Single-molecule analysis reveals the phosphorylation of FLS2 governs its spatiotemporal dynamics and immunity.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 39046447.
- Also identified by DOI 10.7554/eLife.91072 and PMC identifier 11268883.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
The <i>Arabidopsis thaliana</i> FLAGELLIN-SENSITIVE2 (FLS2), a typical receptor kinase, recognizes the conserved 22 amino acid sequence in the N-terminal region of flagellin (flg22) to initiate plant defense pathways, which was intensively studied in the past decades. However, the dynamic regulation of FLS2 phosphorylation at the plasma membrane after flg22 recognition needs further elucidation. Through single-particle tracking, we demonstrated that upon flg22 treatment the phosphorylation of Ser-938 in FLS2 impacts its spatiotemporal dynamics and lifetime. Following Förster resonance energy transfer-fluorescence lifetime imaging microscopy and protein proximity indexes assays revealed that flg22 treatment increased the co-localization of GFP-tagged FLS2/FLS2<sup>S938D</sup> but not FLS2<sup>S938A</sup> with AtRem1.3-mCherry, a sterol-rich lipid marker, indicating that the phosphorylation of FLS2<sup>S938</sup> affects FLS2 sorting efficiency to <i>At</i>Rem1.3-associated nanodomains. Importantly, we found that the phosphorylation of Ser-938 enhanced flg22-induced FLS2 internalization and immune responses, demonstrating that the phosphorylation may activate flg22-triggered immunity through partitioning FLS2 into functional <i>At</i>Rem1.3-associated nanodomains, which fills the gap between the FLS2<sup>S938</sup> phosphorylation and FLS2-mediated immunity.
Medical subject headings
- Arabidopsis Proteins
- Arabidopsis
- Protein Kinases
- Flagellin
- Single Molecule Imaging