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 stiffness
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
Loss of TMEM106B Ameliorates Lysosomal and Frontotemporal Dementia-Related Phenotypes in Progranulin-Deficient Mice
Klein ZA, Takahashi H, Ma M, Stagi M, Zhou M, Lam TT, Strittmatter SM. Loss of TMEM106B Ameliorates Lysosomal and Frontotemporal Dementia-Related Phenotypes in Progranulin-Deficient Mice. Neuron 2017, 95: 281-296.e6. PMID: 28728022, PMCID: PMC5558861, DOI: 10.1016/j.neuron.2017.06.026.Peer-Reviewed Original ResearchConceptsLysosomal protein levelsFrontotemporal lobar degenerationProtein levelsMultiple lysosomal enzymesLysosomal enzymesV0 subunitsTMEM106B geneProteomic analysisProgranulin-deficient miceExtent of neurodegenerationCommon neurodegenerative disorderLysosomal acidificationLysosomal enzyme levelsProtein 1Microglial accumulationRisk modificationFTLD riskBehavioral abnormalitiesRetinal degenerationNeurodegenerative disordersFrontotemporal dementiaGRNTMEM106BFunctional relationshipEnzyme levels
2015
Neuronal ceroid lipofuscinosis with DNAJC5/CSPα mutation has PPT1 pathology and exhibit aberrant protein palmitoylation
Henderson MX, Wirak GS, Zhang YQ, Dai F, Ginsberg SD, Dolzhanskaya N, Staropoli JF, Nijssen PC, Lam TT, Roth AF, Davis NG, Dawson G, Velinov M, Chandra SS. Neuronal ceroid lipofuscinosis with DNAJC5/CSPα mutation has PPT1 pathology and exhibit aberrant protein palmitoylation. Acta Neuropathologica 2015, 131: 621-637. PMID: 26659577, PMCID: PMC4791186, DOI: 10.1007/s00401-015-1512-2.Peer-Reviewed Original ResearchConceptsNeuronal ceroid lipofuscinosesProtein palmitoylationDisease pathwaysPalmitoyl-protein thioesterase 1Forms of NCLEnzyme palmitoyl-protein thioesterase 1Disease-associated proteinsCommon disease pathwaysNCL genesQuantitative proteomicsCSPα mutationsSpecific enzymatic activityCSPαFunctional linkNeuronal ceroid lipofuscinosisGlobal changePPT1Synaptic proteinsEnzymatic activityCeroid lipofuscinosesPalmitoylationGenesCeroid lipofuscinosisNeurodegenerative disordersProtein
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
2010
N-Glycosylation at the SynCAM (Synaptic Cell Adhesion Molecule) Immunoglobulin Interface Modulates Synaptic Adhesion*
Fogel AI, Li Y, Giza J, Wang Q, Lam TT, Modis Y, Biederer T. N-Glycosylation at the SynCAM (Synaptic Cell Adhesion Molecule) Immunoglobulin Interface Modulates Synaptic Adhesion*. Journal Of Biological Chemistry 2010, 285: 34864-34874. PMID: 20739279, PMCID: PMC2966101, DOI: 10.1074/jbc.m110.120865.Peer-Reviewed Original ResearchConceptsN-glycosylationTrans-synaptic interactionsN-glycansSite-specific N-glycansSynaptic cell adhesion molecule 1Site-specific N-glycosylationTrans-synaptic adhesionPost-translational modificationsSelect adhesion moleculesMutational studiesSynaptic adhesionGlycosylation sitesHeterophilic interactionsIg1 domainSynapse inductionPostsynaptic membraneAdhesion moleculesNeurobiological questionsSynaptic cleftStructural modelingPresynaptic terminalsDifferential mannerSialic acidCell adhesion molecule-1Adhesion
2005
Functional visualization of viral molecular motor by hydrogen-deuterium exchange reveals transient states
Lísal J, Lam TT, Kainov DE, Emmett MR, Marshall AG, Tuma R. Functional visualization of viral molecular motor by hydrogen-deuterium exchange reveals transient states. Nature Structural & Molecular Biology 2005, 12: 460-466. PMID: 15834422, DOI: 10.1038/nsmb927.Peer-Reviewed Original Research