Featured Publications
Actuating tension-loaded DNA clamps drives membrane tubulation
Liu L, Xiong Q, Xie C, Pincet F, Lin C. Actuating tension-loaded DNA clamps drives membrane tubulation. Science Advances 2022, 8: eadd1830. PMID: 36223466, PMCID: PMC9555772, DOI: 10.1126/sciadv.add1830.Peer-Reviewed Original ResearchConceptsDNA clampMembrane tubulationMembrane dynamicsMembrane-remodeling eventsVesicle tubulationConformational changesSpatiotemporal controlDNA signalsCell membraneDNA nanostructuresTubulationMembrane deformationClosed stateOpen stateSelf-assembled DNA nanostructuresOrganismsProteinMembrane tubeArtificial systemsTube widthMembraneDynamicsFunctionalized DNA-Origami-Protein Nanopores Generate Large Transmembrane Channels with Programmable Size-Selectivity
Shen Q, Xiong Q, Zhou K, Feng Q, Liu L, Tian T, Wu C, Xiong Y, Melia T, Lusk C, Lin C. Functionalized DNA-Origami-Protein Nanopores Generate Large Transmembrane Channels with Programmable Size-Selectivity. Journal Of The American Chemical Society 2022, 145: 1292-1300. PMID: 36577119, PMCID: PMC9852090, DOI: 10.1021/jacs.2c11226.Peer-Reviewed Original ResearchConceptsExchange of macromoleculesCholesterol-rich membranesHybrid nanoporesSynthetic biologyBiophysical toolsSynthetic cellsTransmembrane channelsTransmembrane nanoporesDNA ringsProtein nanoporeCell membraneBacterial toxinsDNA origami techniqueLipid membranesAnalytical chemistryMacromolecule sizeDNA origamiMembraneProgrammable sizeNanoporesSized poresNucleoporinsAverage inner diameterCellsPneumolysinPlacing and shaping liposomes with reconfigurable DNA nanocages
Zhang Z, Yang Y, Pincet F, Llaguno M, Lin C. Placing and shaping liposomes with reconfigurable DNA nanocages. Nature Chemistry 2017, 9: 653-659. PMID: 28644472, PMCID: PMC5542812, DOI: 10.1038/nchem.2802.Peer-Reviewed Original ResearchConceptsMembrane-bound vesiclesDNA cagesRegulated deformationsDNA nanocagesMembrane curvatureMembrane fusionConformational changesBiological membranesCell membraneLipid bilayer membranesMembrane mechanicsVesiclesDiverse structuresMembraneCellsBilayer membranesVersatile toolDelivery vesiclesToroid shapeLiposome shape
2021
FisB relies on homo-oligomerization and lipid binding to catalyze membrane fission in bacteria
Landajuela A, Braun M, Rodrigues CDA, Martínez-Calvo A, Doan T, Horenkamp F, Andronicos A, Shteyn V, Williams ND, Lin C, Wingreen NS, Rudner DZ, Karatekin E. FisB relies on homo-oligomerization and lipid binding to catalyze membrane fission in bacteria. PLOS Biology 2021, 19: e3001314. PMID: 34185788, PMCID: PMC8274934, DOI: 10.1371/journal.pbio.3001314.Peer-Reviewed Original ResearchConceptsMembrane fissionMembrane fission machineryMother cell membraneNegative-curvature lipidsMother cell cytoplasmUnique membrane topologyFission machineryMembrane scissionMembrane topologyLipid microdomainsMembrane necksFission proteinsLipid bindingMembrane curvatureFilamentous cellsBacillus subtilisFisBProtein BCell cytoplasmAcidic lipidsCell membraneCurvature sensingImmobile clustersIntrinsic abilityBacteria