2025
Visualizing nuclear pore complex plasticity with pan-expansion microscopy
Morgan K, Carley E, Coyne A, Rothstein J, Lusk C, King M. Visualizing nuclear pore complex plasticity with pan-expansion microscopy. Journal Of Cell Biology 2025, 224: e202409120. PMID: 40504117, PMCID: PMC12162248, DOI: 10.1083/jcb.202409120.Peer-Reviewed Original ResearchNup107 contributes to the maternal-to-zygotic transition by preventing the premature nuclear export of pri-miR427
Kostiuk V, Kabir R, Levangie K, Empke S, Morgan K, Owens N, Lusk C, Khokha M. Nup107 contributes to the maternal-to-zygotic transition by preventing the premature nuclear export of pri-miR427. Development 2025, 152: dev202865. PMID: 39791357, PMCID: PMC11829755, DOI: 10.1242/dev.202865.Peer-Reviewed Original ResearchConceptsMaternal transcriptsMaternal-to-zygotic transitionMaternal RNA clearanceZinc-finger transcription factorDegradation of maternal transcriptsEctodermal cell fatesMaternal-zygotic transitionNuclear pore complexNucleoporin functionZygotic transcriptionNuclear exportTranscript stabilityCell fateNuclear retentionTranscription factorsPore complexNup107TranscriptionEarly embryosRecognition sitesRNA clearanceGastrulationGerm layersTime course
2024
Channel width modulates the permeability of DNA origami–based nuclear pore mimics
Feng Q, Saladin M, Wu C, Cao E, Zheng W, Zhang A, Bhardwaj P, Li X, Shen Q, Kapinos L, Kozai T, Mariappan M, Lusk C, Xiong Y, Lim R, Lin C. Channel width modulates the permeability of DNA origami–based nuclear pore mimics. Science Advances 2024, 10: eadq8773. PMID: 39536094, PMCID: PMC11559598, DOI: 10.1126/sciadv.adq8773.Peer-Reviewed Original ResearchA-tisket, a-tasket, what a beautiful nuclear basket
Lusk C, King M. A-tisket, a-tasket, what a beautiful nuclear basket. Cell 2024, 187: 5225-5227. PMID: 39303690, DOI: 10.1016/j.cell.2024.08.030.Peer-Reviewed Original ResearchProtein folding and quality control during nuclear transport
Mallik S, Poch D, Burick S, Schlieker C. Protein folding and quality control during nuclear transport. Current Opinion In Cell Biology 2024, 90: 102407. PMID: 39142062, DOI: 10.1016/j.ceb.2024.102407.Peer-Reviewed Original ResearchProtein foldingNuclear transportCo-translational transportProtein-folding environmentAggregation of folding intermediatesProtein quality controlNuclear import machineryNuclear pore complexFolding environmentImport machineryNuclear importCytosolic aggregatesContext of neurological disordersNuclear compartmentPore complexProtein synthesisProteinQuality controlFoldingBarrier functionEvolution of transport systemsKaryopherinNucleoporinsCompartmentTemporal coordination
2023
An ESCRT grommet cooperates with a diffusion barrier to maintain nuclear integrity
Ader N, Chen L, Surovtsev I, Chadwick W, Rodriguez E, King M, Lusk C. An ESCRT grommet cooperates with a diffusion barrier to maintain nuclear integrity. Nature Cell Biology 2023, 25: 1465-1477. PMID: 37783794, PMCID: PMC11365527, DOI: 10.1038/s41556-023-01235-4.Peer-Reviewed Original ResearchConceptsSpindle pole body proteinNuclear envelope barrierESCRT-III proteinsNuclear pore complexSpindle pole bodyNucleocytoplasmic compartmentalizationESCRT functionPore complexPole bodyDistinct complementNuclear compartmentNuclear integrityTransport proteinsMolecular mechanismsRemodelling mechanismProteinBody proteinChanging the guard—nuclear pore complex quality control
