2024
Cellular stiffness sensing through talin 1 in tissue mechanical homeostasis
Chanduri M, Kumar A, Weiss D, Emuna N, Barsukov I, Shi M, Tanaka K, Wang X, Datye A, Kanyo J, Collin F, Lam T, Schwarz U, Bai S, Nottoli T, Goult B, Humphrey J, Schwartz M. Cellular stiffness sensing through talin 1 in tissue mechanical homeostasis. Science Advances 2024, 10: eadi6286. PMID: 39167642, PMCID: PMC11338229, DOI: 10.1126/sciadv.adi6286.Peer-Reviewed Original ResearchConceptsTissue mechanical homeostasisStiffness sensingExtracellular matrixTalin-1Mechanical homeostasisExtracellular matrix mechanicsIncreased cell spreadingCell spreadingTalinMutationsCellular sensingFibrillar collagenReduced axial stiffnessTissue mechanical propertiesMechanical propertiesAxial stiffnessCompliant substratesHomeostasisRupture pressureArp2/3ARPC5LStiffnessHomeostasis hypothesisResident cellsTissue stiffnessA 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
2023
Proteome-wide screening for mitogen-activated protein kinase docking motifs and interactors
Shi G, Song C, Torres Robles J, Salichos L, Lou H, Lam T, Gerstein M, Turk B. Proteome-wide screening for mitogen-activated protein kinase docking motifs and interactors. Science Signaling 2023, 16: eabm5518. PMID: 36626580, PMCID: PMC9995140, DOI: 10.1126/scisignal.abm5518.Peer-Reviewed Original ResearchConceptsMitogen-activated protein kinaseDocking motifSequence motifsDocking sequenceShort linear sequence motifsLinear sequence motifsSubstrate recruitmentHuman proteomeProtein kinaseCatalytic cleftExchange mutantsEssential functionsCultured cellsScreening pipelineWide screeningInteractorsMotifSequenceLimited repertoireSelective bindingInteractomeCombinatorial librariesMKK6ProteomeMKK7
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 kineticsProtein
2017
Mycobacterium tuberculosis universal stress protein Rv2623 interacts with the putative ATP binding cassette (ABC) transporter Rv1747 to regulate mycobacterial growth
Glass LN, Swapna G, Chavadi SS, Tufariello JM, Mi K, Drumm JE, Lam TT, Zhu G, Zhan C, Vilchéze C, Arcos J, Chen Y, Bi L, Mehta S, Porcelli SA, Almo SC, Yeh SR, Jacobs WR, Torrelles JB, Chan J. Mycobacterium tuberculosis universal stress protein Rv2623 interacts with the putative ATP binding cassette (ABC) transporter Rv1747 to regulate mycobacterial growth. PLOS Pathogens 2017, 13: e1006515. PMID: 28753640, PMCID: PMC5549992, DOI: 10.1371/journal.ppat.1006515.Peer-Reviewed Original ResearchConceptsPutative ATP-binding cassette transporterCassette transportersATP-binding cassette (ABC) transportersProtein-protein interactionsNon-phosphorylatable alanineVivo growth phenotypesHost-pathogen interactionsCell envelope componentsAffinity chromatography experimentsFHA domainPhosphorylated threonineMutant displaysTwo-hybridGrowth phenotypePutative ATPProtein modulesMutant proteinsPhosphorylated residuesMycobacterial growthBiological processesInositol mannosidesPIM expressionTransportersInteractsEnvelope components
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 cells
2013
Assembly of the SLIP1–SLBP Complex on Histone mRNA Requires Heterodimerization and Sequential Binding of SLBP Followed by SLIP1
Bansal N, Zhang M, Bhaskar A, Itotia P, Lee E, Shlyakhtenko LS, Lam TT, Fritz A, Berezney R, Lyubchenko YL, Stafford WF, Thapar R. Assembly of the SLIP1–SLBP Complex on Histone mRNA Requires Heterodimerization and Sequential Binding of SLBP Followed by SLIP1. Biochemistry 2013, 52: 520-536. PMID: 23286197, PMCID: PMC3580866, DOI: 10.1021/bi301074r.Peer-Reviewed Original ResearchCarrier ProteinsHistonesHumansKineticsMRNA Cleavage and Polyadenylation FactorsMutagenesis, Site-DirectedMutant ProteinsNuclear ProteinsPeptide FragmentsPhosphorylationPoint MutationProtein BindingProtein Interaction Domains and MotifsProtein MultimerizationProtein Processing, Post-TranslationalRecombinant ProteinsRNA FoldingRNA-Binding ProteinsRNA, MessengerSerineThreonineTyrosine
2006
Interaction of packaging motor with the polymerase complex of dsRNA bacteriophage
Lísal J, Kainov DE, Lam TT, Emmett MR, Wei H, Gottlieb P, Marshall AG, Tuma R. Interaction of packaging motor with the polymerase complex of dsRNA bacteriophage. Virology 2006, 351: 73-79. PMID: 16643976, DOI: 10.1016/j.virol.2006.03.025.Peer-Reviewed Original ResearchConceptsC-terminal faceP4 hexamersDsRNA bacteriophagesPackaging motorPolymerase complexHydrogen-deuterium exchangeSubunit interfaceProcapsidRNA loadingBiochemical studiesMolecular motorsEmpty capsidsHexamerViral capsidCapsidMass spectrometryGenomeDsRNAProcessivityBacteriophagesInteractionRegulationAssociates
2005
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
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