Journal
CURRENT OPINION IN PLANT BIOLOGY
Volume 45, Issue -, Pages 112-119Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.pbi.2018.05.017
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Funding
- Deutsche Forschungsgemeinschaft [SCHW751/11-1/SPP1365, Sonderforschungsbereich 924]
- EU Framework Program Horizon2020 [COST ACTION BM1307 PROTEOSTASIS]
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The ubiquitin-related protein NEDD8 is conjugated and deconjugated to and from proteins in processes related to ubiquitin conjugation and deconjugation. Neddylation is a well-studied posttranslational modification of Cullin-RING E3 ligases (CRLs). Biochemical and structural studies aiming at understanding the role of NEDD8 in CRL function have now resulted in a convincing model of how neddylation and deneddylation antagonistically regulate CRL stability, conformation, activity as well as degradation substrate receptor exchange. Studies of the Arabidopsis thaliana deneddylation-deficient den1 mutant led to the identification of many low abundant, non-Cullin NEDD8 conjugates. Examination of neddylated AUXIN RESISTANT1 (AXR1), a prominent neddylated protein in den1, suggests, however, that AXR1 neddylation may be an auto-catalytic side-reaction of Cullin-targeted neddylation and that DEN1 may serve to antagonize non-productive, auto-neddylation from substrates to provide free NEDD8 for CRL regulation.
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