2024
A complex of the lipid transport ER proteins TMEM24 and C2CD2 with band 4.1 at cell–cell contacts
Johnson B, Iuliano M, Lam T, Biederer T, De Camilli P. A complex of the lipid transport ER proteins TMEM24 and C2CD2 with band 4.1 at cell–cell contacts. Journal Of Cell Biology 2024, 223: e202311137. PMID: 39158698, PMCID: PMC11334333, DOI: 10.1083/jcb.202311137.Peer-Reviewed Original ResearchConceptsPlasma membraneNon-vesicular lipid transferSites of cell contactC-terminus motifsCell contact-dependent signalsContact-dependent signalingCell-cell contactER/PM junctionsTMEM24ER proteinsPM proteinsSynCAM 1Cell adhesion moleculesCellular functionsLipid transferC2CD2Phospholipid transportLipid transportCell contactProteinAdhesion moleculesCalcium homeostasisCellsFamily membersParalogs
2020
Bioactive Plasma Mitochondrial DNA Is Associated With Disease Progression in Scleroderma‐Associated Interstitial Lung Disease
Ryu C, Walia A, Ortiz V, Perry C, Woo S, Reeves BC, Sun H, Winkler J, Kanyo JE, Wang W, Vukmirovic M, Ristic N, Stratton EA, Meena SR, Minasyan M, Kurbanov D, Liu X, Lam TT, Farina G, Gomez JL, Gulati M, Herzog EL. Bioactive Plasma Mitochondrial DNA Is Associated With Disease Progression in Scleroderma‐Associated Interstitial Lung Disease. Arthritis & Rheumatology 2020, 72: 1905-1915. PMID: 32602227, PMCID: PMC8081728, DOI: 10.1002/art.41418.Peer-Reviewed Original ResearchConceptsCGAS/STING activationExtracellular vesiclesMitochondrial DNAPattern recognition receptorsCyclic GMP-AMP synthase/stimulatorHuman lung fibroblastsSSc-ILD cohortsInterstitial lung diseaseMT-ATP6 geneΑ-SMA expressionI interferonSSc-ILDScleroderma-Associated Interstitial Lung DiseaseSynthetic CpG DNATLR-9Clinical outcomesLung diseaseSTING activationInterleukin-6Enzyme-linked immunosorbent assay-based methodProteomic profilesMulticellular originSystemic sclerosis-associated interstitial lung diseaseImmune pattern recognition receptorsExtracellular mtDNA
2019
A single phosphoacceptor residue in BGLF3 is essential for transcription of Epstein-Barr virus late genes
Li J, Walsh A, Lam TT, Delecluse HJ, El-Guindy A. A single phosphoacceptor residue in BGLF3 is essential for transcription of Epstein-Barr virus late genes. PLOS Pathogens 2019, 15: e1007980. PMID: 31461506, PMCID: PMC6713331, DOI: 10.1371/journal.ppat.1007980.Peer-Reviewed Original ResearchConceptsPost-translational modificationsLate gene expressionLate genesGene expressionPhosphoacceptor residuesPre-initiation complexPotential phosphorylation sitesViral DNA replicationNew virus particlesEarly gene expressionPhosphorylation sitesVirus particlesDNA replicationTATA boxHerpesvirus proteinsEctopic expressionTrimeric complexLate proteinsLate transcriptsHost cellsEarly proteinsGenesTranscriptionLate kineticsProteinPreincubation With Everolimus and Sirolimus Reduces Organic Anion-Transporting Polypeptide (OATP)1B1- and 1B3-Mediated Transport Independently of mTOR Kinase Inhibition: Implication in Assessing OATP1B1- and OATP1B3-Mediated Drug-Drug Interactions
Farasyn T, Crowe A, Hatley O, Neuhoff S, Alam K, Kanyo J, Lam T, Ding K, Yue W. Preincubation With Everolimus and Sirolimus Reduces Organic Anion-Transporting Polypeptide (OATP)1B1- and 1B3-Mediated Transport Independently of mTOR Kinase Inhibition: Implication in Assessing OATP1B1- and OATP1B3-Mediated Drug-Drug Interactions. Journal Of Pharmaceutical Sciences 2019, 108: 3443-3456. PMID: 31047942, PMCID: PMC6759397, DOI: 10.1016/j.xphs.2019.04.019.Peer-Reviewed Original Research
2018
Isoform-Level Interpretation of High-Throughput Proteomics Data Enabled by Deep Integration with RNA-seq
Carlyle B, Kitchen RR, Zhang J, Wilson R, Lam T, Rozowsky JS, Williams KR, Sestan N, Gerstein M, Nairn AC. Isoform-Level Interpretation of High-Throughput Proteomics Data Enabled by Deep Integration with RNA-seq. Journal Of Proteome Research 2018, 17: 3431-3444. PMID: 30125121, PMCID: PMC6392456, DOI: 10.1021/acs.jproteome.8b00310.Peer-Reviewed Original ResearchConceptsRNA-seqProteomic dataGene expressionLiquid chromatography-tandem mass spectrometry proteomicsTandem mass spectrometry proteomicsHigh-throughput proteomic dataTranscriptomic profiling methodsDistinct amino acid sequencesTranscript-level expressionAmino acid sequenceMass spectrometry proteomicsHEK293 cell culturesTranslatome dataMost genesProfound functional implicationsProtein isoformsAlternate isoformsGene productsAcid sequenceCellular controlBiosynthetic stateGeneration of peptidesCell typesFunctional relevanceFunctional implications
