A domain swap approach reveals a role of the plant wall-associated kinase 1 (WAK1) as a receptor of oligogalacturonides
By Alexandre Brutus, F. Sicilia, A. Macone, F. Cervone, G. De Lorenzo. Proceedings of the National Academy of Sciences of the United States of America, 2010
693 citations recorded by the source corpus.
Subfields: Molecular Biology, Plant Science
View Paper: https://www.semanticscholar.org/paper/eca7cd8ee8a9ee4de94d0ed3eade27f500a17fb1
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Citations in the corpus
- Plant pattern recognition receptor complexes at the plasma membrane. (2012, background): “An innovative chimeric receptor approach using the intracellular region of EFR revealed that the EGF-like domain-containing RLK WAK1 is a PRR for oligogalacturonides, which are released from plant cell walls during fungal infections or wounding [31 ].”
- Comprehending crystalline β-carotene accumulation by comparing engineered cell models and the natural carotenoid-rich system of citrus (2011, neutral): “It is probable that wall-associated kinase 1 (WAK1) and WAK2 are the actual receptors of these molecules (Brutus et al., 2010), transferring the signal across the plasma membrane.”
- The FLS2-associated kinase BIK1 directly phosphorylates the NADPH oxidase RbohD to control plant immunity. (2014, background): “Cell Ho patterns such as oligogalacturonides and small peptides that are generated during pathogen infection (Brutus et al., 2010; Krol et al., 2010; Yamaguchi et al., 2010).”
- Oligo-carrageenans induce a long-term and broad-range protection against pathogens in tobacco plants (var. Xanthi) (2012, background): “In addition, it was recently determined that oligo-galacturonides binds to Wall-Associated Kinase-1 (WAK-1) receptor which contains an extracellular domain having several Epidermal Growth Factor (EGF)-like repeats and an N-terminal and non-EGF domain that binds oligogalacturonides [15] which is coup”
- REVIEW: PART OF A SPECIAL ISSUE ON PLANT CELL WALLS An update on receptor-like kinase involvement in the maintenance of plant cell wall integrity (2014, background): “It has been demonstrated that WAK1 binds oligogalacturonides, and that oligogalacturonide binding elicits defence responses in a chimaeric RLK consisting of an extracellular WAK1 domain and an intracellular kinase domain of the EF-Tu receptor (Brutus et al., 2010).”