2024
Lipid osmosis, membrane tension, and other mechanochemical driving forces of lipid flow
Zhang Y, Lin C. Lipid osmosis, membrane tension, and other mechanochemical driving forces of lipid flow. Current Opinion In Cell Biology 2024, 88: 102377. PMID: 38823338, PMCID: PMC11193448, DOI: 10.1016/j.ceb.2024.102377.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsMembrane tensionLipid transportNonvesicular lipid transportLipid transfer proteinsOrganelle biogenesisLipid transferMembrane proteinsMembrane domainsLipid homeostasisBiological functionsLipid flowMembrane protein densityTransfer proteinMembrane regionsProtein densityProteinMembraneLipidBiogenesisOrganelles
2023
Force redistribution in clathrin-mediated endocytosis revealed by coiled-coil force sensors
Ren Y, Yang J, Fujita B, Jin H, Zhang Y, Berro J. Force redistribution in clathrin-mediated endocytosis revealed by coiled-coil force sensors. Science Advances 2023, 9: eadi1535. PMID: 37831774, PMCID: PMC10575576, DOI: 10.1126/sciadv.adi1535.Peer-Reviewed Original ResearchConceptsActin cytoskeletonPlasma membraneHuntingtin Interacting Protein 1Clathrin-mediated endocytosisCountless cellular processesEndocytic machineryCellular processesClathrin latticesProtein condensationCytoskeletonEnd4pProtein 1Membrane deformationPiconewton forcesEndocytosisVivo force measurementsMembranePiconewtonsClathrinMachineryProteinCoatMolecular scale
2018
Munc18-1 catalyzes neuronal SNARE assembly by templating SNARE association
Jiao J, He M, Port SA, Baker RW, Xu Y, Qu H, Xiong Y, Wang Y, Jin H, Eisemann TJ, Hughson FM, Zhang Y. Munc18-1 catalyzes neuronal SNARE assembly by templating SNARE association. ELife 2018, 7: e41771. PMID: 30540253, PMCID: PMC6320071, DOI: 10.7554/elife.41771.Peer-Reviewed Original ResearchConceptsSNARE assemblyMunc18-1Sec1/Munc18-family (SM) proteinsSM protein Munc18-1Membrane fusionMunc18-1 mutationsNeuronal SNARE assemblyFour-helix bundleC-terminal regionN-terminal regionSingle-molecule force spectroscopySNARE motifSm proteinsSynaptic SNAREsMunc18-3SNARE zipperingProtein mechanismsTemplate complexForce spectroscopySnareZipperingProteinAssemblyComplexesVps33Single-Molecule Optical Tweezers Study of Regulated SNARE Assembly
Ma L, Jiao J, Zhang Y. Single-Molecule Optical Tweezers Study of Regulated SNARE Assembly. Methods In Molecular Biology 2018, 1860: 95-114. PMID: 30317500, PMCID: PMC6441361, DOI: 10.1007/978-1-4939-8760-3_6.Peer-Reviewed Original ResearchConceptsSoluble N-ethylmaleimide-sensitive factor attachment protein receptorsSNARE assemblyHigh-resolution optical tweezersN-ethylmaleimide-sensitive factor attachment protein receptorsMembrane fusionFactor attachment protein receptorsOptical tweezers studiesNeuronal SNARE assemblyIntracellular membrane fusionAttachment protein receptorsOptical tweezersΑ-SNAPDetailed experimental protocolCellular compartmentsRegulatory proteinsProtein receptorsDifferent cellsSpatiotemporal resolutionProteinAssemblyFusion processManipulation approachTweezersExperimental approachFusion
2017
Single-molecule force spectroscopy of protein-membrane interactions
Ma L, Cai Y, Li Y, Jiao J, Wu Z, O'Shaughnessy B, De Camilli P, Karatekin E, Zhang Y. Single-molecule force spectroscopy of protein-membrane interactions. ELife 2017, 6: e30493. PMID: 29083305, PMCID: PMC5690283, DOI: 10.7554/elife.30493.Peer-Reviewed Original ResearchConceptsProtein-membrane interactionsC2 domainPlasma membraneMultiple C2 domainsSingle-molecule force spectroscopy approachSingle-molecule force spectroscopyOptical tweezersE-SytsUnprecedented spatiotemporal resolutionForce spectroscopyMembrane bindingMembrane fusionSingle proteinSynaptotagmin-1Biological processesEndoplasmic reticulumSpectroscopy approachLipid exchangeSynaptic vesiclesSynaptotagmin 2ProteinSilica beadsMechanical forcesHigh-resolution methodsSpatiotemporal resolution
2016
Single-Molecule Protein Folding Experiments Using High-Precision Optical Tweezers
Jiao J, Rebane AA, Ma L, Zhang Y. Single-Molecule Protein Folding Experiments Using High-Precision Optical Tweezers. Methods In Molecular Biology 2016, 1486: 357-390. PMID: 27844436, PMCID: PMC5508109, DOI: 10.1007/978-1-4939-6421-5_14.Peer-Reviewed Original ResearchConceptsOptical tweezersProtein complexesHigh-resolution optical tweezersSingle-molecule manipulationFolding of proteinsFundamental biological problemOptical trapSingle-molecule measurementsUnprecedented spatiotemporal resolutionThree-dimensional structureTweezersSingle proteinSpontaneous foldingDetailed protocolAmino acidsMolecule proteinProteinBiological problemsPowerful approachMechanical forcesFoldingSpatiotemporal resolutionEnergyTransition kineticsLinear chains
2009
Closing the Loop on Protein-DNA Interactions: Interplay Between Shape and Flexibility in Nucleoprotein Assemblies Having Implications for Biological Regulation
Levene S, Zhang Y. Closing the Loop on Protein-DNA Interactions: Interplay Between Shape and Flexibility in Nucleoprotein Assemblies Having Implications for Biological Regulation. The IMA Volumes In Mathematics And Its Applications 2009, 150: 195-212. DOI: 10.1007/978-1-4419-0670-0_10.Peer-Reviewed Original ResearchDNA loop formationProtein-DNA interactionsProtein-binding sitesArchitectural proteinsGene repressionLoop formationGene regulationProtein domainsDNA replicationDNA loopsNucleoprotein assembliesBiological regulationLac repressorBiological processesBiological importanceConformational flexibilityProteinEssential mechanistic aspectsDNARegulationSingle moleculesRepressorMechanistic aspectsDistant sitesRepression