The COP9 signalosome (CSN) is a conserved protein complex that regulates the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3ligase complexes [], which leads to a decrease in Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2 []. Protein kinases CK2 and D, which phosphorylate proteins such as cJun and p53 resulting in their degradation by the ubiquitin-26S proteasome system, also binds to CSN [, ]. The mammalian CSN typically consistis of eight subunits designated CSN1-CSN8. The fission yeast possesses a smaller version of the CSN, consisting only of six subunits, whereas a more distant CSN-like complex has been described in Saccharomyces cerevisiae [].This entry includes the COP9 signalosome complex (CSN) subunit 3 (CSN3). Interactions have been identified between CSN3 and IKKgamma, which prevents activation of transcription factor nuclear factor kappaB (NF-kappaB) []; and the Int-6 protein subunit of the eIF3 translation initiation factor [].
