Ligand-induced monoubiquitination of BIK1 regulates plant immunity

Xiyu Ma, Lucas A. N. Claus, Michelle E. Leslie, Kai Tao, Zhiping Wu, Jun Liu, Xiao Yu, Bo Li, Jinggeng Zhou, Daniel V. Savatin, Junmin Peng, Brett M. Tyler, Antje Heese, Eugenia Russinova, Ping He () and Libo Shan ()
Additional contact information
Xiyu Ma: Texas A&M University
Lucas A. N. Claus: Ghent University
Michelle E. Leslie: University of Missouri-Columbia
Kai Tao: Oregon State University
Zhiping Wu: St Jude Children’s Research Hospital
Jun Liu: Texas A&M University
Xiao Yu: Texas A&M University
Bo Li: Texas A&M University
Jinggeng Zhou: Texas A&M University
Daniel V. Savatin: Ghent University
Junmin Peng: St Jude Children’s Research Hospital
Brett M. Tyler: Oregon State University
Antje Heese: University of Missouri-Columbia
Eugenia Russinova: Ghent University
Ping He: Texas A&M University
Libo Shan: Texas A&M University

Nature, 2020, vol. 581, issue 7807, 199-203

Abstract: Abstract Recognition of microbe-associated molecular patterns (MAMPs) by pattern recognition receptors (PRRs) triggers the first line of inducible defence against invading pathogens1–3. Receptor-like cytoplasmic kinases (RLCKs) are convergent regulators that associate with multiple PRRs in plants4. The mechanisms that underlie the activation of RLCKs are unclear. Here we show that when MAMPs are detected, the RLCK BOTRYTIS-INDUCED KINASE 1 (BIK1) is monoubiquitinated following phosphorylation, then released from the flagellin receptor FLAGELLIN SENSING 2 (FLS2)–BRASSINOSTEROID INSENSITIVE 1-ASSOCIATED KINASE 1 (BAK1) complex, and internalized dynamically into endocytic compartments. The Arabidopsis E3 ubiquitin ligases RING-H2 FINGER A3A (RHA3A) and RHA3B mediate the monoubiquitination of BIK1, which is essential for the subsequent release of BIK1 from the FLS2–BAK1 complex and activation of immune signalling. Ligand-induced monoubiquitination and endosomal puncta of BIK1 exhibit spatial and temporal dynamics that are distinct from those of the PRR FLS2. Our study reveals the intertwined regulation of PRR–RLCK complex activation by protein phosphorylation and ubiquitination, and shows that ligand-induced monoubiquitination contributes to the release of BIK1 family RLCKs from the PRR complex and activation of PRR signalling.

Date: 2020
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DOI: 10.1038/s41586-020-2210-3

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