Journal article
Arabidopsis BPM Proteins Function as Substrate Adaptors to a CULLIN3-Based E3 Ligase to Affect Fatty Acid Metabolism in Plants[W]
The Plant cell, Vol.25(6), pp.2253-2264
06/2013
Handle:
https://hdl.handle.net/2376/113443
PMCID: PMC3723624
PMID: 23792371
Abstract
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.
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Details
- Title
- Arabidopsis BPM Proteins Function as Substrate Adaptors to a CULLIN3-Based E3 Ligase to Affect Fatty Acid Metabolism in Plants[W]
- Creators
- Liyuan Chen - School of Biological Sciences, Washington State University, Pullman, Washington 99164Joo Hyun Lee - School of Biological Sciences, Washington State University, Pullman, Washington 99164Henriette Weber - Angewandte Genetik, Freie University, 14195 Berlin, GermanyTakayuki Tohge - Max-Planck Institute for Molecular Plant Physiology, 14476 Golm, GermanySandra Witt - Max-Planck Institute for Molecular Plant Physiology, 14476 Golm, GermanySanja Roje - Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164Alisdair R Fernie - Max-Planck Institute for Molecular Plant Physiology, 14476 Golm, GermanyHanjo Hellmann - School of Biological Sciences, Washington State University, Pullman, Washington 99164
- Publication Details
- The Plant cell, Vol.25(6), pp.2253-2264
- Academic Unit
- Biological Chemistry, Institute of; Biological Sciences, School of
- Publisher
- American Society of Plant Biologists
- Identifiers
- 99900547444201842
- Language
- English
- Resource Type
- Journal article