CBS9106-induced CRM1 degradation is mediated by cullin ring ligase activity and the
neddylation pathway.
Neddylation is a reversible post-translational protein modification whereby a small ubiquitin like protein (UBL), NEDD8 (neural precursor cell expressed developmentally downregulated protein (8), is attached to substrate proteins through a series of enzymatic reactions.
25) However, a recent report demonstrated that neddylation was increased during postnatal brain development, and this active post-translational modification in the synapse was shown to regulate the maturation, stability and function of dendritic spines in the brain.
These results suggest that the myelin paranode may be one of the regions where neddylation occurs, and this is influenced by paranodal junction formation and by the diameter of the nerves.
DCUN1D2 is a recently identified member of the DCNL family required for cullin neddylation in vivo.
Although NEDD8 was originally found in the embryonic mouse brain, (25) neddylation is now believed to have important roles in various cell functions in animals of all ages.
It has also been reported that bacteria elicit ROS generation in epithelial cells that inactivate the Ubc12 enzyme, preventing the
neddylation of cullin-1.
Source:RefSeq mRNA;Acc:NM_213801] ENSSSCG00000009425 laccase (multicopper oxidoreductase) domain containing 1 [Source:HGNC Symbol;Acc:26789] ENSSSCG00000009540 ligase IV, DNA, ATP-dependent [Source:HGNC Symbol;Acc:6601] ENSSSCG00000026536 DCN1, defective in cullin
neddylation 1, domain containing 2 [Source:HGNC Symbol;Acc:20328] ENSSSCG00000017142 BAI1-associated protein 2 [Source:HGNC Symbol;Acc:947] ENSSSCG00000017146 ring finger protein 213 [Source:HGNC Symbol;Acc:14539] ENSSSCG00000017169 SEC14-like 1 (S.
The remarkable pleiotropy of CSN is partially explained through its enzymatic activity towards Cullin-RING E3 ubiquitin ligases (CRLs), which are activated by
neddylation and inactivated by CSN-mediated deneddylation.
Expression of this miRNA was shown to promote proliferation by regulation of CAND1 [encoded by cullin-associated and
neddylation dissociated 1 (CAM51)] (49).
Phosphorylation of VACM-1/Cul5 by Protein Kinase A regulates its neddylation and antiproliferative effect.
The aim of this study was to determine if PKA-dependent phosphorylation of VACM-1/Cul5 controls its neddylation status, phosphorylation by PKC, and ultimately growth.
