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

被引:153
作者
Figueroa, P
Gusmaroli, G
Serino, G
Habashi, J
Ma, LG
Shen, YP
Feng, SH
Bostick, M
Callis, J
Hellmann, H
Deng, XW [1 ]
机构
[1] Yale Univ, Dept Mol Cellular & Dev Biol, New Haven, CT 06520 USA
[2] Univ Roma La Sapienza, Dipartimento Genet & Biol Mol, I-00185 Rome, Italy
[3] Peking Univ, Coll Life Sci, Peking Yale Joint Ctr Plant Mol Genet & Agrobiote, Beijing 100871, Peoples R China
[4] Univ Calif Davis, Sect Biochem & Mol Biol, Davis, CA 95616 USA
[5] Free Univ Berlin, Inst Biol Appl Genet, D-14195 Berlin, Germany
关键词
D O I
10.1105/tpc.105.031989
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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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页码:1180 / 1195
页数:16
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