2019
Phosphorylation of human placental aromatase CYP19A1.
Ghosh D, Egbuta C, Kanyo J, Lam TT. Phosphorylation of human placental aromatase CYP19A1. Biochemical Journal 2019, 476: 3313-3331. PMID: 31652308, PMCID: PMC7069221, DOI: 10.1042/bcj20190633.Peer-Reviewed Original ResearchConceptsAromatase CYP19A1Protein-level regulationPhosphorylation/dephosphorylationMultiple phosphorylation sitesNon-genomic signaling pathwaysPost-translational modificationsNon-genomic signalingTranscriptional activatorPhosphorylation sitesProline residuesSignaling pathwaysHistidine residuesPhosphorylationLevel regulationAromatase inhibitor resistanceInhibitor resistanceMembrane interfaceRegulationReproductive systemStructural dataAromatase activityActive siteResiduesGenotoxic effectsSynaptic terminals
2018
Evaluation of the Phosphoproteome of Mouse Alpha 4/Beta 2-Containing Nicotinic Acetylcholine Receptors In Vitro and In Vivo
Miller MB, Wilson RS, Lam TT, Nairn AC, Picciotto MR. Evaluation of the Phosphoproteome of Mouse Alpha 4/Beta 2-Containing Nicotinic Acetylcholine Receptors In Vitro and In Vivo. Proteomes 2018, 6: 42. PMID: 30326594, PMCID: PMC6313896, DOI: 10.3390/proteomes6040042.Peer-Reviewed Original ResearchProtein kinase APhosphorylation sitesPKA sitesHEK cellsNicotinic acetylcholine receptorsCalmodulin-dependent protein kinase IICalcium/calmodulin-dependent protein kinase IIProtein kinase IIAcetylcholine receptorsKinase AKinase IIMouse brainSubunit phosphorylationNovel siteSubunitsAcute nicotine administrationΒ2 subunitMammalian brainCaMKIIPhosphorylationReceptor functionΑ4 subunitHuman brain tissueBeta 2Nicotine administration
2017
Reciprocal regulation of ARPP-16 by PKA and MAST3 kinases provides a cAMP-regulated switch in protein phosphatase 2A inhibition
Musante V, Li L, Kanyo J, Lam TT, Colangelo CM, Cheng SK, Brody AH, Greengard P, Le Novère N, Nairn AC. Reciprocal regulation of ARPP-16 by PKA and MAST3 kinases provides a cAMP-regulated switch in protein phosphatase 2A inhibition. ELife 2017, 6: e24998. PMID: 28613156, PMCID: PMC5515580, DOI: 10.7554/elife.24998.Peer-Reviewed Original ResearchConceptsARPP-16ARPP-19Protein phosphatase 2A inhibitionProtein phosphatase PP2A.Inhibition of PP2ASwitch-like responseKinase inhibitsPhosphatase PP2A.Regulatory interactionsPKA phosphorylationAntagonistic interplayReciprocal regulationBasal phosphorylationPhosphorylationMAST3PP2APKAENSAKinaseStriatal signalingPP2A.Multiple sitesInhibitionMitosisSignalingBrain Region and Isoform-Specific Phosphorylation Alters Kalirin SH2 Domain Interaction Sites and Calpain Sensitivity
Miller MB, Yan Y, Machida K, Kiraly DD, Levy AD, Wu YI, Lam TT, Abbott T, Koleske AJ, Eipper BA, Mains RE. Brain Region and Isoform-Specific Phosphorylation Alters Kalirin SH2 Domain Interaction Sites and Calpain Sensitivity. ACS Chemical Neuroscience 2017, 8: 1554-1569. PMID: 28418645, PMCID: PMC5517348, DOI: 10.1021/acschemneuro.7b00076.Peer-Reviewed Original ResearchConceptsLong-term potentiationCalpain sensitivityEffects of cocaineRat nucleus accumbensAdult rat nucleus accumbensRho GDP/GTP exchange factorRegion-specific effectsChronic cocaineNucleus accumbensSynaptic functionBrain regionsKALRN geneSpine morphologyPrefrontal cortexKal7CocainePotentiationFunctional significanceCalpainPhosphorylation
2012
Interaction 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
2011
Complex interactions in EML cell stimulation by stem cell factor and IL-3
Ye ZJ, Gulcicek E, Stone K, Lam T, Schulz V, Weissman SM. Complex interactions in EML cell stimulation by stem cell factor and IL-3. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 4882-4887. PMID: 21383156, PMCID: PMC3064389, DOI: 10.1073/pnas.1018002108.Peer-Reviewed Original ResearchConceptsStem cell factorHematopoietic precursor cell lineIL-3Cell factorPrecursor cell lineIL-3 receptorEML cellsTyrosine phosphorylationSubset of cellsSCF receptorDirect interactionCell linesMixed populationRelative levelsCell stimulationCellsComplex interactionsHeterogeneous mixtureReceptorsPhosphorylationLymphoid cells
2009
Palmitoylation of Nicotinic Acetylcholine Receptors
Alexander JK, Govind AP, Drisdel RC, Blanton MP, Vallejo Y, Lam TT, Green WN. Palmitoylation of Nicotinic Acetylcholine Receptors. Journal Of Molecular Neuroscience 2009, 40: 12-20. PMID: 19693711, PMCID: PMC3523180, DOI: 10.1007/s12031-009-9246-z.Peer-Reviewed Original ResearchMeSH KeywordsAcetylcholineAcylationAlpha7 Nicotinic Acetylcholine ReceptorAnimalsBinding SitesBiological AssayBrainCell LineElectric OrganHumansLigandsLipoylationMass SpectrometryNeuromuscular JunctionProtein Processing, Post-TranslationalProtein SubunitsProtein TransportReceptors, NicotinicSynaptic TransmissionTorpedoConceptsNicotinic acetylcholine receptorsSites of palmitoylationLigand-gated ion channelsDifferent posttranslational modificationsDisulfide bond formationMass spectrometry strategyLigand binding siteLow abundant proteinsAcetylcholine receptorsProtein palmitoylationPosttranslational modificationsSubunit assemblyPalmitoylationAbundant proteinsMuscle-type nAChRsIon channelsLoss of ligandBinding sitesSubunitsSitesReceptorsPhosphorylationTraffickingGlycosylationSensitive assay