2024
Real-time imaging of axonal membrane protein life cycles
Tyagi S, Higerd-Rusli G, Akin E, Baker C, Liu S, Dib-Hajj F, Waxman S, Dib-Hajj S. Real-time imaging of axonal membrane protein life cycles. Nature Protocols 2024, 19: 2771-2802. PMID: 38831222, DOI: 10.1038/s41596-024-00997-x.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsMembrane proteinsRecycling of membrane proteinsProtein subcellular localizationMembrane protein homeostasisMembrane protein traffickingEngineered membrane proteinsMultiple membrane proteinsSelf-labeling tagsCell culturesProtein traffickingProtein tagsSubcellular localizationProtein homeostasisSpatiotemporal regulationCellular processesMultiple proteinsSubcellular distributionVesicular packagingThroughput mannerProteinNeuronal compartmentsDistal axonsProtein spatial organizationFluorescent labelingNeuronal cultures
2023
Pain-causing stinging nettle toxins target TMEM233 to modulate NaV1.7 function
Jami S, Deuis J, Klasfauseweh T, Cheng X, Kurdyukov S, Chung F, Okorokov A, Li S, Zhang J, Cristofori-Armstrong B, Israel M, Ju R, Robinson S, Zhao P, Ragnarsson L, Andersson Å, Tran P, Schendel V, McMahon K, Tran H, Chin Y, Zhu Y, Liu J, Crawford T, Purushothamvasan S, Habib A, Andersson D, Rash L, Wood J, Zhao J, Stehbens S, Mobli M, Leffler A, Jiang D, Cox J, Waxman S, Dib-Hajj S, Neely G, Durek T, Vetter I. Pain-causing stinging nettle toxins target TMEM233 to modulate NaV1.7 function. Nature Communications 2023, 14: 2442. PMID: 37117223, PMCID: PMC10147923, DOI: 10.1038/s41467-023-37963-2.Peer-Reviewed Original ResearchConceptsSensory neuronsVoltage-sensing domainNav channelsTransmembrane proteinAccessory proteinsVoltage-gated sodium channelsCritical regulatorPore domainChannel gatingExtracellular loopToxin-mediated effectsNeuronal excitabilityPeptide toxinsProteinSodium channelsPharmacological activitiesNav1.7 functionKnottin peptidesNeuronsImportant insightsToxinSubunitsRegulatorDomainExcelsa
2022
The fates of internalized NaV1.7 channels in sensory neurons: Retrograde cotransport with other ion channels, axon-specific recycling, and degradation
Higerd-Rusli G, Tyagi S, Liu S, Dib-Hajj F, Waxman S, Dib-Hajj S. The fates of internalized NaV1.7 channels in sensory neurons: Retrograde cotransport with other ion channels, axon-specific recycling, and degradation. Journal Of Biological Chemistry 2022, 299: 102816. PMID: 36539035, PMCID: PMC9843449, DOI: 10.1016/j.jbc.2022.102816.Peer-Reviewed Original ResearchConceptsMembrane proteinsIon channelsNeuronal functionDistinct neuronal compartmentsAxonal membrane proteinsRetrograde traffickingNeuronal polarityRecycling pathwayLate endosomesPlasma membraneSpecific proteinsAxonal traffickingNovel mechanismCell membraneSodium channel NaNeuronal compartmentsMultiple pathwaysLive neuronsVoltage-gated sodium channel NaProteinEndocytosisMembrane specializationsTraffickingMembraneChannel Na
2020
Cumulative hydropathic topology of a voltage‐gated sodium channel at atomic resolution
Xenakis M, Kapetis D, Yang Y, Heijman J, Waxman S, Lauria G, Faber C, Smeets H, Westra R, Lindsey P. Cumulative hydropathic topology of a voltage‐gated sodium channel at atomic resolution. Proteins Structure Function And Bioinformatics 2020, 88: 1319-1328. PMID: 32447794, DOI: 10.1002/prot.25951.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceArcobacterBacterial ProteinsBinding SitesHydrophobic and Hydrophilic InteractionsIon Channel GatingModels, MolecularProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsSodiumThermodynamicsVoltage-Gated Sodium ChannelsConceptsVoltage-gated sodium channelsBacterial channelsPhysiological cellular activitySodium channelsCellular activitiesCell membraneBiological poresPore stabilityAtomic resolutionBiophysical significanceMembrane surfaceHydropathicityGenesProteinMutationsWide spectrumMembraneFunctional architectureAccumulationComputational frameworkSodium ionsPores
2001
Glycosylation Alters Steady-State Inactivation of Sodium Channel Nav1.9/NaN in Dorsal Root Ganglion Neurons and Is Developmentally Regulated
Tyrrell L, Renganathan M, Dib-Hajj S, Waxman S. Glycosylation Alters Steady-State Inactivation of Sodium Channel Nav1.9/NaN in Dorsal Root Ganglion Neurons and Is Developmentally Regulated. Journal Of Neuroscience 2001, 21: 9629-9637. PMID: 11739573, PMCID: PMC6763018, DOI: 10.1523/jneurosci.21-24-09629.2001.Peer-Reviewed Original ResearchMeSH KeywordsAgingAnimalsAnimals, NewbornAntibody SpecificityAxotomyCell MembraneCells, CulturedFemaleGanglia, SpinalGlycosylationImmunoblottingMembrane PotentialsN-Acetylneuraminic AcidNAV1.9 Voltage-Gated Sodium ChannelNeuraminidaseNeuronsNeuropeptidesPatch-Clamp TechniquesRatsRats, Sprague-DawleySciatic NerveSodiumSodium ChannelsSubcellular FractionsTetrodotoxinTrigeminal GanglionConceptsImmunoreactive proteinMembrane fractionAdult DRG neuronsTranscription-PCR analysisHigh molecular weight immunoreactive proteinTheoretical molecular weightWhole-cell patch-clamp analysisLong transcriptsGlycosylation statePatch-clamp analysisAdult tissuesLarge proteinsLimited glycosylationEnzymatic deglycosylationExtensive glycosylationState of glycosylationProteinAdult dorsal root gangliaGlycosylationNative neuronsDevelopmental changesInactivationMembrane preparationsDRG neuronsDorsal root ganglia
1983
Myelin protein metabolism in demyelination and remyelination in the sciatic nerve
Smith M, Kocsis J, Waxman S. Myelin protein metabolism in demyelination and remyelination in the sciatic nerve. Brain Research 1983, 270: 37-44. PMID: 6871715, DOI: 10.1016/0006-8993(83)90789-8.Peer-Reviewed Original ResearchConceptsMyelin proteinsControl nervesLPC injectionSciatic nerveRight sciatic nerveSeries of ratsLeft nerveSchwann cellsNerveStructural myelin proteinsLPC treatmentFirst weekTime pointsAmino acid incorporationProtein metabolismLabeled amino acidsAcid incorporationMyelinDaysInjectionLysophosphatidylcholineDemyelinationRemyelinationProteinRats
1977
The clinical and physiological implications of hepatoma B12-binding proteins.
Waxman S, Liu C, Schreiber C, Helson L. The clinical and physiological implications of hepatoma B12-binding proteins. Cancer Research 1977, 37: 1908-14. PMID: 66988.Peer-Reviewed Original ResearchConceptsCell linesElevated sialyltransferase activityB12 binding capacitySerum B12Hepatocellular carcinomaHepatoma seraSialic acid contentNormal liverHepatoma cell lineB12Previous casesPatientsHepatomaPerfusateSialyltransferase activityLiverSerumPhysiological implicationsChemotherapyCarcinomaNeoplasiaProteinTumorsDisease