Biotic Stress/Applied Plant Bio

Abstract

CS-13-1 - Phosphorylation and ubiquitination in FLS2 and BRI1 receptor complex regulation

Monday, July 16
1:03 PM - 1:23 PM

Plant plasma membrane-resident receptor-like kinases (RLKs) sense extracellular and intracellular stimuli, and play pivotal roles in coordinating cell differentiation, growth and immunity. Arabidopsis RLK FLS2 perceives bacterial flagellin in regulating plant immunity, and BRI1 perceives the polyhydroxylated steroid hormone brassinosteroids (BRs) in regulating growth and development. Both BRI1 and FLS2 heterodimerize with BAK1 family RLKs upon the cognate ligand perception. The activity of FLS2-BAK1 and BRI1-BAK1 receptor complexes undergoes multi-layered positive and negative regulations, including protein phosphorylation and ubiquitination, for signaling activation and attenuation. FLS2 is ubiquitinated by two closely related plant U-box (PUB) E3 ubiquitin ligases PUB12 and PUB13. Upon flagellin perception, FLS2 associates with PUB12 and PUB13 in a BAK1-phosphorylation dependent manner, resulting in ligand-induced FLS2 ubiquitination and degradation to down-regulate FLS2 signaling. We recently found that endocytosis and protein abundance of BRI1 is also regulated by PUB12 and PUB13-mediated ubiquitination. BR perception promotes BRI1 association with PUB12 and PUB13, and BRI1 regulates PUB13 ubiquitination activity through phosphorylation at serine 344 residue, which is distinct from BAK1-mediated phosphorylation. The detailed mechanism underlying phosphorylation and ubiquitination in regulating RLK intracellular degradation and endocytosis will be discussed.


 


 

Co-Authors

Jinggeng Zhou – Texas A&M University; Derui Liu – Ghent University; Eugenia Russinova – Ghent University; Ping He – Texas A&M University

Libo Shan, PhD

Professor
Texas A&M University
Texas A&M University

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CS-13-1 - Phosphorylation and ubiquitination in FLS2 and BRI1 receptor complex regulation



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