Vps2pVPS2p

Vps2p is a protein involved in the endosomal sorting pathway in yeast. It is a component of the ESCRT-III (Endosomal Sorting Complex Required for Transport III) machinery, which plays a crucial role in various cellular processes, including multivesicular body (MVB) formation, cargo sorting to lysosomes, and cytokinesis. Vps2p is a coiled-coil protein that polymerizes into helical filaments on the endosomal membrane. These filaments are thought to mediate the membrane deformation and scission events required for vesicle budding into the MVB lumen.

The ESCRT-III complex, of which Vps2p is a part, is a dynamic assembly of proteins that are recruited to the endosomal membrane in a stepwise manner. Vps2p interacts with other ESCRT-III components, such as Vps24p and Snf7p, to form functional complexes. These complexes are essential for the proper formation of MVBs, which are specialized endosomal compartments that sort ubiquitously ubiquitinated cargo for degradation in the lysosome. Defects in Vps2p function or assembly can lead to impaired MVB formation, leading to the accumulation of undegraded proteins and other cellular components.

Beyond MVB formation, Vps2p and the ESCRT-III machinery have also been implicated in other membrane remodeling events, including the abscission step of cytokinesis, where the plasma membrane is severed to separate daughter cells. Vps2p's ability to form ordered filaments and induce membrane curvature makes it a versatile component of the cell's membrane trafficking and remodeling toolkit. The study of Vps2p has provided significant insights into the mechanisms underlying endosomal sorting and other fundamental cellular processes.