UV radiation resistance-associated gene protein (UVRAG)

UV radiation resistance-associated gene protein (UVRAG) is a multifunctional cytoplasmic protein originally identified for its ability to partially correct UV sensitivity in xeroderma pigmentosum cells. UVRAG contains several domains—proline-rich, C2, coiled-coil, CEP63-binding, and DNA-PK-binding—enabling its interaction with various molecular partners to regulate autophagy, endocytic trafficking, apoptosis (mainly through BAX sequestration), chromosome stability, DNA repair, and cellular development processes including organ rotation. UVRAG acts as a tumor suppressor; its mutation or loss is linked with enhanced tumorigenesis, chromosomal instability, and can drive the development of certain cancers and cardiomyopathies. As a regulatory subunit in autophagic and endocytic pathways, UVRAG controls vesicle trafficking through interaction with Beclin 1 and other protein complexes, often in connection with the PI3K complex and HOPS/SNARE machinery. It is not a classical drug target currently, but its central role in vital intracellular processes makes it a focus for research into therapy for diseases like cancer and failing heart

Other names

p63DHTXVPS38beclin 1 binding proteindisrupted in heterotaxyUV radiation resistance-associated gene protein

Drugs indirectly affect UVRAG by modulating autophagy, apoptosis, or pathways where UVRAG is a component (e.g., Beclin1-PI3KC3 pathway); direct pharmacological modulators are not yet established in mainstream therapeutics