2024
A-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 Research
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 ResearchThe 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 effectsSpecializationMechanismMachinery
2019
An 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
2014
Surveillance of Nuclear Pore Complex Assembly by ESCRT-III/Vps4
Webster BM, Colombi P, Jäger J, Lusk CP. Surveillance of Nuclear Pore Complex Assembly by ESCRT-III/Vps4. Cell 2014, 159: 388-401. PMID: 25303532, PMCID: PMC4194032, DOI: 10.1016/j.cell.2014.09.012.Peer-Reviewed Original ResearchConceptsNuclear pore complexNPC assemblyNuclear compartmentalizationIntegral inner nuclear membrane proteinsESCRT-III/Vps4Functional nuclear pore complexesNuclear pore complex assemblyInner nuclear membrane proteinPore complex assemblyNuclear membrane proteinsAAA ATPase Vps4LEM familyPore complexAssembly intermediatesMembrane proteinsLoss of compartmentalizationComplex assemblyNuclear envelopeComplex compartmentVps4CompartmentalizationCell functionContinuum of mechanismsAssemblySnf7
2006
Karyopherin-mediated import of integral inner nuclear membrane proteins
King MC, Lusk C, Blobel G. Karyopherin-mediated import of integral inner nuclear membrane proteins. Nature 2006, 442: 1003-1007. PMID: 16929305, DOI: 10.1038/nature05075.Peer-Reviewed Original ResearchConceptsIntegral membrane proteinsInner nuclear membraneINM proteinsMembrane proteinsIntegral inner nuclear membrane proteinsInner nuclear membrane proteinNuclear pore complex proteinsNuclear membrane proteinsRan GTPase cycleBasic sequence motifsNuclear localization signalNuclear pore complexPore complex proteinsAppropriate cellular compartmentDiscrete sequence elementsINM targetingLocalization signalPore complexGTPase cycleNuclear transportSequence motifsCellular compartmentsComplex proteinsSequence elementsKaryopherin β1