Phosphorylation-dependent routing of RLP44 towards brassinosteroid or phytosulfokine signalling

Plants rely on cell surface receptors to integrate developmental and environmental cues into behaviour adapted to the conditions. The largest group of these receptors, leucine-rich repeat receptor-like kinases, form a complex interaction network that is modulated and extended by receptor-like proteins. This raises the question of how specific outputs can be generated when receptor proteins are engaged in a plethora of promiscuous interactions. RECEPTOR-LIKE PROTEIN 44 (RLP44) acts to promote both brassinosteroid and phytosulfokine signalling, which orchestrate diverse cellular responses. However, it is unclear how these activities are coordinated. Here, we show that RLP44 is phosphorylated in its highly conserved cytosolic tail and that this post-translational modification governs its subcellular localization. Whereas phosphorylation is essential for brassinosteroid-associated functions of RLP44, its role in phytosulfokine signalling is not affected by phospho-status. Detailed mutational analysis suggests that phospho-charge, rather than modification of individual amino acids determines routing of RLP44 to its target receptor complexes, providing a framework to understand how a common component of different receptor complexes can get specifically engaged in a particular signalling pathway.

Automated summary

Plants rely on cell surface receptors to integrate developmental and environmental cues into behavior, but how specific outputs are generated when receptor proteins engage in various interactions remains a question. The study reveals that phosphorylation of RLP44 in its cytosolic tail governs its subcellular localization, crucial for its brassinosteroid-associated functions. However, this phosphorylation status does not affect its role in phytosulfokine signaling.