2025
High-resolution structures of Myosin-IC reveal a unique actin-binding orientation, ADP release pathway, and power stroke trajectory
Chavali S, Carman P, Shuman H, Ostap E, Sindelar C. High-resolution structures of Myosin-IC reveal a unique actin-binding orientation, ADP release pathway, and power stroke trajectory. Proceedings Of The National Academy Of Sciences Of The United States Of America 2025, 122: e2415457122. PMID: 40014570, PMCID: PMC11892617, DOI: 10.1073/pnas.2415457122.Peer-Reviewed Original ResearchConceptsN-terminal extensionATP bindingRegulating ATP bindingADP releaseClass I myosinsLever arm swingStructure of myosinCryo-EM structureHigh-resolution structuresMembrane-bound vesiclesActin interfaceMyosin superfamilyMyosin familyActin filamentsAbsence of ADPMembrane remodelingNucleotide pocketMotile behaviorMyo1cPlasma membraneBiological functionsActinCryo-EM dataMotor domainMyosinDendritic cell phagosomes recruit GRASP55 for export of antigen-loaded MHC molecules
Cebrian I, Dinamarca S, Rodríguez M, Priego E, Brouwers N, Barends M, Brunnberg J, Tampé R, Blanchard N, Sancho D, Malhotra V. Dendritic cell phagosomes recruit GRASP55 for export of antigen-loaded MHC molecules. Cell Reports 2025, 44: 115333. PMID: 39955774, PMCID: PMC11861518, DOI: 10.1016/j.celrep.2025.115333.Peer-Reviewed Original ResearchConceptsExogenous antigen presentationDendritic cellsAntigen presentationMHC moleculesBone marrow-derived dendritic cellsBone marrow-derived DCCD4<sup>+</sup> T cellsMHC-IActivated CD8<sup>+</sup>MHC class IIDendritic cell phagosomesMHC II moleculesCD8<sup>+</sup>Peptide-loaded MHC moleculesT cellsExogenous antigensMHC-IIClass IIAntigenEndocytic systemGRASP55Cell surfaceIntracellular transportPlasma membranePresentationTrogocytosis-mediated immune evasion in the tumor microenvironment
Kim J, Park S, Kim J, Kim Y, Yoon H, Rayhan B, Jeong J, Bothwell A, Shin J. Trogocytosis-mediated immune evasion in the tumor microenvironment. Experimental & Molecular Medicine 2025, 57: 1-12. PMID: 39741180, PMCID: PMC11799389, DOI: 10.1038/s12276-024-01364-2.Peer-Reviewed Original ResearchConceptsCD4 T cellsT cellsMajor histocompatibility complexTumor microenvironmentImmune evasionMechanisms of immune evasionAnti-tumor immunityImmune regulatory moleculesAntigen-presenting cellsImmune-regulatory moleculesCTLA-4Cell-to-cell interactionsDonor cellsHistocompatibility complexTrogocytosisRecipient cellsTumorMembrane lossMembrane moleculesRegulatory moleculesMicroenvironmentSurface localizationPlasma membraneCellsTrogoptosis
2024
Vesicle docking and fusion pore modulation by the neuronal calcium sensor Synaptotagmin-1
Tsemperouli M, Cheppali S, Rivera-Molina F, Chetrit D, Landajuela A, Toomre D, Karatekin E. Vesicle docking and fusion pore modulation by the neuronal calcium sensor Synaptotagmin-1. Biophysical Journal 2024 PMID: 39719826, DOI: 10.1016/j.bpj.2024.12.023.Peer-Reviewed Original ResearchVesicle dockingSynaptotagmin-1C2 domainFusion triggeringCalcium sensor synaptotagmin 1Neuronal SNARE complexFusion pore dynamicsSensor synaptotagmin-1Domains of Syt1Neuroendocrine cell linePolybasic patchSNARE complexTriggers exocytosisFusion poreFusion eventsDense-core vesiclesSyt1Synaptic vesiclesPlasma membranePore regulationCalcium sensorNegatively charged phospholipidsBind calciumPore dynamicsCell linesDNA-Assisted Assays for Studying Lipid Transfer Between Membranes