Veldsink A, Gallardo P, Lusk C, Veenhoff L. Changing the guard—nuclear pore complex quality control. FEBS Letters 2023, 597: 2739-2749. PMID: 37715940, DOI: 10.1002/1873-3468.14739.Peer-Reviewed Original ResearchCoordinating nucleoporin condensation and nuclear pore complex assembly
Kuiper E, Prophet S, Schlieker C. Coordinating nucleoporin condensation and nuclear pore complex assembly. FEBS Letters 2023, 597: 2534-2545. PMID: 37620293, DOI: 10.1002/1873-3468.14725.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsNPC assemblyNuclear pore complexNuclear pore complex assemblyPore complex assemblyAberrant condensationNPC biogenesisAssembly machineryPore complexProtein complexesComplex assemblyRepeat nucleoporinsHuman disordersAmyotrophic lateral sclerosisAssemblyEukaryotesNucleoporinsBiogenesisRibosomesRecent progressProteasomeComplexesLateral sclerosisMachineryHomeostasisTherapeutic interventionsThe capsid lattice engages a bipartite NUP153 motif to mediate nuclear entry of HIV-1 cores
Shen Q, Kumari S, Xu C, Jang S, Shi J, Burdick R, Levintov L, Xiong Q, Wu C, Devarkar S, Tian T, Tripler T, Hu Y, Yuan S, Temple J, Feng Q, Lusk C, Aiken C, Engelman A, Perilla J, Pathak V, Lin C, Xiong Y. The capsid lattice engages a bipartite NUP153 motif to mediate nuclear entry of HIV-1 cores. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2202815120. PMID: 36943880, PMCID: PMC10068764, DOI: 10.1073/pnas.2202815120.Peer-Reviewed Original ResearchConceptsHIV-1 capsidC-terminal tail regionTriple arginine motifNuclear pore complexPhenylalanine-glycine motifsBipartite motifNuclear importPore complexNuclear poresNuclear entryNup153Capsid latticeInteraction moduleProtein latticeCA assemblyCA hexamersIntact capsidsNucleoporinsHIV-1 coreMotifCapsidTail regionIntact formInfection studiesMechanistic evidenceModeling HIV-1 nuclear entry with nucleoporin-gated DNA-origami channels
Shen Q, Feng Q, Wu C, Xiong Q, Tian T, Yuan S, Shi J, Bedwell G, Yang R, Aiken C, Engelman A, Lusk C, Lin C, Xiong Y. Modeling HIV-1 nuclear entry with nucleoporin-gated DNA-origami channels. Nature Structural & Molecular Biology 2023, 30: 425-435. PMID: 36807645, PMCID: PMC10121901, DOI: 10.1038/s41594-023-00925-9.Peer-Reviewed Original ResearchConceptsNuclear pore complexHIV-1 nuclear entryNuclear entryNuclear importNPC central channelPore complexHost nucleusCapsid dockingVirus genomeAffinity gradientNup153Central channelMechanistic insightsMolecular interactionsCapsidNucleoporinsNup358Nup62GenomeNucleusVirusDockingVirus-1 infectionImportComplexes
2022
Quality control mechanisms that protect nuclear envelope identity and function
Mannino PJ, Lusk CP. Quality control mechanisms that protect nuclear envelope identity and function. Journal Of Cell Biology 2022, 221: e202205123. PMID: 36036741, PMCID: PMC9442147, DOI: 10.1083/jcb.202205123.Peer-Reviewed Original ResearchConceptsNuclear pore complexQuality control mechanismsNuclear envelopeCellular degradative machineryNE integrityGenome stabilityPore complexMembrane remodelingDegradative machineryOuter membraneDistinct biochemistryBiochemical identityEndoplasmic reticulumAutophagy mechanismControl mechanismsSelective barrierPore membraneMembraneRecent workEukaryotesProteomeDeleterious effectsSpecializationMechanismMachineryNdc1 drives nuclear pore complex assembly independent of membrane biogenesis to promote nuclear formation and growth
