CSNAP, the smallest CSN subunit, modulates proteostasis through cullin-RING ubiquitin ligases.The cullin-RING ubiquitin E3 ligase (CRL) family consists of ~250 complexes that catalyze ubiquitylation of proteins to achieve cellular regulation.  Here, we decouple the mechanisms using CSNAP, the recently discovered ninth subunit of the CSN.  We find that CSNAP reduces the affinity of CSN toward CRL complexes.  Removing CSNAP does not affect deneddylation, but leads to global effects on the CRL, causing altered reproductive capacity, suppressed DNA damage response, and delayed cell cycle progression.  Thus, although CSNAP is only 2% of the CSN mass, it plays a critical role in the steric regulation of CRLs by the CSN.
CSNAP
CSNAP, the smallest CSN subunit, modulates proteostasis through cullin-RING ubiquitin ligases.The cullin-RING ubiquitin E3 ligase (CRL) family consists of ~250 complexes that catalyze ubiquitylation of proteins to achieve cellular regulation.  Here, we decouple the mechanisms using CSNAP, the recently discovered ninth subunit of the CSN.  We find that CSNAP reduces the affinity of CSN toward CRL complexes.  Removing CSNAP does not affect deneddylation, but leads to global effects on the CRL, causing altered reproductive capacity, suppressed DNA damage response, and delayed cell cycle progression.  Thus, although CSNAP is only 2% of the CSN mass, it plays a critical role in the steric regulation of CRLs by the CSN.
CSNAP
CSNAP, the smallest CSN subunit, modulates proteostasis through cullin-RING ubiquitin ligases.The cullin-RING ubiquitin E3 ligase (CRL) family consists of ~250 complexes that catalyze ubiquitylation of proteins to achieve cellular regulation.  All CRLs are inhibited by the COP9 signalosome complex (CSN) through both enzymatic (deneddylation) and nonenzymatic (steric) mechanisms.  We find that CSNAP reduces the affinity of CSN toward CRL complexes.  Removing CSNAP does not affect deneddylation, but leads to global effects on the CRL, causing altered reproductive capacity, suppressed DNA damage response, and delayed cell cycle progression.  Thus, although CSNAP is only 2% of the CSN mass, it plays a critical role in the steric regulation of CRLs by the CSN.
CRL
CSNAP, the smallest CSN subunit, modulates proteostasis through cullin-RING ubiquitin ligases.The cullin-RING ubiquitin E3 ligase (CRL) family consists of ~250 complexes that catalyze ubiquitylation of proteins to achieve cellular regulation.  All CRLs are inhibited by the COP9 signalosome complex (CSN) through both enzymatic (deneddylation) and nonenzymatic (steric) mechanisms.  Here, we decouple the mechanisms using CSNAP, the recently discovered ninth subunit of the CSN.  We find that CSNAP reduces the affinity of CSN toward CRL complexes.  Removing CSNAP does not affect deneddylation, but leads to global effects on the CRL, causing altered reproductive capacity, suppressed DNA damage response, and delayed cell cycle progression.  Thus, although CSNAP is only 2% of the CSN mass, it plays a critical role in the steric regulation of CRLs by the CSN.
CSN
CSNAP, the smallest CSN subunit, modulates proteostasis through cullin-RING ubiquitin ligases.The cullin-RING ubiquitin E3 ligase (CRL) family consists of ~250 complexes that catalyze ubiquitylation of proteins to achieve cellular regulation.  All CRLs are inhibited by the COP9 signalosome complex (CSN) through both enzymatic (deneddylation) and nonenzymatic (steric) mechanisms.  Here, we decouple the mechanisms using CSNAP, the recently discovered ninth subunit of the CSN.  We find that CSNAP reduces the affinity of CSN toward CRL complexes.  Removing CSNAP does not affect deneddylation, but leads to global effects on the CRL, causing altered reproductive capacity, suppressed DNA damage response, and delayed cell cycle progression.  Thus, although CSNAP is only 2% of the CSN mass, it plays a critical role in the steric regulation of CRLs by the CSN.
CSN