Wang Y, Shi Q, Yang Q, Yang Y, Bian X. DNA-Assisted Assays for Studying Lipid Transfer Between Membranes. Methods In Molecular Biology 2024, 2888: 221-236. PMID: 39699734, DOI: 10.1007/978-1-0716-4318-1_15.Peer-Reviewed Original ResearchConceptsSynaptotagmin-like mitochondrial lipid-binding proteinLipid transfer assaysFluorescence resonance energy transferEndoplasmic reticulumLipid transferPlasma membraneLipid-binding proteinsLipid transfer proteinsTransfer assayE-SytsExtended-synaptotagminsResonance energy transferLipid homeostasisReleased lipidsTransfer proteinProteinAssayMembraneLipidTransfer signalsReticulumHomeostasisEnergy transferPeriodic ER-plasma membrane junctions support long-range Ca2+ signal integration in dendrites
Benedetti L, Fan R, Weigel A, Moore A, Houlihan P, Kittisopikul M, Park G, Petruncio A, Hubbard P, Pang S, Xu C, Hess H, Saalfeld S, Rangaraju V, Clapham D, De Camilli P, Ryan T, Lippincott-Schwartz J. Periodic ER-plasma membrane junctions support long-range Ca2+ signal integration in dendrites. Cell 2024, 188: 484-500.e22. PMID: 39708809, DOI: 10.1016/j.cell.2024.11.029.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulum-plasma membrane junctionsEndoplasmic reticulum-plasma membranePlasma membrane of dendritesVoltage-gated Ca<sup>2+</sup> channelsER-plasma membrane junctionsMembrane of dendritesProtein kinase IIRyanodine receptorSynaptic inputsDendritic computationsSpine stimulationNeuronal dendritesKinase IIIntracellular signalingMembrane junctionsPlasma membraneER tubulesSignal propagationSignal transmissionSubcellular architectureRyanodineLadder-like arraysLocal activationReleaseDendritesConformational response of αIIbβ3 and αVβ3 integrins to force
Kolasangiani R, Farzanian K, Chen Y, Schwartz M, Bidone T. Conformational response of αIIbβ3 and αVβ3 integrins to force. Structure 2024, 33: 289-299.e4. PMID: 39706199, DOI: 10.1016/j.str.2024.11.016.Peer-Reviewed Original ResearchConceptsBind similar ligandsExtended conformationAvb3 integrinCellular mechanosensingAdhesion receptorsSubunit domainsCell mechanosensingPlasma membraneIntegrinMechanical signalsAll-atom simulationsSingle molecule measurementsConformational responseSubunitMechanosensingStructural dynamicsSolid tissuesCellsMolecule measurementsConformationAvb3Circulating plateletsEquivalent levelMembraneKv1.3 regulation of brain immune function in vitro and in vivo
Bowen C, Nguyen H, Lin Y, Bagchi P, Natu A, Xiao H, Espinosa‐Garcia C, Kumar P, Wulff H, Seyfried N, Rangaraju S. Kv1.3 regulation of brain immune function in vitro and in vivo. Alzheimer's & Dementia 2024, 20: e093042. PMCID: PMC11709668, DOI: 10.1002/alz.093042.Peer-Reviewed Original ResearchProtein processingN-terminusProximity-based proteomicsProtein-protein interactomePDZ-binding motifPDZ-binding domainPlasma membrane proteinsDeletion in vivoJurkat T cellsT cellsKO miceBiotin ligaseCMV-Cre miceRNA-seqTrafficking proteinsBiotinylated proteinsTranscriptome levelC-terminusMembrane proteinsInteractorsMicroglial signatureImmune signalingPlasma membraneLPS stimulationDifferential expressionEzrin drives adaptation of monocytes to the inflamed lung microenvironment
Gudneppanavar R, Di Pietro C, H Öz H, Zhang P, Cheng E, Huang P, Tebaldi T, Biancon G, Halene S, Hoppe A, Kim C, Gonzalez A, Krause D, Egan M, Gupta N, Murray T, Bruscia E. Ezrin drives adaptation of monocytes to the inflamed lung microenvironment. Cell Death & Disease 2024, 15: 864. PMID: 39613751, PMCID: PMC11607083, DOI: 10.1038/s41419-024-07255-8.Peer-Reviewed Original ResearchConceptsActivation of focal adhesion kinaseExtracellular matrixActin-binding proteinsFocal adhesion kinaseLung extracellular matrixKnock-out mouse modelProtein kinase signalingCortical cytoskeletonLoss of ezrinKinase signalingPlasma membraneCell migrationSignaling pathwayEzrinResponse to lipopolysaccharideTissue-resident macrophagesMouse modelLipopolysaccharideCytoskeletonEzrin expressionLung microenvironmentKinaseMonocyte recruitmentProteinAktSpatiotemporal control of subcellular O-GlcNAc signaling using Opto-OGT
