Ring finger protein 157 (RNF157)

Ring finger protein 157 (RNF157) is a RING-type E3 ubiquitin ligase enzyme predominantly expressed in the brain and found throughout many tissues. RNF157 catalyzes the ubiquitination of target proteins, thereby targeting them for proteasomal degradation. It plays a pivotal role as a node integrating PI3K and MAPK oncogenic signal transduction with the molecular machinery governing cell cycle transitions through phosphorylation-dependent interactions with the APC/C activator CDH1, ensuring synchronized cell cycle progression, particularly in cancerous cells. RNF157 is also essential for neuronal survival and dendrite extension, acting partly through ubiquitination and degradation of substrates such as APBB1/Fe65 and HDAC1. It functions as a negative regulator of apoptosis and an important modulator of immune responses, especially in CD4+ T cell differentiation and Th17-dependent autoimmune disease. Its dysregulation has been implicated in cancer, neurodevelopmental/neurodegenerative conditions, and inflammatory/autoimmune diseases.

Other names

E3 ubiquitin ligase RNF157KIAA1917RING finger protein 157RING-type E3 ubiquitin transferase RNF157

For indirectly acting inhibitors: Inhibition of upstream kinases (PI3K, MEK, CDK2) alters RNF157 phosphorylation, modulating its ubiquitin ligase activity and resulting in cell cycle arrest and increased apoptosis in cancer cells. Hypothetical: Direct inhibitors of RNF157 E3 ligase activity would be expected to prevent ubiquitination/degradation of specific substrates (such as HDAC1 or APBB1), thereby altering cell cycle, apoptosis, or neuronal function.