Mauro MS, Celma G, Zimyanin V, Magaj MM, Gibson KH, Redemann S, Bahmanyar S. Ndc1 drives nuclear pore complex assembly independent of membrane biogenesis to promote nuclear formation and growth. ELife 2022, 11: e75513. PMID: 35852146, PMCID: PMC9296133, DOI: 10.7554/elife.75513.Peer-Reviewed Original ResearchConceptsNuclear pore complexNPC assemblyMembrane biogenesisNE formationNPC densityNuclear pore complex assemblyEndoplasmic reticulumPore complex assemblyNuclear growthPore complexNDC1Redundant rolesComplex assemblyNPC numberBiogenesisMembrane incorporationFast turnoverNuclear formationBilayer lipidsNup53Membrane synthesisFirst divisionAssemblyGrowthNup160The nucleoporin Gle1 activates DEAD-box protein 5 (Dbp5) by promoting ATP binding and accelerating rate limiting phosphate release
Gray S, Cao W, Montpetit B, De La Cruz EM. The nucleoporin Gle1 activates DEAD-box protein 5 (Dbp5) by promoting ATP binding and accelerating rate limiting phosphate release. Nucleic Acids Research 2022, 50: 3998-4011. PMID: 35286399, PMCID: PMC9023272, DOI: 10.1093/nar/gkac164.Peer-Reviewed Original ResearchConceptsNuclear pore complexRNA exportDEAD-box protein Dbp5ATPase cycleDbp5's ATPase activityDEAD (Asp-Glu-Ala-Asp) box protein 5Pore complexDbp5ATP bindingATPase cyclingNucleotide stateCytoplasmic faceGle1Pool of ATPADP-PiGene expressionProtein 5Mechanistic understandingNucleoporinsNup159ATPase activityATP dissociationATPPi releasePi release rateEmerging Connections between Nuclear Pore Complex Homeostasis and ALS
Chandra S, Lusk CP. Emerging Connections between Nuclear Pore Complex Homeostasis and ALS. International Journal Of Molecular Sciences 2022, 23: 1329. PMID: 35163252, PMCID: PMC8835831, DOI: 10.3390/ijms23031329.Peer-Reviewed Original ResearchConceptsNuclear pore complexNuclear envelopeQuality control pathwaysNuclear transport machineryNuclear transport receptorsQuality control mechanismsDipeptide repeat proteinsNew experimental avenuesNucleoporin proteinsRan GTPaseAmyotrophic lateral sclerosisTransport machineryPore complexRepeat proteinsSurveillance pathwayTransport receptorsRepeat RNANPC structureTransport proteinsControl pathwaysPatient neuronsComplex homeostasisHexanucleotide repeat expansionExperimental avenuesRepeat expansion
2021
Nuclear Import of HIV-1
Shen Q, Wu C, Freniere C, Tripler TN, Xiong Y. Nuclear Import of HIV-1. Viruses 2021, 13: 2242. PMID: 34835048, PMCID: PMC8619967, DOI: 10.3390/v13112242.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsDistinct roles of nuclear basket proteins in directing the passage of mRNA through the nuclear pore
Li Y, Aksenova V, Tingey M, Yu J, Ma P, Arnaoutov A, Chen S, Dasso M, Yang W. Distinct roles of nuclear basket proteins in directing the passage of mRNA through the nuclear pore. Proceedings Of The National Academy Of Sciences Of The United States Of America 2021, 118: e2015621118. PMID: 34504007, PMCID: PMC8449422, DOI: 10.1073/pnas.2015621118.Peer-Reviewed Original ResearchConceptsNuclear pore complexNuclear basket proteinsNative nuclear pore complexesCopy numberDistinct rolesExport routesSingle-molecule microscopyExport kineticsPore complexNative copyNuclear exportNuclear poresExact copy numberComposite proteinsNup153Live cellsMessenger RNASpecific functionsFull complementProteinSpecific mannerNup50Specific roleExport efficiencyRNADNA-Origami NanoTrap for Studying the Selective Barriers Formed by Phenylalanine-Glycine-Rich Nucleoporins
