Function
CSN-5 is a probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in a wide array of cellular and developmental processes. The CSN complex plays a critical role in regulating the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of cullin subunits within SCF-type E3 ligase complexes. This deneddylation process leads to a decrease in the Ubl ligase activity of SCF. Within the complex, CSN-5 likely serves as the catalytic center responsible for cleaving Nedd8 from cullins. However, it lacks metalloprotease activity on its own and requires the presence of other CSN complex subunits. The CSN complex is essential for proper embryogenesis and oogenesis, and it is required to maintain microtubule stability in early embryos. CSN-5 mediates the targeting of mei-3/katanin for degradation during the transition from meiosis to mitosis via deneddylation of cul-3. Additionally, CSN-5 may contribute to the stabilization of glh-1 protein levels by counteracting the effects of kgb-1.