A molecular glue in plants: The lectin domain of LecRK-I.9 creates persistent plasma membrane – cell wall connections
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eLife Assessment
The cell wall and plasma membrane are tightly associated in plant cells, and even after plasmolysis, sites of strong contact remain between the plasma membrane and cell wall. Here, the authors provide solid data to implicate an Arabidopsis lectin-like receptor kinase in plasma-membrane-to-cell-wall contact sites, and propose that these attachment sites are of importance for plant resistance to hyperosmotic stress, yet the evidence remains incomplete without key controls. These important results broaden our view on dynamic modulation of plasma membrane topology and its physiological consequences.
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Abstract
Water stress challenges plasma membrane – wall attachment. When plants are exposed to strong hyperosmotic stress, water exits the cell leading to plasmolysis, where the plasma membrane detaches partially from the cell wall and reveals discrete and persistent attachment sites in the form of Hechtian strands. Although these structures have been observed in several species for more than a century, the molecular bases behind plasma membrane – wall attachment remains elusive. Through a screen of candidate proteins, we reveal that the overexpression of two lectin receptor-like proteins (LecRK-I.9 and LecTM) increases the density of plasma membrane – wall connections in N. Benthamiana. The extracellular lectin domain of LecRK-I.9 was able to remain in the wall during plasmolysis. Conversely, deletion of the lectin domain in the LecRK-I.9 overexpressor restored the density of Hechtian strands to WT levels. In Arabidopsis, upon hyperosmotic stress, LecRK-I.9 formed largely immobile clusters, whereas lectin-deleted versions of LecRK-I.9 clusters were mobile. Cluster density correlated with predicted tensile stress levels and mechanical reinforcement in the wall before plasmolysis, consistent with a scenario in which attachment of the lectin domain also reflects the wall properties. Last, while overexpressing LecRK-I.9 conferred resistance to low water potential conditions, deletion of the lectin domain in the LecRK-I.9 overexpressor restored a WT response to water stress. Altogether, this demonstrates that the lectin domain of LecRK-I.9 creates persistent plasma membrane – wall attachment sites, with physiological relevance for plant resistance to water stress.
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eLife Assessment
The cell wall and plasma membrane are tightly associated in plant cells, and even after plasmolysis, sites of strong contact remain between the plasma membrane and cell wall. Here, the authors provide solid data to implicate an Arabidopsis lectin-like receptor kinase in plasma-membrane-to-cell-wall contact sites, and propose that these attachment sites are of importance for plant resistance to hyperosmotic stress, yet the evidence remains incomplete without key controls. These important results broaden our view on dynamic modulation of plasma membrane topology and its physiological consequences.
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Reviewer #1 (Public review):
This work identifies two lectin receptor-like proteins as cell wall -plasma membrane anchors that contribute to persistent attachment sites maintained during plasmolysis. The authors propose that these attachment sites are important for plant resistance to hyperosmotic stress. Although the existence of persistent attachment sites between the cell wall and the plasma membrane, particularly evident in plasmolysed cells, was recognised long ago, the molecular components tethering the two cellular components remain largely unknown. Therefore, the findings presented by Arico et al. address an important question in plant cell biology.
Through a screening of potential anchors, they found that the overexpression of fluorescently tagged LecRK-I.9, LecTM, AGP18 and AT14A in Nicotiana benthamiana increased the density …
Reviewer #1 (Public review):
This work identifies two lectin receptor-like proteins as cell wall -plasma membrane anchors that contribute to persistent attachment sites maintained during plasmolysis. The authors propose that these attachment sites are important for plant resistance to hyperosmotic stress. Although the existence of persistent attachment sites between the cell wall and the plasma membrane, particularly evident in plasmolysed cells, was recognised long ago, the molecular components tethering the two cellular components remain largely unknown. Therefore, the findings presented by Arico et al. address an important question in plant cell biology.
Through a screening of potential anchors, they found that the overexpression of fluorescently tagged LecRK-I.9, LecTM, AGP18 and AT14A in Nicotiana benthamiana increased the density of Hechtian strands in plasmolysed cotyledon epidermis cells. They show that for LecRK-I.9* (* indicates kinase-dead version) and LecTM, this effect depends on the Lectin domain. Focusing on LecRK-I.9*, the overexpressed Lectin domain localized to cell walls, accumulating in certain foci. The authors interpret this as a possible preference for certain cell wall composition. I find these results convincing and the methodology robust.
The second part of the manuscript, however, relies on interpretations that, in my opinion, are not fully supported by the presented evidence. The authors move to Arabidopsis thaliana and show that overexpression of both LecRK-I.9* and LecRK-I.9*ΔLec fluorescent reporters also localizes to the plasma membrane and Hechtian strands in plasmolysed cells, although the density of Hechtian strands is not quantified. Thus, it is unclear whether LecRK-I.9* promotes Lectin domain-dependent strong cell wall-plasma membrane attachment sites in Arabidopsis.
