Vacuolar protein sorting-associated protein 53 subunit of Golgi-associated retrograde protein complex (VPS53)

VPS53 is a core subunit of the Golgi-associated retrograde protein (GARP) complex, a multisubunit tethering complex localized to the cytosolic face of the trans-Golgi network in eukaryotic cells. The GARP complex, which consists of VPS51, VPS52, VPS53, and VPS54, is essential for the tethering and fusion of endosome-derived vesicles with the trans-Golgi network, facilitating the recycling of proteins and maintaining proper Golgi function. VPS53 contains a C-terminal domain with tandem alpha-helical bundles that are critical for vesicle recognition and binding. Mutations or knockout of VPS53 lead to severe defects in protein trafficking, fragmentation of vacuoles, and abnormal glycosylation due to destabilization and mislocalization of Golgi enzymes[1][2][3]. While essential for basic cell physiology, VPS53 has not been directly established as a drug target or biomarker in human disease, but disruption of this pathway causes pronounced cellular dysfunction. Notes: - VPS53, as a subunit of the GARP complex, is not considered a canonical "therapeutic target" (such as a receptor, transporter, or enzyme) but is instead a core trafficking protein required for cell viability and protein homeostasis[1][3]. - No approved drugs target VPS53 directly, and no clinical mechanism-of-action or biomarker profiles exist for this molecule as a pharmacological target. - The entry is not incorrect or ambiguous but is not a conventional drug target by current therapeutic categorizations.

Other names

VPS53Vacuolar protein sorting 53Vps53p (yeast)Vps fifty-threeGolgi-associated retrograde protein complex subunit VPS53