The lysosome membrane is a new functional location for the ESCRTs in yeast.

ESCRT-III heteropolymers utilize non-specific lateral electrostatic interactions to recognize one another, which may enable the polymers to slide along one another and adapt to different curvatures.

Quantitative 3D lattice light sheet microscopy of unperturbed cells combined with electron tomography and acute loss of function experiments reveals how dynamic ESCRT-III/Vps4 assemblies succeed in reverse membrane budding on endosomes.

ULK3 is a kinase in the abscission checkpoint that temporarily inactivates ESCRT-III proteins via phosphorylation, which is required to delay cytokinesis in response to defects in mitosis.

ESCRT-driven mechanisms that sense and seal holes in the nuclear membranes directly monitor the nuclear transport system and the exposure of the inner nuclear membrane.

The release of Acb1 protein from yeast cells requires the ESCRT-III complex to stabilize the compartment for unconventional protein secretion (CUPS).

Building on previous work (Tang et al., 2015), novel ESCRT-III subunit Snf7 auto-activation mutants are used to reveal two parallel ubiquitin-dependent pathways during multivesicular endosome biogenesis.

Snf7 crystal structures reveal the mechanisms of ESCRT-III activation and polymerization into membrane-remodeling filaments.

Electron microscopy on native membranes reveals the shape and potential function of protein machinery responsible for budding vesicles and viruses away from the cytoplasm.

During viral assembly, ESCRTIII and VPS4 are recruited after most of the HIV-1 membrane is bent but disappear prior to scission of the virion from the cell.