The Arabidopsis E3 ubiquitin ligase DOA10A promotes localization of abscisic acid (ABA) receptors to the membrane through mono-ubiquitination in ABA signaling

© 2024 The Author(s). New Phytologist © 2024 New Phytologist Foundation.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 245(2025), 1 vom: 01. Jan., Seite 169-182
1. Verfasser: Liu, Cuixia (VerfasserIn)
Weitere Verfasser: Li, Qingliang, Shen, Zhengwei, Xia, Ran, Chen, Qian, Li, Xiao, Ding, Yanglin, Yang, Shuhua, Serino, Giovanna, Xie, Qi, Yu, Feifei
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2025
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article ABA signaling Arabidopsis DOA10A E3 ubiquitin ligase ERAD mono‐ubiquitination Abscisic Acid 72S9A8J5GW Ubiquitin-Protein Ligases mehr... EC 2.3.2.27 Arabidopsis Proteins Receptors, Cell Surface
Beschreibung
Zusammenfassung:© 2024 The Author(s). New Phytologist © 2024 New Phytologist Foundation.
The endoplasmic reticulum-associated degradation (ERAD) system eliminates misfolded and short-lived proteins to maintain physiological homeostasis in the cell. We have previously reported that ERAD is involved in salt tolerance in Arabidopsis. Given the central role of the phytohormone abscisic acid (ABA) in plant stress responses, we sought to identify potential intersections between the ABA and the ERAD pathways in plant stress response. By screening for the ABA response of a wide array of ERAD mutants, we isolated a gain-of-function mutant, doa10a-1, which conferred ABA hypersensitivity to seedlings. Genetic and biochemical assays showed that DOA10A is a functional E3 ubiquitin ligase which, by acting in concert with specific E2 enzymes, mediates mono-ubiquitination of the ABA receptor, followed by their relocalization to the plasma membrane. This in turn leads to enhanced ABA perception. In summary, we report here the identification of a novel RING-type E3 ligase, DOA10A, which regulates ABA perception by affecting the localization and the activity of ABA receptors through their mono-ubiquitination
Beschreibung:Date Completed 05.12.2024
Date Revised 05.12.2024
published: Print-Electronic
Citation Status MEDLINE
ISSN:1469-8137
DOI:10.1111/nph.20224