Ong Q, Lim L, Goh C, Liao Y, Chan S, Lim C, Kam V, Yap J, Tseng T, Desrouleaux R, Wang L, Ler S, Lim S, Kim S, Sobota R, Bennett A, Han W, Yang X. Spatiotemporal control of subcellular O-GlcNAc signaling using Opto-OGT. Nature Chemical Biology 2024, 21: 300-308. PMID: 39543398, DOI: 10.1038/s41589-024-01770-7.Peer-Reviewed Original ResearchO-GlcNAc transferaseO-GlcNAcLocalized to specific subcellular sitesResponse to insulin stimulationPost-translational modification of intracellular proteinsModification of intracellular proteinsO-GlcNAc signalingPost-translational modificationsTargeting O-GlcNAc transferaseSpatiotemporal controlMulticellular organismsOGT activityOrganelle functionO-GlcNAcylationSubcellular sitesMTORC activitySignal transductionIntracellular proteinsNutrient-sensing signalsCell signalingInsulin stimulationPlasma membraneGene expressionRegulatory mechanismsAkt phosphorylationAntagonistic nanobodies implicate mechanism of GSDMD pore formation and potential therapeutic application
Schiffelers L, Tesfamariam Y, Jenster L, Diehl S, Binder S, Normann S, Mayr J, Pritzl S, Hagelauer E, Kopp A, Alon A, Geyer M, Ploegh H, Schmidt F. Antagonistic nanobodies implicate mechanism of GSDMD pore formation and potential therapeutic application. Nature Communications 2024, 15: 8266. PMID: 39327452, PMCID: PMC11427689, DOI: 10.1038/s41467-024-52110-1.Peer-Reviewed Original ResearchConceptsMembrane insertionGasdermin DN-terminal domainCleavage of gasdermin DPore formationPro-inflammatory caspasesPyroptosis to apoptosisActivated caspase-3Caspase-1 activationTarget membraneCaspase-3Assembled poresPlasma membraneCytosolic expressionLiving cellsConformational changesEnhanced caspase-1 activityOligomerizationPotential therapeutic applicationsInflammasome activationNanobodiesPyroptosisStudy pore formationMembraneTherapeutic applicationsA 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 membersParalogsCompetition and synergy of Arp2/3 and formins in nucleating actin waves
Le Chua X, San Tong C, Su M, Xǔ X, Xiao S, Wu X, Wu M. Competition and synergy of Arp2/3 and formins in nucleating actin waves. Cell Reports 2024, 43: 114423. PMID: 38968072, PMCID: PMC11378572, DOI: 10.1016/j.celrep.2024.114423.Peer-Reviewed Original ResearchActin wavesActin regulatory proteinsActin cytoskeletal networkConstitutively active mutantArp2/3 complexActin assemblyMonomeric actinActive Cdc42Cdc42-interactingCytoskeletal networkArp2/3Active mutantCellular processesRegulatory proteinsUpstream regulatorCdc42ActinPlasma membraneFMNL1Complex feedback loopsForminPhysiological stateDelayed recruitmentFeedback loopGTPaseMechano-inhibition of endocytosis sensitizes cancer cells to Fas-induced Apoptosis
Kural M, Djakbarova U, Cakir B, Tanaka Y, Chan E, Arteaga Muniz V, Madraki Y, Qian H, Park J, Sewanan L, Park I, Niklason L, Kural C. Mechano-inhibition of endocytosis sensitizes cancer cells to Fas-induced Apoptosis. Cell Death & Disease 2024, 15: 440. PMID: 38909035, PMCID: PMC11193792, DOI: 10.1038/s41419-024-06822-3.Peer-Reviewed Original ResearchConceptsFas-induced apoptosisCell surface Fas expressionDeath receptor FasInhibition of endocytosisSurface Fas expressionPlasma membrane tensionCancer cell apoptosisEndocytosis dynamicsApoptotic signalingReceptor FasGlioblastoma cell growthFas expressionPlasma membraneCell growthEndocytosisXenograft mouse modelSoluble FasLCell apoptosisFasApoptosisRho-kinase inhibitorCancer cellsMembrane tensionNonmalignant cellsInduce tumor regressionDual-Ring SNAREpin Machinery Tuning for Fast Synaptic Vesicle Fusion
Caruel M, Pincet F. Dual-Ring SNAREpin Machinery Tuning for Fast Synaptic Vesicle Fusion. Biomolecules 2024, 14: 600. PMID: 38786007, PMCID: PMC11117985, DOI: 10.3390/biom14050600.Peer-Reviewed Original ResearchEzrin drives adaptation of monocytes to the inflamed lung microenvironment.
