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Arabidopsis BPM Proteins Function as Substrate Adaptors to a CULLIN3-Based E3 Ligase to Affect Fatty Acid Metabolism in Plants[W]
8 auth. Liyuan Chen, Joo Hyun Lee, H. Weber, Takayuki Tohge, Sandra Witt, S. Roje, ... A. Fernie, H. Hellmann
Plants regulate transcriptional processes to coordinate protein synthesis in response to environmental cues. Here it is shown that CULLIN3-based E3 ubiquitin ligases, which help mark proteins for degradation via the 26S proteasome, are key regulator…
Plants regulate transcriptional processes to coordinate protein synthesis in response to environmental cues. Here it is shown that CULLIN3-based E3 ubiquitin ligases, which help mark proteins for degradation via the 26S proteasome, are key regulators of processes involving ERF/AP2 transcription factors via the activity of MATH-BTB/POZ proteins, which affect metabolism and fatty acid content. Regulation of transcriptional processes is a critical mechanism that enables efficient coordination of the synthesis of required proteins in response to environmental and cellular changes. Transcription factors require accurate activity regulation because they play a critical role as key mediators assuring specific expression of target genes. In this work, we show that CULLIN3-based E3 ligases have the potential to interact with a broad range of ETHYLENE RESPONSE FACTOR (ERF)/APETALA2 (AP2) transcription factors, mediated by MATH-BTB/POZ (for Meprin and TRAF [tumor necrosis factor receptor associated factor] homolog)-Broad complex, Tramtrack, Bric-a-brac/Pox virus and Zinc finger) proteins. The assembly with an E3 ligase causes degradation of their substrates via the 26S proteasome, as demonstrated for the WRINKLED1 ERF/AP2 protein. Furthermore, loss of MATH-BTB/POZ proteins widely affects plant development and causes altered fatty acid contents in mutant seeds. Overall, this work demonstrates a link between fatty acid metabolism and E3 ligase activities in plants and establishes CUL3-based E3 ligases as key regulators in transcriptional processes that involve ERF/AP2 family members.
Published in The Plant Cell
2
 6 2013