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 transmissionDomainCellsFission
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
Molecular mechanisms of force production in clathrin‐mediated endocytosis
Lacy MM, Ma R, Ravindra NG, Berro J. Molecular mechanisms of force production in clathrin‐mediated endocytosis. FEBS Letters 2018, 592: 3586-3605. PMID: 30006986, PMCID: PMC6231980, DOI: 10.1002/1873-3468.13192.Peer-Reviewed Original Research
2014
Synergies between Aip1p and capping protein subunits (Acp1p and Acp2p) in clathrin-mediated endocytosis and cell polarization in fission yeast
Berro J, Pollard TD. Synergies between Aip1p and capping protein subunits (Acp1p and Acp2p) in clathrin-mediated endocytosis and cell polarization in fission yeast. Molecular Biology Of The Cell 2014, 25: 3515-3527. PMID: 25143407, PMCID: PMC4230613, DOI: 10.1091/mbc.e13-01-0005.Peer-Reviewed Original ResearchConceptsActin-depolymerizing factorActin filamentsFission yeastNew cellular functionsHeterodimeric capping proteinClathrin-mediated endocytosisActin filament barbedEndocytic patchesEndocytic sitesCellular functionsAip1pCapping proteinEndocytic vesiclesFilament barbedCapping activityPlasma membraneProtein subunitsActin meshworkCell polarizationIndependent pathwaysProteinEndocytosisYeastQuantitative microscopyFilamentsLocal and global analysis of endocytic patch dynamics in fission yeast using a new “temporal superresolution” realignment method
Berro J, Pollard TD. Local and global analysis of endocytic patch dynamics in fission yeast using a new “temporal superresolution” realignment method. Molecular Biology Of The Cell 2014, 25: 3501-3514. PMID: 25143395, PMCID: PMC4230612, DOI: 10.1091/mbc.e13-01-0004.Peer-Reviewed Original ResearchConceptsFission yeastEndocytic actin patchesWild-type cellsEndocytic patchesActin patchesQuantitative microscopyActin assemblyCellular processesVesicle movementEndocytic vesiclesInterphase cellsVesicle formationMolecular mechanismsPatch dynamicsYeastCell lengthGlobal analysisNumber of patchesMicroscopy moviesCellsClathrinEndocytosisNew toolValuable toolPatches