Target intelligence / Profile preview

Vacuolar protein sorting-associated protein 8 homolog (VPS8)

Target
VPS8
Molecular classification
Other (CORVET complex subunit/tethering complex subunit; HOPS/CORVET family), Peripheral membrane protein
01

Overview

Vacuolar protein sorting-associated protein 8 homolog (VPS8) is a **CORVET complex-specific subunit** that functions as a peripheral membrane protein crucial for membrane tethering and fusion within the endolysosomal system[1][2]. VPS8 directly interacts with Rab GTPases (particularly the Rab5 homolog Vps21) and other CORVET core proteins, playing a central role in clustering late endosomal membranes and regulating multivesicular body (MVB) biogenesis[2]. It is distinguished by additional α-helical regions that enable its unique conformation and interactions with core complex subunits, notably Vps11[1]. Proper balance between VPS8 and HOPS complex-specific subunits (like VPS41) governs functional assembly of tethering complexes, impacting endosome maturation, autophagy, and lysosomal fusion routes[3][4]. Overexpression or mutation of VPS8 can disrupt these trafficking events, but VPS8 is not itself targeted by approved drugs and is not currently used as a biomarker or therapeutic target in clinical medicine[1][2][3][4].

Other names
VPS8KIAA0804FLJ32099CORVET complex subunitVacuolar protein sorting-associated protein 8 homologVacuolar protein sorting 8 homolog
02

Biological functions

Endosomal membrane tetheringMultivesicular body (MVB) biogenesisEndosome maturation/fusionCooperation with Rab GTPases (Rab5 homologs) for vesicle clustering and fusion[2]Negative regulation of HOPS complex assembly[1][3][4]Involvement in endocytic transport and vesicle sorting[1][2][3][4]Regulation of autophagic vesicle fusion/trafficking (via competition with HOPS)[3][4]
03

Disease associations

Other (Defects in VPS8/CORVET function lead to abnormal endosome maturation and autophagy; reported in model organisms, but no direct human disease associations widely recognized in literature[3][4])Possibly relevant in lysosomal storage, neurodegeneration, or cancer by indirect modulation of endosomal trafficking (speculative; not directly reported in provided sources)

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