M, Lam TT, Tonelli M, Marzluff WF, Thapar R. Interaction of the Histone mRNA Hairpin with Stem–Loop Binding Protein (SLBP) and Regulation of the SLBP–RNA Complex by Phosphorylation and Proline Isomerization. Biochemistry 2012, 51: 3215-3231. PMID: 22439849, PMCID: PMC3328597, DOI: 10.1021/bi2018255.Peer-Reviewed Original ResearchConceptsStem-loop binding proteinStem-loop structureHistone mRNAProline isomerizationThreonine phosphorylationEnd formationC base pairsReplication-dependent histone mRNAsBase pairsBinding proteinPossible structural roleAdjacent prolineHistone proteinsRibonucleoprotein complexesHelix motifMRNA hairpinsMRNA complexesUntranslated regionStructural roleFirst binding sitePhosphorylationProteinComplex dissociationCritical hingeMRNA
2005
Multicomponent Internal Recalibration of an LC−FTICR-MS Analysis Employing a Partially Characterized Complex Peptide Mixture: Systematic and Random Errors
Yanofsky CM, Bell AW, Lesimple S, Morales F, Lam TT, Blakney GT, Marshall AG, Carrillo B, Lekpor K, Boismenu D, Kearney RE. Multicomponent Internal Recalibration of an LC−FTICR-MS Analysis Employing a Partially Characterized Complex Peptide Mixture: Systematic and Random Errors. Analytical Chemistry 2005, 77: 7246-7254. PMID: 16285672, DOI: 10.1021/ac050640q.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCalibrationChromatography, LiquidMass SpectrometryMolecular Sequence DataPeptide LibraryPeptidesRatsSpectroscopy, Fourier Transform InfraredFourier Transform Ion Cyclotron Resonance Mass Spectrometry for the Analysis of Small Ubiquitin-like Modifier (SUMO) Modification: Identification of Lysines in RanBP2 and SUMO Targeted for Modification during the E3 AutoSUMOylation Reaction
Cooper HJ, Tatham MH, Jaffray E, Heath JK, Lam TT, Marshall AG, Hay RT. Fourier Transform Ion Cyclotron Resonance Mass Spectrometry for the Analysis of Small Ubiquitin-like Modifier (SUMO) Modification: Identification of Lysines in RanBP2 and SUMO Targeted for Modification during the E3 AutoSUMOylation Reaction. Analytical Chemistry 2005, 77: 6310-6319. PMID: 16194093, DOI: 10.1021/ac058019d.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCyclotronsFourier AnalysisIonsLysineMass SpectrometryMethylationMolecular ChaperonesMolecular Sequence DataMolecular WeightNuclear Pore Complex ProteinsProtein BindingRecombinant ProteinsSequence AlignmentSmall Ubiquitin-Related Modifier ProteinsUbiquitinUbiquitin-Protein LigasesConceptsFourier transform ion cyclotron resonance mass spectrometryTransform ion cyclotron resonance mass spectrometryIon cyclotron resonance mass spectrometryFourier transform ion cyclotron resonanceCyclotron resonance mass spectrometryMass spectrometryTransform ion cyclotron resonanceElectron capture dissociationResonance mass spectrometryMass spectrometry techniquesSUMO modificationIon cyclotron resonanceIdentification of LysinesCapture dissociationFunctional analysisUbiquitin-like protein SUMOLysine residuesSmall ubiquitin-like modifier (SUMO) modificationFT-ICRAcceptor lysine residuesImportant cellular processesSpectrometry techniquesSite-directed mutagenesisSites of sumoylationSUMO polymers
2004
Identification of Sites of Ubiquitination in Proteins: A Fourier Transform Ion Cyclotron Resonance Mass Spectrometry Approach
Cooper HJ, Heath JK, Jaffray E, Hay RT, Lam TT, Marshall AG. Identification of Sites of Ubiquitination in Proteins: A Fourier Transform Ion Cyclotron Resonance Mass Spectrometry Approach. Analytical Chemistry 2004, 76: 6982-6988. PMID: 15571350, DOI: 10.1021/ac0401063.Peer-Reviewed Original ResearchConceptsSites of ubiquitinationPolyubiquitin chainsFourier transform ion cyclotron resonance mass spectrometryTransform ion cyclotron resonance mass spectrometryIon electron capture dissociationIon cyclotron resonance mass spectrometryCyclotron resonance mass spectrometryLysine residuesTandem mass spectrometric techniquesElectron capture dissociationResonance mass spectrometryExtensive sequence coverageMass spectrometric techniquesConsequences of ubiquitinationCapture dissociationMass spectrometry approachPolyubiquitinated speciesSingle ubiquitinFT-ICRStructural elucidationCellular functionsUbiquitinated proteinsModified peptideUbiquitination modificationSpectrometric techniques
2002
Mapping of protein:protein contact surfaces by hydrogen/deuterium exchange, followed by on-line high-performance liquid chromatography–electrospray ionization fourier-transform ion-cyclotron-resonance mass analysis
Lam TT, Lanman JK, Emmett MR, Hendrickson CL, Marshall AG, Prevelige PE. Mapping of protein:protein contact surfaces by hydrogen/deuterium exchange, followed by on-line high-performance liquid chromatography–electrospray ionization fourier-transform ion-cyclotron-resonance mass analysis. Journal Of Chromatography A 2002, 982: 85-95. PMID: 12489858, DOI: 10.1016/s0021-9673(02)01357-2.Peer-Reviewed Original ResearchConceptsHigh-Performance Liquid Chromatography-Electrospray IonizationMass analysisHydrogen/deuterium exchangeLiquid Chromatography-Electrospray IonizationNuclear magnetic resonance analysisX-ray diffractionFront-end separationMagnetic resonance analysisBackbone amide hydrogensProtein contact surfacesAmide hydrogensDeuterium exchangeConventional X-ray diffractionH/2H exchangeReaction periodResonance analysisLow concentrationsDiffractionProtein complexesComplexedHydrogenComplexesIonizationSeparationSurface