2023
Dynamic regulation of LINC complex composition and function across tissues and contexts
King M. Dynamic regulation of LINC complex composition and function across tissues and contexts. FEBS Letters 2023, 597: 2823-2832. PMID: 37846646, DOI: 10.1002/1873-3468.14757.Peer-Reviewed Original ResearchMeSH KeywordsCell NucleusCytoskeletonMechanotransduction, CellularMicrotubulesNuclear EnvelopeNuclear MatrixConceptsLINC complex componentsLINC complexLinker of nucleoskeletonProtein turnover mechanismsCytoplasmic intermediate filament networkIntermediate filament networkCytoskeleton (LINC) complexComplex componentsNuclear laminaCellular contextCytoplasmic cytoskeletonCell biologistsDynamic regulationNuclear envelopeRegulated expressionTurnover mechanismsFilament networkSplice variantsCell typesProtein configurationUnique functionCytoskeletonConcept of mechanotransductionComplexesNucleoskeletonAn 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 ResearchMeSH KeywordsAnaphaseEndosomal Sorting Complexes Required for TransportNuclear EnvelopeNuclear PoreSchizosaccharomycesConceptsSpindle pole body proteinNuclear envelope barrierESCRT-III proteinsNuclear pore complexSpindle pole bodyNucleocytoplasmic compartmentalizationESCRT functionPore complexPole bodyDistinct complementNuclear compartmentNuclear integrityTransport proteinsMolecular mechanismsRemodelling mechanismProteinBody protein
2019
Ablation of SUN2-containing LINC complexes drives cardiac hypertrophy without interstitial fibrosis
Stewart RM, Rodriguez EC, King MC. Ablation of SUN2-containing LINC complexes drives cardiac hypertrophy without interstitial fibrosis. Molecular Biology Of The Cell 2019, 30: 1664-1675. PMID: 31091167, PMCID: PMC6727752, DOI: 10.1091/mbc.e18-07-0438.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCardiomegalyCell AdhesionCell Nucleus ShapeDNA-Binding ProteinsFibrosisGene DeletionIntegrinsMAP Kinase Signaling SystemMembrane ProteinsMice, Inbred C57BLMice, KnockoutMultiprotein ComplexesMyocardiumNuclear EnvelopeProto-Oncogene Proteins c-aktSarcomeresTelomere-Binding ProteinsTransforming Growth Factor betaConceptsLINC complexType laminsInner nuclear membrane protein MAN1Nuclear envelopeA-type laminsSarcomeric contractile apparatusNuclear laminaDisease etiologyProfibrotic signalingCytoskeletal linkageAKT/MAPK signalingCardiomyocyte cytoskeletonPlasma membraneMAPK signalingNegative regulatorAntagonistic rolesTGFβ signalingLaminsCellular adhesionSignalingCardiac hypertrophySUN2Human cardiomyopathyHypertrophy markersContractile apparatus
2016
Improved Determination of Subnuclear Position Enabled by Three-Dimensional Membrane Reconstruction
Zhao Y, Schreiner SM, Koo PK, Colombi P, King MC, Mochrie SG. Improved Determination of Subnuclear Position Enabled by Three-Dimensional Membrane Reconstruction. Biophysical Journal 2016, 111: 19-24. PMID: 27410730, PMCID: PMC4945324, DOI: 10.1016/j.bpj.2016.05.036.Peer-Reviewed Original ResearchConceptsChromatin biologyLac operator arraysMembrane marker proteinsNuclear positionBroad practical utilityNuclear volumeNuclear peripheryOrganelle shapeChromatin markersTranscriptional regulationSubnuclear positionLacI-GFPDNA repairIndividual lociNuclear compartmentPopulation of cellsNuclear envelopeLocus positionParticular locusMarker proteinsImage analysis pipelineLociCell populationsAnalysis pipelineBiological accuracy
2015
The tethering of chromatin to the nuclear envelope supports nuclear mechanics
Schreiner SM, Koo PK, Zhao Y, Mochrie SG, King MC. The tethering of chromatin to the nuclear envelope supports nuclear mechanics. Nature Communications 2015, 6: 7159. PMID: 26074052, PMCID: PMC4490570, DOI: 10.1038/ncomms8159.Peer-Reviewed Original ResearchMeSH KeywordsCell NucleusChromatinMicroscopy, Electron, ScanningNuclear EnvelopeNuclear LaminaOptical TweezersSchizosaccharomycesConceptsNuclear mechanicsRole of chromatinOptical tweezersWild-type nucleiNetwork of lipidsCytoskeletal forcesNuclear laminaCytoskeletal dynamicsMechanical defensesMembrane tethersDeformable nucleiNuclear envelopeChromatinNuclear shapeIsolated nucleiIndividual mechanical contributionsMembrane resultsNucleusTweezersMechanicsLaminsProteinTetheringLaminaDefense
2014
A Role for Nuclear Envelope Bridging Complexes in Homology-Directed Repair
Swartz RK, Rodriguez EC, King MC. A Role for Nuclear Envelope Bridging Complexes in Homology-Directed Repair. Molecular Biology Of The Cell 2014, 25: mbc.e13-10-0569. PMID: 24943839, PMCID: PMC4142617, DOI: 10.1091/mbc.e13-10-0569.Peer-Reviewed Original ResearchConceptsDNA double-strand breaksHomology-directed repairRepair of DSBsNumber of genesDouble-strand breaksSame gene productCytoskeleton (LINC) complexLINC complexGenome instabilityATR kinaseGene conversionKms1DSB resectionGene productsDepolymerization of microtubulesCell cycleCytoplasmic microtubulesG2 phaseDNA damageSad1MicrotubulesComplexesNucleoskeletonMTO1Cytoskeleton
2008
A Network of Nuclear Envelope Membrane Proteins Linking Centromeres to Microtubules
King MC, Drivas TG, Blobel G. A Network of Nuclear Envelope Membrane Proteins Linking Centromeres to Microtubules. Cell 2008, 134: 427-438. PMID: 18692466, PMCID: PMC2617791, DOI: 10.1016/j.cell.2008.06.022.Peer-Reviewed Original ResearchConceptsSUN-KASH complexesNuclear membrane proteinsMembrane proteinsIntegral inner nuclear membrane proteinsSUN domain protein Sad1Nuclear envelopeSpindle pole body componentInner nuclear membrane proteinFission yeast S. pombeOuter nuclear membrane proteinsCytoplasmic microtubulesYeast S. pombeMicrotubule-dependent forcesNuclear envelope membranesCentromeric DNAS. pombeCentromeric heterochromatinHeterochromatic regionsEnvelope membraneIMA1MicrotubulesSad1HeterochromatinProteinNuclear heterochromatin
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