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Comment
. 2003 Mar;15(3):580-1.
doi: 10.1105/tpc.150370.

Characterization of the last subunit of the Arabidopsis COP9 signalosome

Nancy A Eckardt  1
Affiliations
Comment

Characterization of the last subunit of the Arabidopsis COP9 signalosome

Nancy A Eckardt. Plant Cell. 2003 Mar.
No abstract available

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Figures

Figure 1.
Figure 1.
Model of CSN Function. The CSN is thought to interact with CUL1 of SCFTIR1 E3 ubiquitin ligase (and with cullin subunits of other E3 ligases) and to regulate E3 ligase activity via deneddylation, or removal of the ubiquitin-like molecule RUB1/NEDD8 (orange circles). SCFTIR1 E3 is made up of four subunits: RBX1, CUL1, ASK1, and the F-box protein TIR1, which is responsible for E3 ligase substrate recognition and the transfer of ubiquitin (gray circles) from the E2 ubiquitin-conjugating enzyme to the substrate. E2 is conjugated to ubiquitin that is activated by the E1 ubiquitin-activating enzyme. Also shown in this model is the interaction of AUX/IAA proteins, which are transcriptional regulators of auxin-responsive genes, with SCFTIR1. Auxin induces the transcription of AUX/IAA proteins and also enhances their degradation via SCFTIR1-mediated interactions, thus modulating the expression of downstream auxin-responsive genes in a complex interplay of protein synthesis and degradation (reviewed by Kepinsky and Leyser, 2002). AXR1 and ECR1 are subunits of an E1-like RUB1-activating enzyme that activates RUB1/NEDD8, which subsequently binds to the E2-like protein RCE1, and promotes the neddylation of CUL1. 2, 5, and 6 designate respective CSN subunits. (Figure courtesy of G. Serino and X.W. Deng.)
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References

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