Related Experiment Video
Updated: May 31, 2026

Identification of Post-translational Modifications of Plant Protein Complexes
Published on: February 22, 2014
Direct ubiquitination of pattern recognition receptor FLS2 attenuates plant innate immunity
Dongping Lu1, Wenwei Lin, Xiquan Gao
1Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA.
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.
Related Concept Videos
Cell Signaling in Plants
Defenses Against Pathogens and Herbivores
The Extrinsic Apoptotic Pathway
Regulation of the Unfolded Protein Response
Introduction to Plant Diversity
NF-κB-dependent Signaling Pathway
NF-κB-dependent Signaling Mechanism
The heterodimer of NF-κB...

