Adenosine monophosphate deaminase modulates BIN2 activity through hydrogen peroxide-induced oligomerization

Autor: Qing Lu, Anaxi Houbaert, Qian Ma, Jingjing Huang, Lieven Sterck, Cheng Zhang, René Benjamins, Frederik Coppens, Frank Van Breusegem, Eugenia Russinova
Rok vydání: 2022
Předmět:
Zdroj: The Plant Cell 34 (2022) 10
PLANT CELL
The Plant Cell, 34(10), 3844-3859
ISSN: 1532-298X
1040-4651
DOI: 10.1093/plcell/koac203
Popis: The Arabidopsis thaliana GSK3-like kinase, BRASSINOSTEROID-INSENSITIVE2 (BIN2) is a key negative regulator of brassinosteroid (BR) signaling and a hub for crosstalk with other signaling pathways. However, the mechanisms controlling BIN2 activity are not well understood. Here we performed a forward genetic screen for resistance to the plant-specific GSK3 inhibitor bikinin and discovered that a mutation in the ADENOSINE MONOPHOSPHATE DEAMINASE (AMPD)/EMBRYONIC FACTOR1 (FAC1) gene reduces the sensitivity of Arabidopsis seedlings to both bikinin and BRs. Further analyses revealed that AMPD modulates BIN2 activity by regulating its oligomerization in a hydrogen peroxide (H2O2)-dependent manner. Exogenous H2O2 induced the formation of BIN2 oligomers with a decreased kinase activity and an increased sensitivity to bikinin. By contrast, AMPD activity inhibition reduced the cytosolic reactive oxygen species (ROS) levels and the amount of BIN2 oligomers, correlating with the decreased sensitivity of Arabidopsis plants to bikinin and BRs. Furthermore, we showed that BIN2 phosphorylates AMPD to possibly alter its function. Our results uncover the existence of an H2O2 homeostasis-mediated regulation loop between AMPD and BIN2 that fine-tunes the BIN2 kinase activity to control plant growth and development. A mutation in the AMPD gene reduces the sensitivity of Arabidopsis seedlings to brassinosteroids by modulating BIN2 oligomerization and activity in a hydrogen peroxide-dependent manner.
Databáze: OpenAIRE