Vps24

Vps24 is a conserved eukaryotic protein that serves as a core component of the ESCRT-III complex, a collection of proteins responsible for membrane remodeling and scission in various cellular processes. In yeast, Vps24p participates in endosomal sorting and the formation of intralumenal vesicles within multivesicular bodies (MVBs). In metazoans, the closest homologs are CHMP family proteins, with CHMP3 being a recognized counterpart to Vps24 in the ESCRT-III system.

Functionally, Vps24 acts as part of a dynamic polymer that assembles on endosomal membranes to drive membrane scission events. It cooperates with other ESCRT-III subunits and is involved in the biogenesis of MVBs, cytokinesis, and the budding of certain enveloped viruses. The protein is typically recruited to membranes where it forms filaments or lattice structures and subsequently interacts with the VPS4 ATPase, which powers disassembly and turnover of ESCRT-III complexes after membrane remodeling.

Structure and localization approaches indicate that Vps24 is a small, cytosolic protein that adopts coiled-coil–rich configurations enabling oligomerization. It is broadly expressed across tissues in higher eukaryotes and is highly conserved, reflecting its essential role in the ESCRT-III–mediated pathways.

Clinical and research relevance centers on the ESCRT pathway’s involvement in endosomal sorting, cell division, and viral budding. Disruptions to Vps24 function can impair MVB formation and cytokinesis, and studying its interactions helps elucidate the broader mechanisms of membrane remodeling in cells.