The Ubiquitin E3 Ligase RHA2b Promotes Degradation of MYB30 in Abscisic Acid Signaling

Plant Physiology
Yuan ZhengChancan Liao

Abstract

The phytohormone abscisic acid (ABA) is critical for plants encountering abiotic stress. We reported previously that the Arabidopsis (Arabidopsis thaliana) transcription factor MYB30 participates in ABA responses via SUMO ligase SAP-MIZ Domain-Containing SIZ1-mediated sumoylation. Here, we show that the RING-type ubiquitin E3 ligase RHA2b, which positively regulates ABA signaling, interacted with and ubiquitinated MYB30 to modulate MYB30 stability through the 26S proteasome pathway. The degradation rate of MYB30 was repressed significantly in the rha2b-1 mutant. Phenotypic analyses showed that MYB30 acts genetically downstream of RHA2b in ABA signaling. Substitutions of lysine-283 (K283) and K165 blocked ubiquitination, suggesting that these residues are sites of ubiquitination. K283 residue substitution significantly inhibited the degradation of MYB30 induced by ABA. The K165 site functioned additively with K283 in ABA-induced MYB30 degradation and ABA responses. At the same time, sumoylation protected MYB30 from degradation under cycloheximide and ABA treatment. Compared with MYB30, overexpression of MYB30-SUMO1 partially recovered the ABA sensitivity of siz1-2 But MYB30-SUMO1 exhibited similar localization with MYB30 in nucl...Continue Reading

Citations

May 23, 2020·International Journal of Molecular Sciences·Xinpeng ZhaoSuoping Li
Jun 12, 2020·BMC Plant Biology·Xiaohui QinChun-Peng Song
Jan 31, 2021·Plants·Paymon Doroodian, Zhihua Hua
Feb 3, 2021·The Plant Journal : for Cell and Molecular Biology·Fei XiaoHuapeng Zhou
Apr 3, 2021·International Journal of Biological Macromolecules·Shambhavi SharmaManoj Prasad
Apr 3, 2021·Frontiers in Plant Science·Katrina J LindenJudy Callis
May 1, 2021·International Journal of Molecular Sciences·Agnieszka SirkoMarzena Sieńko
Jul 3, 2021·International Journal of Molecular Sciences·Xiaopei WangYuan Zheng

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