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Article

DENEDDYLASE1 Protein Counters Automodification of Neddylating Enzymes to Maintain NEDD8 Protein Homeostasis in Arabidopsis.

The Journal of biological chemistry - 3 Mar 2017

Mergner Julia, Kuster Bernhard, Schwechheimer Claus

Abstract excerpt

In eukaryotes, the conjugation of the ubiquitin-like protein NEDD8 onto protein targets is an important post-translational modification. The best understood neddylation targets are the cullins, scaffold subunits of E3 ubiquitin ligases, where neddylation as well as deneddylation, facilitated by the protease activity of the CSN (COP9 signalosome), are required to control ubiquitin ligase assembly, function, and...

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Identifiers

PMID: 28096463
DOI: 10.1074/jbc.M116.767103
PMCID: PMC5339766

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NEDD8

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Research trail→

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DENEDDYLASE1 Protein Counters Automodification of Neddylating Enzymes to Maintain NEDD8 Protein Homeostasis in Arabidopsis.PMID 28096463Read ↗

DENEDDYLASE1 deconjugates NEDD8 from non-cullin protein substrates in Arabidopsis thaliana.Semantic proximity Read ↗

DEN1 deneddylates non-cullin proteins in vivo.Semantic proximity Read ↗

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AXR1-ECR1 and AXL1-ECR1 heterodimeric RUB-activating enzymes diverge in function in Arabidopsis thaliana.Semantic proximity Read ↗

Arabidopsis CAND1, an unmodified CUL1-interacting protein, is involved in multiple developmental pathways controlled by ubiquitin/proteasome-mediated protein Degradation.Semantic proximity Read ↗

Arabidopsis auxin-resistance gene AXR1 encodes a protein related to ubiquitin-activating enzyme E1.Semantic proximity Read ↗

The eta7/csn3-3 auxin response mutant of Arabidopsis defines a novel function for the CSN3 subunit of the COP9 signalosome.Semantic proximity Read ↗

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