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Abstract:
Innate immune responses are triggered by the activation of pattern-recognition receptors (PRRs). The Arabidopsis PRR FLAGELLIN-SENSING 2 (FLS2) senses bacterial flagellin and initiates immune signaling through association with BAK1. The molecular mechanisms underlying the attenuation of FLS2 activation are largely unknown. We report that flagellin induces recruitment of two closely related U-box E3 ubiquitin ligases, PUB12 and PUB13, to FLS2 receptor complex in Arabidopsis. BAK1 phosphorylates PUB12 and PUB13 and is required for FLS2-PUB12/13 association. PUB12 and PUB13 polyubiquitinate FLS2 and promote flagellin-induced FLS2 degradation, and the pub12 and pub13 mutants displayed elevated immune responses to flagellin treatment. Our study has revealed a unique regulatory circuit of direct ubiquitination and turnover of FLS2 by BAK1-mediated phosphorylation and recruitment of specific E3 ligases for attenuation of immune signaling.
1 Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA. 2 Department of Plant Pathology and Microbiology, Texas A&M University, College Station, TX 77843, USA. 3 Institute for Plant Genomics and Biotechnology, Texas A&M University, College Station, TX 77843, USA. 4 Key Laboratory of Biopesticide and Chemical Biology, Ministry of Education, Fujian Agriculture and Forestry University, Fuzhou 350002, China. 5 Department of Biochemistry, University of Missouri–Columbia, Columbia, MO 65211, USA.
* To whom correspondence should be addressed. E-mail: lshan{at}tamu.edu (L.S.); pinghe{at}tamu.edu (P.H.)
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