Gudneppanavar R, Di Pietro C, Oez H, Zhang P, Huang P, Braga C, Tebaldi T, Biancon G, Kim C, Gonzalez A, Halene S, Krause D, Egan M, Gupta N, Murray T, Bruscia E. Ezrin drives adaptation of monocytes to the inflamed lung microenvironment. The Journal Of Immunology 2024, 212: 0078_5418-0078_5418. DOI: 10.4049/jimmunol.212.supp.0078.5418.Peer-Reviewed Original ResearchRNA-seqActin-binding protein ezrinF-actin distributionImmune response to bacteriaCystic fibrosisIn vitro functional studiesResponse to bacteriaIncreased expression of pro-inflammatory markersCytoskeleton rearrangementF-actinResponse to lung infectionExpressed genesProtein ezrinTranscriptional profilesExpression of pro-inflammatory markersPlasma membranePro-inflammatory markersFunctional studiesEzrinLung extracellular matrixCF miceExtracellular matrixWT micePI3K/Akt signalingLung infectionVolume microscopic analysis of membrane contact sites in mouse kidney renal proximal tubule epithelial cells
Pandya R, Pang S, Lackner E, Reyna-Neyra A, Li W, Sy K, Burdyniuk M, Weisz O, Xu C, Caplan M. Volume microscopic analysis of membrane contact sites in mouse kidney renal proximal tubule epithelial cells. Physiology 2024, 39: 1086. DOI: 10.1152/physiol.2024.39.s1.1086.Peer-Reviewed Original ResearchMembrane contact sitesProximal tubule epithelial cellsTubule epithelial cellsEndoplasmic reticulumEpithelial cellsContact sitesPlasma membraneER volumeRenal proximal tubule epithelial cellsFunction of membrane contact sitesVolume of endoplasmic reticulumProximal tubule cellsInter-organelle communicationBasal-lateral surfacesRenal epithelial cellsAdvanced imaging techniquesMedian volumeTubule cellsMale miceCell plasma membraneRenal cortexScanning electron microscopyFIB-SEMMouse kidneySmooth ERLow-input lipidomics reveals lipid metabolism remodelling during early mammalian embryo development
Zhang L, Zhao J, Lam S, Chen L, Gao Y, Wang W, Xu Y, Tan T, Yu H, Zhang M, Liao X, Wu M, Zhang T, Huang J, Li B, Zhou Q, Shen N, Lee H, Ye C, Li D, Shui G, Zhang J. Low-input lipidomics reveals lipid metabolism remodelling during early mammalian embryo development. Nature Cell Biology 2024, 26: 278-293. PMID: 38302721, DOI: 10.1038/s41556-023-01341-3.Peer-Reviewed Original ResearchConceptsMammalian preimplantation embryo developmentEmbryo developmentIn vitro blastocyst developmentPreimplantation embryo developmentEight-cell embryosMammalian early embryonic developmentMammalian embryo developmentDegree of phospholipid unsaturationEarly embryo developmentApical-basal polarityBlastocyst developmentBlastocyst stageLipid metabolism remodelingHuman early embryo developmentBlastocyst implantationRegulation of embryogenesisEarly embryonic developmentBlastocystLipid landscapeApical proteinsLipid desaturasesMetabolic remodelingCell signalingPlasma membraneLipid signaturesCompartment-specific regulation of NaV1.7 in sensory neurons after acute exposure to TNF-α
Tyagi S, Higerd-Rusli G, Ghovanloo M, Dib-Hajj F, Zhao P, Liu S, Kim D, Shim J, Park K, Waxman S, Choi J, Dib-Hajj S. Compartment-specific regulation of NaV1.7 in sensory neurons after acute exposure to TNF-α. Cell Reports 2024, 43: 113685. PMID: 38261513, PMCID: PMC10947185, DOI: 10.1016/j.celrep.2024.113685.Peer-Reviewed Original ResearchTNF-aSensory neuronsEffect of TNF-aSensory neuron excitabilityTumor necrosis factor-aRegulation of NaV1.7Voltage-gated sodiumPro-inflammatory cytokinesCompartment-specific effectsNeuronal plasma membraneSensitize nociceptorsNeuronal excitabilitySomatic membraneChannel N terminusElectrophysiological recordingsP38 MAPKIon channelsFactor AAcute exposureMolecular determinantsNeuronsAxonal endingsPhospho-acceptor sitesPlasma membraneCompartment-specific regulationElectrophysiology of fluoride channels in the yeasts Saccharomyces cerevisiae and Candida albicans
Rivetta A, Slayman C. Electrophysiology of fluoride channels in the yeasts Saccharomyces cerevisiae and Candida albicans. Methods In Enzymology 2024, 696: 3-24. PMID: 38658085, DOI: 10.1016/bs.mie.2024.01.005.Peer-Reviewed Original ResearchYeast Saccharomyces cerevisiaeOpportunistic human pathogenFree-living microorganismsSingle cellsPlasma membrane of single cellsYeast spheroplastsSaccharomyces cerevisiaeRegulation of moleculesCandida albicansHuman pathogensPlasma membraneCell wallExtracellular environmentMembrane of single cellsPatch-clamp techniqueOsmotic strengthYeastSpheroplastsCandidaFluoride channelsSmall cell volumeToxic moleculesCell membraneDiverse moleculesCell populations
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