Interactions of the COP9 Signalosome with the E3 Ubiquitin Ligase SCF <sup>TIR1</sup> in Mediating Auxin Response
Claus Schwechheimer(Yale University), Giovanna Serino(Yale University), Judy Callis(University of California, Davis), William L. Crosby(Plant Biotechnology Institute), Svetlana Lyapina(California Institute of Technology), Raymond J. Deshaies(California Institute of Technology), William M. Gray(Institut de Biologie Moléculaire et Cellulaire), Mark Estelle(Institut de Biologie Moléculaire et Cellulaire), Xing‐Wang Deng(Yale University)
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Abstract
The COP9 signalosome is an evolutionary conserved multiprotein complex of unknown function that acts as a negative regulator of photomorphogenic seedling development in Arabidopsis. Here, we show that plants with reduced COP9 signalosome levels had decreased auxin response similar to loss-of-function mutants of the E3 ubiquitin ligase SCFTIR1. Furthermore, we found that the COP9 signalosome and SCFTIR1 interacted in vivo and that the COP9 signalosome was required for efficient degradation of PSIAA6, a candidate substrate of SCFTIR1. Thus, the COP9 signalosome may play an important role in mediating E3 ubiquitin ligase-mediated responses.
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