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
2016
Phosphoproteomic Analysis Reveals a Novel Mechanism of CaMKIIα Regulation Inversely Induced by Cocaine Memory Extinction versus Reconsolidation
Rich MT, Abbott TB, Chung L, Gulcicek EE, Stone KL, Colangelo CM, Lam TT, Nairn AC, Taylor JR, Torregrossa MM. Phosphoproteomic Analysis Reveals a Novel Mechanism of CaMKIIα Regulation Inversely Induced by Cocaine Memory Extinction versus Reconsolidation. Journal Of Neuroscience 2016, 36: 7613-7627. PMID: 27445140, PMCID: PMC4951572, DOI: 10.1523/jneurosci.1108-16.2016.Peer-Reviewed Original ResearchMeSH Keywords1-(5-Isoquinolinesulfonyl)-2-MethylpiperazineAmygdalaAnimalsBenzylaminesCalcium-Calmodulin-Dependent Protein Kinase Type 2CocaineConditioning, OperantCuesEnzyme InhibitorsExtinction, PsychologicalHEK293 CellsHumansMaleMemoryPhosphorylationProteomicsRatsRats, Sprague-DawleySelf AdministrationSerineSignal TransductionSulfonamidesConceptsRelapse-like behaviorMemory extinctionSubsequent cue-induced reinstatementAddiction treatmentDrug-associated memoriesCocaine-associated memoryCue-induced reinstatementRelapse prevention therapySelf-administer cocaineLong-term abstinenceReconsolidation disruptionAbstinence effortsAudiovisual cuesEssential therapeutic goalCocaine memoryMemory strengtheningAmygdala inhibitionDrug useReconsolidationExtinction enhancementAddictive disordersRelapse preventionMemoryCuesEnvironmental cues
2013
Palmitoylation of Superoxide Dismutase 1 (SOD1) Is Increased for Familial Amyotrophic Lateral Sclerosis-linked SOD1 Mutants*
Antinone SE, Ghadge GD, Lam TT, Wang L, Roos RP, Green WN. Palmitoylation of Superoxide Dismutase 1 (SOD1) Is Increased for Familial Amyotrophic Lateral Sclerosis-linked SOD1 Mutants*. Journal Of Biological Chemistry 2013, 288: 21606-21617. PMID: 23760509, PMCID: PMC3724620, DOI: 10.1074/jbc.m113.487231.Peer-Reviewed Original ResearchMeSH KeywordsAmyotrophic Lateral SclerosisAnimalsBlotting, WesternCell Line, TumorCell MembraneCysteineDisulfidesHEK293 CellsHumansLipoylationLuminescent ProteinsMass SpectrometryMiceMice, TransgenicMutationNeuronsOxidation-ReductionProtein Processing, Post-TranslationalSpinal CordSuperoxide DismutaseSuperoxide Dismutase-1ConceptsWild-type SOD1Familial amyotrophic lateral sclerosisSuperoxide dismutase 1Copper chaperoneCysteine mutagenesisReversible post-translational modificationAcyl-biotin exchangeDisulfide bondingPost-translational modificationsMass spectrometryWild-type superoxide dismutase 1PalmitoylationSOD1 maturationMotor neuron cell lineProtein structureSOD1 mutantsNeuron cell lineAmyotrophic lateral sclerosisZn-superoxide dismutaseHEK cellsResidues 6ChaperonesCell linesMutagenesisDismutase 1
2012
The Prolyl Isomerase Pin1 Targets Stem-Loop Binding Protein (SLBP) To Dissociate the SLBP-Histone mRNA Complex Linking Histone mRNA Decay with SLBP Ubiquitination
Krishnan N, Lam TT, Fritz A, Rempinski D, O'Loughlin K, Minderman H, Berezney R, Marzluff WF, Thapar R. The Prolyl Isomerase Pin1 Targets Stem-Loop Binding Protein (SLBP) To Dissociate the SLBP-Histone mRNA Complex Linking Histone mRNA Decay with SLBP Ubiquitination. Molecular And Cellular Biology 2012, 32: 4306-4322. PMID: 22907757, PMCID: PMC3486140, DOI: 10.1128/mcb.00382-12.Peer-Reviewed Original ResearchMeSH KeywordsCell CycleCell Line, TumorCell NucleusDown-RegulationHEK293 CellsHeLa CellsHistonesHumansMRNA Cleavage and Polyadenylation FactorsNIMA-Interacting Peptidylprolyl IsomeraseNuclear ProteinsPeptidylprolyl IsomeraseProtein Phosphatase 2RNA InterferenceRNA StabilityRNA, MessengerRNA, Small InterferingRNA-Binding ProteinsUbiquitinationConceptsStem-loop binding proteinHistone mRNADegradation of SLBPMRNA stabilityBinding proteinHistone mRNA stabilityRNA degradation machineryHistone mRNA decayS phaseProtein phosphatase 2AHistone mRNA degradationCore histone mRNAsExosome-mediated degradationDownregulation of Pin1Ubiquitin-proteasome systemMRNA 3' endsProlyl isomerase Pin1Phosphatase 2ADegradation machineryMRNA decayMRNA degradationProteasome systemIsomerase Pin1MRNA complexesUntranslated regionEndothelial 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 substrates