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First published online September 6, 2002; 10.1105/tpc.003434

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The Plant Cell, Vol. 14, 2553-2563, October 2002, Copyright © 2002,
American Society of Plant Biologists

Multiple Ubiquitin Ligase–Mediated Processes Require COP9 Signalosome and AXR1 Function

Claus Schwechheimer1, Giovanna Serino and Xing-Wang Deng2

Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut 06520-8104

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

The COP9 signalosome (CSN) is an evolutionarily conserved multiprotein complex that mediates the repression of photomorphogenesis in the dark in Arabidopsis through the degradation of transcription factors such as HY5 and HYH. CSN-mediated HY5 and HYH degradation also requires the activity of the putative E3 ubiquitin ligase (E3) component COP1 and the E2-conjugating enzyme variant COP10. Recently, it was shown that CSN also is required for auxin responses mediated by the SCF-type E3 SCFTIR1. To determine whether Arabidopsis CSN is required for E3-mediated processes in a more general manner, we generated plants with reduced E3 function by suppressing AtRBX1, an essential core subunit of SCF-type E3s. We observed that AtRBX1 transgenic plants share multiple phenotypes with CSN reduced-function plants, such as morphological defects and reduced responses to auxin, jasmonic acid, and cold stress, suggesting that CSN is required for multiple AtRBX1-mediated processes. Furthermore, we observed that mutants with defects in AXR1, a protein that had been described only as a regulator of SCFTIR1 function, also is required for other E3-mediated processes and for the COP1/COP10/CSN-mediated repression of photomorphogenesis in the dark. We conclude that CSN and AXR1 are of general importance for different pathways that are controlled by E3-mediated protein degradation.




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