CUL1 regulates TOC1 protein stability in the Arabidopsis circadian clock
Article first published online: 21 APR 2008
Journal compilation © 2008 Blackwell Publishing Ltd. No claim to original US government works
The Plant Journal
Volume 55, Issue 4, pages 568–579, August 2008
How to Cite
Harmon, F., Imaizumi, T. and Gray, W. M. (2008), CUL1 regulates TOC1 protein stability in the Arabidopsis circadian clock. The Plant Journal, 55: 568–579. doi: 10.1111/j.1365-313X.2008.03527.x
- Issue published online: 7 AUG 2008
- Article first published online: 21 APR 2008
- Received 17 December 2007; revised 27 March 2008; accepted 15 April 2008; published online 6 June 2008.
- circadian rhythms;
- post-translational regulation;
- ubiquitin ligase;
The circadian clock is the endogenous timer that coordinates physiological processes with daily and seasonal environmental changes. In Arabidopsis thaliana, establishment of the circadian period relies on targeted degradation of TIMING OF CAB EXPRESSION 1 (TOC1) by the 26S proteasome. ZEITLUPE (ZTL) is the F-box protein that associates with the SCF (Skp/Cullin/F-box) E3 ubiquitin ligase that is responsible for marking TOC1 for turnover. CULLIN1 (CUL1) is a core component of SCF complexes and is involved in multiple signaling pathways. To assess the contribution of CUL1-containing SCF complexes to signaling within the plant oscillator, circadian rhythms were examined in the recessive, temperature-sensitive CUL1 allele axr6-3. The activity of CUL1 in this mutant declines progressively with increasing ambient temperature, resulting in more severe defects in CUL1-dependent activities at elevated temperature. Examination of circadian rhythms in axr6-3 revealed circadian phenotypes comparable to those observed in ztl null mutants; namely, lengthened circadian period, altered expression of core oscillator genes, and limited degradation of TOC1. In addition, treatment of seedlings with exogenous auxin did not alter TOC1 stability. These results demonstrate that CUL1 is required for TOC1 degradation and further suggest that this protein is the functional cullin for the SCFZTL complex.