CUL3 <sup>BPM</sup> E3 ubiquitin ligases regulate MYC2, MYC3, and MYC4 stability and JA responses
José Manuel Chico, Esther Lechner, Gemma Fernández‐Barbero, Esther Cañibano, Gloria García‐Casado, José M. Franco‐Zorrilla, Philippe Hammann, Ángel M. Zamarreño, José María García‐Mina, Vicente Rubio, Pascal Genschik, Roberto Solano
Abstract
The jasmonate (JA)-pathway regulators MYC2, MYC3, and MYC4 are central nodes in plant signaling networks integrating environmental and developmental signals to fine-tune JA defenses and plant growth. Continuous activation of MYC activity is potentially lethal. Hence, MYCs need to be tightly regulated in order to optimize plant fitness. Among the increasing number of mechanisms regulating MYC activity, protein stability is arising as a major player. However, how the levels of MYC proteins are modulated is still poorly understood. Here, we report that MYC2, MYC3, and MYC4 are targets of BPM (BTB/POZ-MATH) proteins, which act as substrate adaptors of CUL3-based E3 ubiquitin ligases. Reduction of function of CUL3 BPM in amiR-bpm lines, bpm235 triple mutants, and cul3ab double mutants enhances MYC2 and MYC3 stability and accumulation and potentiates plant responses to JA such as root-growth inhibition and MYC-regulated gene expression. Moreover, MYC3 polyubiquitination levels are reduced in amiR-bpm lines. BPM3 protein is stabilized by JA, suggesting a negative feedback regulatory mechanism to control MYC activity, avoiding harmful runaway responses. Our results uncover a layer for JA-pathway regulation by CUL3 BPM -mediated degradation of MYC transcription factors.