Format

Send to

Choose Destination
Protoplasma. 2013 Jun;250(3):671-81. doi: 10.1007/s00709-012-0459-6. Epub 2012 Oct 5.

Mapping FLS2 function to structure: LRRs, kinase and its working bits.

Author information

1
The Sainsbury Laboratory, Norwich Research Park, Norwich, NR4 7UH, UK. robatzek@tsl.ac.uk

Erratum in

  • Protoplasma. 2014 May;251(3):727.

Abstract

The plasma membrane-localised FLAGELLIN SENSING 2 (FLS2) receptor is an important component of plant immunity against potentially pathogenic bacteria, acting to recognise the conserved flg22 peptide of flagellin. FLS2 shares the common structure of transmembrane receptor kinases with a receptor-like ectodomain composed of leucine-rich repeats (LRR) and an active intracellular kinase domain. Upon ligand binding, FLS2 dimerises with the regulatory LRR-receptor kinase BRI1-associated kinase 1, which in turn triggers downstream signalling cascades. Although lacking crystal structure data, recent advances have been made in our understanding of flg22 recognition based on structural and functional analyses of FLS2. These studies have revealed critical regions/residues of FLS2 and post-translational modifications that regulate the abundance and activity of this receptor. In this review, we present the current knowledge on the structural mechanism of the FLS2-flg22 interaction and subsequent receptor-mediated signalling.

PMID:
23053766
DOI:
10.1007/s00709-012-0459-6
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Springer
Loading ...
Support Center