BAK1-induced RPK1 phosphorylation is essential for RPK1-mediated cell death in Arabidopsis.

Being sessile, plants must deploy highly exquisite systems to respond to various internal and external signals for modulating growth and development throughout their lifespan. Many studies on Arabidopsis have shown that leucine-rich repeat-containing receptor-like kinases, including BRI1-associated receptor kinase 1 (BAK1) and receptor-like protein kinase 1 (RPK1), are suitable for such pleiotropic demands of plants. Previously, BAK1 and RPK1 were independently proven to be involved in the regulation of premature cell death. BAK1 inhibits spontaneous cell death and promotes defense-induced cell death. Meanwhile, RPK1 mediates reactive oxygen species (ROS) production through complexation with CaM4 and RbohF in an age-dependent manner. In the present study, RPK1-induced cell death and growth retardation were abolished both with respect to the phenotype and ROS production in bak1 mutants. Moreover, BAK1 interacts with RPK1 and mediates its unidirectional phosphorylation in plants. Further, BAK1-mediated RPK1 phosphorylation is indispensable for RPK1-CaM4 interaction, which is vital for ROS production, resulting in cell death. The presence of BAK1 enhanced the expression of cell death- and senescence-related genes, such as ORE1, PR1, SAG12, and SIRK in RPK1-mediated signaling cascades. Overall, in Arabidopsis, in addition to independent cell death regulation by BAK1 and RPK1, multiple-layers control cell death and premature senescence via the coordinated action of BAK1 and RPK1. Copyright © 2021 Elsevier Inc. All rights reserved.

Citation

Yun Shang, Dami Yang, Yunmi Ha, Kyoung Hee Nam. BAK1-induced RPK1 phosphorylation is essential for RPK1-mediated cell death in Arabidopsis. Biochemical and biophysical research communications. 2021 Oct 08;573:125-131

PMID: 34403809

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