Other Publications (1)
Articles by Mijo Simunovic in JoVE
Trekke membran nanorør fra gigantiske Unilamellar blemmer Coline Prévost*1,2,3, Feng-Ching Tsai*1,4, Patricia Bassereau1,4, Mijo Simunovic1,5 1Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 2Department of Genetics and Complex Diseases, T. H. Chan School of Public Health, Harvard Medical School, 3Department of Cell Biology, Harvard Medical School, 4Sorbonne Universités, UPMC University Paris 06, 5Center for Studies in Physics and Biology, The Rockefeller University Mange proteiner i cellen forstand og indusere membran kurvatur. Vi beskriver en metode for å trekke membran nanorør fra lipid blemmer å studere samspillet av proteiner eller et kurvatur-aktiv molekyl med buet membraner i vitro.
Other articles by Mijo Simunovic on PubMed
How Curvature-generating Proteins Build Scaffolds on Membrane Nanotubes Proceedings of the National Academy of Sciences of the United States of America. | Pubmed ID: 27655892 Bin/Amphiphysin/Rvs (BAR) domain proteins control the curvature of lipid membranes in endocytosis, trafficking, cell motility, the formation of complex subcellular structures, and many other cellular phenomena. They form 3D assemblies that act as molecular scaffolds to reshape the membrane and alter its mechanical properties. It is unknown, however, how a protein scaffold forms and how BAR domains interact in these assemblies at protein densities relevant for a cell. In this work, we use various experimental, theoretical, and simulation approaches to explore how BAR proteins organize to form a scaffold on a membrane nanotube. By combining quantitative microscopy with analytical modeling, we demonstrate that a highly curving BAR protein endophilin nucleates its scaffolds at the ends of a membrane tube, contrary to a weaker curving protein centaurin, which binds evenly along the tube's length. Our work implies that the nature of local protein-membrane interactions can affect the specific localization of proteins on membrane-remodeling sites. Furthermore, we show that amphipathic helices are dispensable in forming protein scaffolds. Finally, we explore a possible molecular structure of a BAR-domain scaffold using coarse-grained molecular dynamics simulations. Together with fluorescence microscopy, the simulations show that proteins need only to cover 30-40% of a tube's surface to form a rigid assembly. Our work provides mechanical and structural insights into the way BAR proteins may sculpt the membrane as a high-order cooperative assembly in important biological processes.