Nathaniel Talledge

TL;DR: 4 angstrom resolution cryogenic electron microscopy reconstruction of a one-start, double-stranded helical copolymer composed of two different human ESCRT-III subunits, charged multivesicular body protein 1B (CHMP1B) and increased sodium tolerance 1 (IST1) suggests how common ESC RT-III filament architectures could stabilize different degrees and directions of membrane curvature.

TL;DR: Cryo-EM structures of human ESCRT-III proteins forming membrane-bound and membrane-free filaments show how a two-component, sequential polymerization mechanism drives membrane tubulation, constriction and bilayer thinning, leading to membrane fission.

TL;DR: The results suggest that the interactions between ESCRT-III filaments and the membrane could proceed through multiple interfaces, to provide assembly on membranes with various shapes, or adapt the orientation of the filaments towards the membrane during membrane remodeling.

TL;DR: It is shown that dynamin-mediated membrane fission is potently inhibited in vitro when an excess of endophilin co-assembles with dynamin around membrane tubules and intercalates between turns of the dynamin helix and impairs fission by preventing trans interactions between dynamin rungs that are thought to play critical roles in membrane constriction.

TL;DR: The structure raises the possibility that ESCRT-III proteins may form nucleic acid complexes in mammalian cells.