Zinc finger FYVE domain-containing protein 1 (ZFYVE1)

Zinc finger FYVE domain-containing protein 1 (ZFYVE1) is a phosphoinositide-binding protein characterized by two tandem FYVE-type zinc finger domains, which mediate specific binding to phosphatidylinositol 3-phosphate and recruitment to lipid-rich and membrane compartments such as the Golgi apparatus and endoplasmic reticulum[1][2][4][5]. ZFYVE1 participates in the formation and regulation of lipid droplets and endoplasmic reticulum-lipid droplet contacts, important for cellular lipid and energy homeostasis[1][4]. Functionally, it serves as a positive regulator and cofactor in the Toll-like receptor 3 (TLR3)-mediated innate immune response to viral double-stranded RNA by enhancing the ligand-binding capacity and signaling of TLR3[3]. ZFYVE1 is also hijacked during SARS-CoV-2 infection to facilitate replication organelle formation[1]. Variants in ZFYVE1 have been linked to rare pupillary function disorders, and there is evidence of its role in exacerbating certain inflammatory and antiviral responses, making it a potential target for research in infection, inflammation, and metabolic regulation[1][3]. Note: There are currently no approved drugs, biomarkers, or specific mechanism-of-action descriptions for drugs directly targeting ZFYVE1 in clinical use or clinical trials.

Other names

ZFYVE1DFCP1KIAA1589TAFF1ZNFN2A1PP10436PPP1R172Double FYVE-containing protein 1SR3Tandem FYVE fingers-1protein phosphatase 1 regulatory subunit 172phosphoinositide-binding protein SR3zinc finger protein subfamily 2A member 1ZFYVE1_HUMANKIAA1589[1]