E3 ubiquitin-protein ligase RNF130 (RNF130)

E3 ubiquitin-protein ligase RNF130 is a membrane-bound ring finger protein that functions as an E3 ubiquitin ligase, mediating ubiquitination and degradation of target proteins, notably including the low-density lipoprotein receptor (LDLR), c-Myc, and regulators of apoptosis. It is structurally defined by a RING domain, a protease-associated domain, and a transmembrane segment. RNF130 regulates cellular processes such as apoptosis of hematopoietic cells, controls immune tolerance through T cell anergy, and modulates cell surface receptor abundance, impacting cholesterol homeostasis and fibrotic pathologies. It has been implicated as a tumor suppressor through epigenetic silencing in cancer and participates in metabolic reprogramming in fibrotic lung disease. RNF130 is encoded by the RNF130 gene and is also known by several aliases, including H-Goliath and Goliath homolog.

Other names

RNF130H-GoliathGOLIATHGPG1RZFPG1RPGoliath homologRING finger protein 130RING-type E3 ubiquitin transferase RNF130g1-related zinc finger protein

Post-translational ubiquitination. Drugs targeting RNF130 (hypothetically) would act by modulating ubiquitin-mediated degradation of its substrates, such as LDLR (to affect cholesterol levels), c-Myc (to affect cell proliferation), or proteins involved in apoptosis.