Fas associated factor family member 2 (FAF2)

Fas associated factor family member 2 (FAF2) is a multifunctional, UBX domain-containing adaptor protein localized primarily to the endoplasmic reticulum and lipid droplets[2][3]. FAF2 participates in endoplasmic reticulum–associated degradation (ERAD) by interacting with ubiquitin ligase complexes and the segregase p97/VCP to extract misfolded proteins for proteasomal degradation[2][3]. It is also a sensor and regulator of unsaturated fatty acids, modulating triacylglycerol synthesis and lipid droplet formation[2][3]. FAF2 regulates peroxisomal homeostasis, controlling peroxisomal protein abundance—specifically ether lipid synthesis enzymes—upstream of classical peroxin genes, and influences the cellular response to saturated fatty acid toxicity via modulation of pexophagy (selective peroxisome autophagy)[1]. It may play a disease role in atopic dermatitis (where it is upregulated in T cells and eosinophils), metabolic lipotoxicity, and general cellular stress responses[2][3][4]. No approved drugs are currently directed at FAF2, but experimental modulation of autophagy (e.g., by Bafilomycin A1) can alter its functional consequences on peroxisomal and lipid metabolism[1].

Other names

FAS-associated factor 2UBXD8UBXN3BKIAA0887ETEAUBX domain-containing protein 3BUBX domain-containing protein 8UBX domain protein 3BUBX domain containing 8

Modulation of autophagy/pexophagy (as observed with Bafilomycin A1)[1]