Abstract
Because of its role as an interface, the plasma membrane cell wall nexus is a signaling hub in all walled organisms. It is also a key structural component, being essential to maintain the integrity of the cell. In plants, many plasma membrane proteins have been shown to bind cell wall components, but with no obvious structural role. Conversely, the formation of Hechtian strands has revealed the existence of stiff structural hotspots, where plasma membrane is glued to the cell wall, even in the absence of plasmodesmata. However, the molecular factors behind this behavior remain elusive. Here, we bridge these two angles. Through a screen of candidate proteins, we reveal that the receptor-like kinase LecRKI.9 plays the role of a strong molecular glue at the plant cell cortex. Through deletion experiments, we find that the adhesive function of LecRKI.9 requires the presence of a lectin domain. Upon hyperosmotic stress, LecRKI.9 formed immobile clusters, whereas lectin-deleted versions of LecRKI.9 clusters were mobile. Cluster size and density correlated with the expected magnitude of mechanical stress in the wall before plasmolysis, further suggesting that the development of stiff adhesive hotspots through LecRKI.9 is regulated by stress in the wall. Altogether, this provides a scenario in which a subclass of lectin receptor-like kinases patterns the plasma membrane through stiff attachment sites, in response to stress.
Full text
1,815 characters
· extracted from
oa-doi-fallback
· click to expand
SUMMARY
Because of its role as an interface, the plasma membrane – cell wall nexus is a signaling hub in all walled organisms. It is also a key structural component, being essential to maintain the integrity of the cell. In plants, many plasma membrane proteins have been shown to bind cell wall components, but with no obvious structural role. Conversely, the formation of Hechtian strands has revealed the existence of stiff structural hotspots, where plasma membrane is glued to the cell wall, even in the absence of plasmodesmata. However, the molecular factors behind this behavior remain elusive. Here, we bridge these two angles. Through a screen of candidate proteins, we reveal that the receptor-like kinase LecRK-I.9 plays the role of a strong molecular glue at the plant cell cortex. Through deletion experiments, we find that the adhesive function of LecRK-I.9 requires the presence of a lectin domain. Upon hyperosmotic stress, LecRK-I.9 formed immobile clusters, whereas lectin-deleted versions of LecRK-I.9 clusters were mobile. Cluster size and density correlated with the expected magnitude of mechanical stress in the wall before plasmolysis, further suggesting that the development of stiff adhesive hotspots through LecRK-I.9 is regulated by stress in the wall. Altogether, this provides a scenario in which a subclass of lectin receptor-like kinases patterns the plasma membrane through stiff attachment sites, in response to stress.
Competing Interest Statement
The authors have declared no competing interest.
ABBREVIATIONS
- LTI6B
- Low Temperature-Induced Protein 6B.
- LecRK-I.9*
- Legume-type lectin Receptor-like kinase I.9. * 5 alanine substitutions at positions 350aa – 354aa within the ATP binding motif.
- LecRK-I.9*ΔLec
- LecRKI.9* without lectin (Δ244aa at positions 22aa – 265aa).
Text is read by the "Ask this paper" AI Q&A widget below.
Extraction quality varies by source — PMC NXML preserves structure
cleanly, OA-HTML may include some navigation residue, and OA-PDF can
have broken hyphenation. The publisher copy
(via DOI)
is the canonical version.