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Plant Cell Advance Online Publication
Published on March 16, 2005; 10.1105/tpc.105.031989

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Received February 17, 2005
Accepted February 19, 2005

Arabidopsis Has Two Redundant Cullin3 Proteins That Are Essential for Embryo Development and That Interact with RBX1 and BTB Proteins to Form Multisubunit E3 Ubiquitin Ligase Complexes in Vivo

Pablo Figueroa 1, Giuliana Gusmaroli 1, Giovanna Serino 2, Jessica Habashi 1, Ligeng Ma 3, Yunping Shen 3, Suhua Feng 1, Magnolia Bostick 4, Judy Callis 4, Hanjo Hellmann 5, and Xing Wang Deng 1*

1 Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut 06520-8104
2 Dipartimento di Genetica e Biologia Molecolare, Universitá di Roma "La Sapienza," 00185 Rome, Italy
3 Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut 06520-8104; Peking-Yale Joint Center of Plant Molecular Genetics and Agrobiotechnology, College of Life Sciences, Peking University, Beijing 100871, China
4 Section of Biochemistry and Molecular Biology, University of California, Davis, California 95616
5 Institute for Biology/Applied Genetics, Freie Universität Berlin, 14195 Berlin, Germany

* To whom correspondence should be addressed. E-mail: xingwang.deng{at}yale.edu.

Cullin-based E3 ubiquitin ligases play important roles in the regulation of diverse developmental processes and environmental responses in eukaryotic organisms. Recently, it was shown in Schizosaccharomyces pombe, Caenorhabditis elegans, and mammals that Cullin3 (CUL3) directly associates with RBX1 and BTB domain proteins in vivo to form a new family of E3 ligases, with the BTB protein subunit functioning in substrate recognition. Here, we demonstrate that Arabidopsis thaliana has two redundant CUL3 (AtCUL3) genes that are essential for embryo development. Besides supporting anticipated specific AtCUL3 interactions with the RING protein AtRBX1 and representative Arabidopsis proteins containing a BTB domain in vitro, we show that AtCUL3 cofractionates and specifically associates with AtRBX1 and a representative BTB protein in vivo. Similar to the AtCUL1 subunit of the SKP1-CUL1-F-box protein-type E3 ligases, the AtCUL3 subunit of the BTB-containing E3 ligase complexes is subjected to modification and possible regulation by the ubiquitin-like protein Related to Ubiquitin in vivo. Together with the presence of large numbers of BTB proteins with diverse structural features and expression patterns, our data suggest that Arabidopsis has conserved AtCUL3-RBX1-BTB protein E3 ubiquitin ligases to target diverse protein substrates for degradation by the ubiquitin/proteasome pathway.




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