Phosphocode-dependent functional dichotomy of a common co-receptor in plant signalling

Artemis Perraki, Thomas A. DeFalco, Paul Derbyshire, Julian Avila, David Séré, Jan Sklenar, Xingyun Qi, Lena Stransfeld, Benjamin Schwessinger, Yasuhiro Kadota, Alberto P. Macho, Shushu Jiang, Daniel Couto, Keiko U. Torii, Frank L. H. Menke and Cyril Zipfel ()
Additional contact information
Artemis Perraki: The Sainsbury Laboratory, Norwich Research Park
Thomas A. DeFalco: The Sainsbury Laboratory, Norwich Research Park
Paul Derbyshire: The Sainsbury Laboratory, Norwich Research Park
Julian Avila: University of Washington
David Séré: The Sainsbury Laboratory, Norwich Research Park
Jan Sklenar: The Sainsbury Laboratory, Norwich Research Park
Xingyun Qi: University of Washington
Lena Stransfeld: The Sainsbury Laboratory, Norwich Research Park
Benjamin Schwessinger: The Sainsbury Laboratory, Norwich Research Park
Yasuhiro Kadota: The Sainsbury Laboratory, Norwich Research Park
Alberto P. Macho: The Sainsbury Laboratory, Norwich Research Park
Shushu Jiang: The Sainsbury Laboratory, Norwich Research Park
Daniel Couto: The Sainsbury Laboratory, Norwich Research Park
Keiko U. Torii: University of Washington
Frank L. H. Menke: The Sainsbury Laboratory, Norwich Research Park
Cyril Zipfel: The Sainsbury Laboratory, Norwich Research Park

Nature, 2018, vol. 561, issue 7722, 248-252

Abstract: Abstract Multicellular organisms use cell-surface receptor kinases to sense and process extracellular signals. Many plant receptor kinases are activated by the formation of ligand-induced complexes with shape-complementary co-receptors1. The best-characterized co-receptor is BRASSINOSTEROID INSENSITIVE 1-ASSOCIATED KINASE 1 (BAK1), which associates with numerous leucine-rich repeat receptor kinases (LRR-RKs) to control immunity, growth and development2. Here we report key regulatory events that control the function of BAK1 and, more generally, LRR-RKs. Through a combination of phosphoproteomics and targeted mutagenesis, we identified conserved phosphosites that are required for the immune function of BAK1 in Arabidopsis thaliana. Notably, these phosphosites are not required for BAK1-dependent brassinosteroid-regulated growth. In addition to revealing a critical role for the phosphorylation of the BAK1 C-terminal tail, we identified a conserved tyrosine phosphosite that may be required for the function of the majority of Arabidopsis LRR-RKs, and which separates them into two distinct functional classes based on the presence or absence of this tyrosine. Our results suggest a phosphocode-based dichotomy of BAK1 function in plant signalling, and provide insights into receptor kinase activation that have broad implications for our understanding of how plants respond to their changing environment.

Keywords: BRASSINOSTEROID INSENSITIVE 1-ASSOCIATED KINASE 1 (BAK1); Phosphosites; Plant Receptor Kinases; FLAGELLIN SENSING 2 (FLS2); Chitin Elicitor Receptor Kinase (CERK1) (search for similar items in EconPapers)
Date: 2018
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DOI: 10.1038/s41586-018-0471-x

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