2023
Changing 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 Research
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
2021
Direct binding of ESCRT protein Chm7 to phosphatidic acid–rich membranes at nuclear envelope herniations
Thaller DJ, Tong D, Marklew CJ, Ader NR, Mannino PJ, Borah S, King MC, Ciani B, Lusk CP. Direct binding of ESCRT protein Chm7 to phosphatidic acid–rich membranes at nuclear envelope herniations. Journal Of Cell Biology 2021, 220: e202004222. PMID: 33464310, PMCID: PMC7816628, DOI: 10.1083/jcb.202004222.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceConserved SequenceEndosomal Sorting Complexes Required for TransportHydrophobic and Hydrophilic InteractionsLipid BilayersModels, BiologicalNuclear EnvelopeNuclear PorePhosphatidic AcidsProtein DomainsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsConceptsNuclear pore complex biogenesisNuclear membrane remodelingNuclear envelope herniationsLAP2-emerinNE remodelingNPC assemblyComplex biogenesisHydrophobic stretchMembrane remodelingChm7Nuclear envelopePA bindingPA metabolismFunctional importanceDirect bindingAmino acidsPhosphatidic acidMembraneBindingHeh1RecruitmentESCRTBiogenesisRemodelingYeast
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