2024
Cross-regulations of two connected domains form a mechanical circuit for steady force transmission during clathrin-mediated endocytosis
Ren Y, Yang J, Fujita B, Zhang Y, Berro J. Cross-regulations of two connected domains form a mechanical circuit for steady force transmission during clathrin-mediated endocytosis. Cell Reports 2024, 43: 114725. PMID: 39276354, PMCID: PMC11476202, DOI: 10.1016/j.celrep.2024.114725.Peer-Reviewed Original ResearchClathrin-mediated endocytosisF-actinActin cytoskeletonFission yeast Schizosaccharomyces pombeYeast Schizosaccharomyces pombeCell adhesion complexAdhesion complexesMembrane localizationPN forcesStable bindingEnd4pCross-regulationCytoskeletonActinEndocytosisMembraneBindingMechanical forcesTalinTransmission of forcesThatchForce transmissionDomainCellsFissionLipid 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
2017
Energetics, kinetics, and pathway of SNARE folding and assembly revealed by optical tweezers
Zhang Y. Energetics, kinetics, and pathway of SNARE folding and assembly revealed by optical tweezers. Protein Science 2017, 26: 1252-1265. PMID: 28097727, PMCID: PMC5477538, DOI: 10.1002/pro.3116.Peer-Reviewed Original ResearchConceptsSoluble N-ethylmaleimide-sensitive factor attachment protein receptorsSynaptic soluble N-ethylmaleimide-sensitive factor attachment protein receptorSNARE assemblyMembrane fusionSNARE complexN-ethylmaleimide-sensitive factor attachment protein receptorsFactor attachment protein receptorsFast calcium-triggered fusionAttachment protein receptorsHigh-resolution optical tweezersCalcium-triggered fusionC-terminal domainFour-helix bundleNeurotransmitter-containing vesiclesLinker domainPlasma membraneDomain associationProtein receptorsMolecular engineDifferent functionsPathwayAssemblyMembraneOptical tweezersSynaptic transmission