Structural Basis for flg22-Induced Activation of the Arabidopsis FLS2-BAK1 Immune Complex

By P. H. Janssen, P. Yates, Bronwyn E. Grinton, Paul M. Taylor. 2013

374 citations recorded by the source corpus.

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

The FLS2-associated kinase BIK1 directly phosphorylates the NADPH oxidase RbohD to control plant immunity. (2014, background): “Recent advances demonstrate that BAK1 is a coreceptor of flg22, and intermolecular interactions between the FLS2 LRR domain, flg22, and the BAK1 LRR domain initiate the activation of the PRR complex (Sun et al., 2013).”
Defended to the Nines: 25 Years of Resistance Gene Cloning Identifies Nine Mechanisms for R Protein Function[OPEN] (2018, background): “The crystal structure of FLS2 incomplexwithBAK1and flg22hasbeenelucidated, revealing that flg22 acts as a “molecular glue” inducing complex formation of FLS2 with BAK1 (Sun et al., 2013).”
Growth-defense tradeoffs in plants: a balancing act to optimize fitness. (2014, unknown): “FACTOR-TU RECEPTOR (EFR) are LRR–RKs that recognize bacterial flagellin and bacterial EF-Tu, respectively (Gomez-Gomez and Boller, 2000; Zipfel et al., 2004, 2006; Sun et al., 2013).”
Direct regulation of the NADPH oxidase RBOHD by the PRR-associated kinase BIK1 during plant immunity. (2014, background): “As EFR and FLS2 form a ‘‘core’’ complex with both BAK1 and BIK1 (Chinchilla et al., 2007; Heese et al., 2007; Lu et al., 2010; Zhang et al., 2010; Roux et al., 2011; Sun et al., 2013), we tested in vitro if any of the proteins composing the PRR complex directly interact with RBOHD.”