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.

Cytoplasmic bodies sequester important abscission machinery to delay completion of cytokinesis in response to mitotic errors.

Biochemical, structural, imaging, and functional studies reveal how the ESCRT-III protein IST1 recruits the CAPN7 cysteine protease to midbodies, where its proteolytic activity is required for efficient abscission and NoCut checkpoint arrest.

A comprehensive, quantitative, protein-protein interaction screen maps the network of interactions between human MIT domains and ESCRT-III C-terminal tails, and reveals MIT domain-containing protein cofactors for abscission and the 'No Cut' abscission checkpoint.

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.

A plant peptide hormone controls organ shedding by acting as molecular glue that promotes the interaction between two membrane receptor kinases.

Building on previous work (Picco et al., 2015), we use a hybrid imaging approach to address the role of clathrin during endocytosis: we find that it has no role in shaping or elongating membrane invaginations, but it does contribute to the regularity of vesicle scission.

Rab25a and Rab25b mutant embryos exhibit epithelial spreading delays during morphogenesis and are characterized by cytokinesis defects leading to cell fusions, heterogeneous epithelial cell sizes, and reduced cortical actomyosin contractility.

Caveolae sense the membrane lipid composition, which influences their dynamic behavior at the cell surface.

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