Shen Q, Tian T, Xiong Q, Fisher P, Xiong Y, Melia TJ, Lusk CP, Lin C. DNA-Origami NanoTrap for Studying the Selective Barriers Formed by Phenylalanine-Glycine-Rich Nucleoporins. Journal Of The American Chemical Society 2021, 143: 12294-12303. PMID: 34324340, PMCID: PMC8363578, DOI: 10.1021/jacs.1c05550.Peer-Reviewed Original ResearchConceptsNuclear pore complexFundamental biological activitiesRich nucleoporinsNuclear transport receptorsSelective barrierPhenylalanine-GlycineStructure-function relationshipsPore complexNuclear transportTransport receptorsProtein assembliesFG-NupsMolecular trafficFG interactionsFG networkBiomolecular machinesNucleoporinsCritical determinantDNA nanotechnologyBiomimetic constructsBiological activityDiffusion barrierModel cargoNanotrapsSpatial arrangementLimited Proteolysis-Coupled Mass Spectrometry Identifies Phosphatidylinositol 4,5-Bisphosphate Effectors in Human Nuclear Proteome
Sztacho M, Šalovská B, Červenka J, Balaban C, Hoboth P, Hozák P. Limited Proteolysis-Coupled Mass Spectrometry Identifies Phosphatidylinositol 4,5-Bisphosphate Effectors in Human Nuclear Proteome. Cells 2021, 10: 68. PMID: 33406800, PMCID: PMC7824793, DOI: 10.3390/cells10010068.Peer-Reviewed Original ResearchConceptsGene expressionHuman nuclear proteomeLimited proteolysisLabel-free quantitative mass spectrometryNuclear pore complexGene ontology analysisCell cycle regulationQuantitative mass spectrometryNuclear proteomeProtein effectorsPore complexPol IIRNA splicingOntology analysisMRNA splicingCycle regulationPIP2 bindingProtein interactionsDNA repairBioinformatics analysisNuclear envelopeFunctional domainsMass spectrometry identifiesSpecific proteinsCell cycle
2019
Quantification of Biomolecular Dynamics Inside Real and Synthetic Nuclear Pore Complexes Using Time-Resolved Atomic Force Microscopy
Stanley GJ, Akpinar B, Shen Q, Fisher PDE, Lusk CP, Lin C, Hoogenboom BW. Quantification of Biomolecular Dynamics Inside Real and Synthetic Nuclear Pore Complexes Using Time-Resolved Atomic Force Microscopy. ACS Nano 2019, 13: 7949-7956. PMID: 31241896, PMCID: PMC6660115, DOI: 10.1021/acsnano.9b02424.Peer-Reviewed Original ResearchConceptsNuclear pore complexAtomic force microscopyTransport barrierForce microscopyBiomolecular dynamicsPore complexNative nuclear pore complexesDynamics of biomoleculesNanometer length scaleDNA origami scaffoldMs temporal resolutionCollective transitionsMacromolecular trafficSelective gatewaySuch proteinsBiomolecular systemsOrigami scaffoldCohesive interactionsObserved dynamicsSuch experimentsTime scalesProteinBiological systemsLength scalesDrift correctionAn ESCRT-LEM protein surveillance system is poised to directly monitor the nuclear envelope and nuclear transport system
Thaller DJ, Allegretti M, Borah S, Ronchi P, Beck M, Lusk CP. An ESCRT-LEM protein surveillance system is poised to directly monitor the nuclear envelope and nuclear transport system. ELife 2019, 8: e45284. PMID: 30942170, PMCID: PMC6461442, DOI: 10.7554/elife.45284.Peer-Reviewed Original ResearchConceptsNuclear pore complexNPC assemblyNuclear membraneNuclear envelope barrierNuclear envelope herniationsNuclear envelope integrityNuclear transport systemXPO1/CRM1Membrane deliveryPore complexEnvelope integrityNuclear transportYeast modelNuclear poresChm7Nuclear envelopeFenestrated sheetHeh1Membrane disruptionMechanical membrane disruptionSelective barrierDisease mechanismsMembrane sealingTransport systemMembrane
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