Vacuolar protein sorting-associated protein 11 (VPS11)

Vacuolar protein sorting-associated protein 11 (VPS11) is a core component of both the CORVET and HOPS multisubunit tethering complexes, which are evolutionarily conserved and essential for vesicle fusion events in the endolysosomal system[1][2][3]. The class C core (VPS11 with VPS16, VPS18, and VPS33A) forms a structural backbone shared by both complexes, coordinating homotypic endosome fusion (via CORVET, involving Rab5) as well as late endosome-lysosome and autophagosome-lysosome fusion (via HOPS, involving Rab7)[1][2][3]. Functional deficiencies or mutations in VPS11 are associated with severe developmental and neurodegenerative diseases, including hypomyelination, leukoencephalopathy, and movement disorders[2][3]. In mammalian brain and other tissues, altered VPS11 expression and function can disrupt endolysosomal trafficking, myelin integrity, organelle assembly, and protein homeostasis[3][4]. No therapeutic drugs directly target VPS11, as its cellular role is structural/scaffold rather than as an enzyme, transporter, or receptor.

Other names

Vacuolar protein sorting 11VPS-11hVPS11