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First published online July 14, 2006; 10.1105/tpc.106.043224

The Plant Cell 18:1991-2004 (2006)
© 2006 American Society of Plant Biologists

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tpc.106.043224v1
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Arabidopsis CULLIN4 Forms an E3 Ubiquitin Ligase with RBX1 and the CDD Complex in Mediating Light Control of Development

Haodong Chena,b, Yunping Shena,c, Xiaobo Tangd, Lu Yub, Jia Wangb, Lan Guoa,b, Yu Zhanga,b, Huiyong Zhangb, Suhua Fengb,c, Elizabeth Stricklandc, Ning Zhengd and Xing Wang Denga,b,c,1

a Peking–Yale Joint Center of Plant Molecular Genetics and Agrobiotechnology, College of Life Sciences, Peking University, Beijing 100871, China
b National Institute of Biological Sciences, Zhongguancun Life Science Park, Beijing 102206, China
c Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut 06520-8104
d Department of Pharmacology, University of Washington, Seattle, Washington 98195

1 To whom correspondence should be addressed. E-mail xingwang.deng{at}yale.edu; fax 203-432-5726.

Repression of photomorphogenesis in Arabidopsis thaliana requires activity of the COP9 signalosome (CSN), CDD, and COP1 complexes, but how these three complexes work in concert to accomplish this important developmental switch has remained unknown. Here, we demonstrate that Arabidopsis CULLIN4 (CUL4) associates with the CDD complex and a common catalytic subunit to form an active E3 ubiquitin ligase both in vivo and in vitro. The partial loss of function of CUL4 resulted in a constitutive photomorphogenic phenotype with respect to morphogenesis and light-regulated gene expression. Furthermore, CUL4 exhibits a synergistic genetic interaction with COP10 and DET1. Therefore, this CUL4-based E3 ligase is essential for the repression of photomorphogenesis. This CUL4-based E3 ligase appears to associate physically with COP1 E3 ligase and positively regulates the COP1-dependent degradation of photomorphogenesis-promoting transcription factors, whereas the CSN controls the biochemical modification of CUL4 essential for E3 activity. Thus, this study suggests a biochemical activity connection between CSN and CDD complexes in their cooperation with COP1 in orchestrating the repression of photomorphogenesis.




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