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bioRxiv · 10.1101/685610

BSU1 family phosphatases mediate Flagellin-FLS2 signaling through a specific phosphocode.

Park, C. H.·Youn, J.-H.·Xu, S.-L.·Kim, J.-G.·Bi, Y.·Xu, N.·Mudgett, M. B.·Kim, S.-K.·Kim, T.-W.·Wang, Z.-Y.
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Abstract

Hundreds of leucine-rich repeat receptor kinases (LRR-RKs) have evolved to control diverse processes of growth, development, and immunity in plants; the mechanisms that link LRR-RKs to distinct cellular responses are not understood. Here we show that two LRR-RKs, the brassinosteroid hormone receptor BRI1 (BRASSINOSTEROID INSENSITIVE 1) and the flagellin receptor FLS2 (FLAGELLIN SENSING 2), regulate downstream glycogen synthase kinase 3 (GSK3) and mitogen-activated protein (MAP) kinases, respectively, through phosphocoding of the BRI1-SUPPRESSOR1 (BSU1) phosphatase. BSU1 was previously identified as a component that inactivates GSK3s in the BRI1 pathway. We found surprisingly that loss of the BSU1 family phosphatases activates effector-triggered immunity (ETI) and impairs flagellin-triggered MAP kinase activation and immunity. The flagellin-activated BOTRYTIS-INDUCED KINASE 1 (BIK1) phosphorylates BSU1 at serine-251. Mutation of serine-251 reduces the ability of BSU1 to mediate flagellin-induced MAP kinase activation and immunity, but not its abilities to suppress ETI and interact with GSK3, which is enhanced through the phosphorylation of BSU1 at serine-764 upon brassinosteroid signaling. These results demonstrate that BSU1 plays an essential role in immunity and transduces brassinosteroid-BRI1 and flagellin-FLS2 signals using different phosphorylation sites. Our study illustrates that phosphocoding in shared downstream components provides signaling specificities for diverse plant receptor kinases.

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Park, C. H., Youn, J.-H., Xu, S.-L., Kim, J.-G., Bi, Y., Xu, N., Mudgett, M. B., Kim, S.-K., Kim, T.-W., Wang, Z.-Y.. 2019-06-27. BSU1 family phosphatases mediate Flagellin-FLS2 signaling through a specific phosphocode.. https://doi.org/10.1101/685610

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