The authors focus on the formation of big signal clusters at the plasma membrane in response to hyperosmotic treatment. They studied the dynamics of the clusters upon treatment application and observed increased mobility of LecRK-I.9* compared to LecRK-I.9*ΔLec and a plasma membrane marker. They then analysed the abundance and size (not the mobility) of these clusters on different plasma membranes facing cell walls that have or are predicted to have different mechanical and chemical properties, identifying differences between LecRK-I.9* and LecRK-I.9*ΔLec. Although the reduced mobility of LecRK-I.9 relative to LecRK-I.9ΔLec is consistent with an interaction between the lectin domain and the cell wall, it does not by itself demonstrate that the observed clusters correspond to CW attachment sites. Moreover, the relation between the clusters and Hechtian strands (bona fide cell wall-plasma membrane attachments) is not explored. Likewise, the differential clustering observed on different cell faces is intriguing but could have different interpretations.
Finally, the physiological relevance of the proposed anchoring mechanism is supported by osmotic stress assays, but the scoring method relies on manual classification of resistant seedlings and could benefit from a more objective quantitative readout.
In summary, although I find all these results valuable, I find that the methodology is not completely adequate and that several aspects of the data interpretation require additional support or clarification before the central conclusions can be fully justified.
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Reviewer #2 (Public review):
Summary:
The manuscript submitted by Arico and co-workers describes the impact of two lectin-domain-containing proteins (LecRK-I.9* and LecTM) on the formation and persistence of Hechtian strands. Based on a survey of selected candidates, overexpression of these two proteins resulted in an increase in Hechtian strand formation. Removal of the lectin domains and expression of this variant did not alter HS formation compared to the WT. In addition, the existence of the lectin domain reduced protein mobility, probably due to interactions with the wall. Last but not least, overexpression of LecRK-I.9 increased the resistance of plants towards water loss conditions.
Strengths:
The study seems well conducted, but may require some small additions. While the results themselves seem not surprising, I think that this …
Reviewer #2 (Public review):
Summary:
The manuscript submitted by Arico and co-workers describes the impact of two lectin-domain-containing proteins (LecRK-I.9* and LecTM) on the formation and persistence of Hechtian strands. Based on a survey of selected candidates, overexpression of these two proteins resulted in an increase in Hechtian strand formation. Removal of the lectin domains and expression of this variant did not alter HS formation compared to the WT. In addition, the existence of the lectin domain reduced protein mobility, probably due to interactions with the wall. Last but not least, overexpression of LecRK-I.9 increased the resistance of plants towards water loss conditions.
Strengths:
The study seems well conducted, but may require some small additions. While the results themselves seem not surprising, I think that this is a valuable demonstration of the cell wall binding ability of lectin proteins and its physiological and microscopical consequences.
Weaknesses:
At this stage, some of the study would benefit from some additional quantification.
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Reviewer #3 (Public review):
Summary:
The cell wall and plasma membrane are tightly associated in plant cells, but even after plasmolysis, sites of strong contact remain between the plasma membrane and cell wall. Several hypotheses have been introduced about the molecular makeup of these sites of PM-CW adhesion (e.g., Rui et al 2026 Cell; Qin et al 2026 Current Biol; Pérez-Sancho et al 2025 Cell). Here, the authors implicate two transmembrane lectin proteins in PM-CW adhesion via overexpression in Nicotiana benthamiana and via Arabidopsis knockout phenotypes for one of these candidates, the lectin receptor kinase LecRK-1.9. They further show that the PM-CW adhesion function of LecRK-1.9 requires the extracellular domain, suggesting that this lectin-like domain may interact with the cell wall. Interestingly, LecRK-1.9 has also been …
Reviewer #3 (Public review):
Summary:
The cell wall and plasma membrane are tightly associated in plant cells, but even after plasmolysis, sites of strong contact remain between the plasma membrane and cell wall. Several hypotheses have been introduced about the molecular makeup of these sites of PM-CW adhesion (e.g., Rui et al 2026 Cell; Qin et al 2026 Current Biol; Pérez-Sancho et al 2025 Cell). Here, the authors implicate two transmembrane lectin proteins in PM-CW adhesion via overexpression in Nicotiana benthamiana and via Arabidopsis knockout phenotypes for one of these candidates, the lectin receptor kinase LecRK-1.9. They further show that the PM-CW adhesion function of LecRK-1.9 requires the extracellular domain, suggesting that this lectin-like domain may interact with the cell wall. Interestingly, LecRK-1.9 has also been implicated in extracellular ATP binding in the context of biotic and abiotic stress responses (e.g., Choi et al 2014 Science).
Strengths:
Overall, the work is carefully conducted with high-quality imaging and quantitative image analysis. The results present an interesting candidate for future studies of plasma membrane-to-cell-wall attachment.
Weaknesses:
There are two major caveats to this work. First, all work was conducted with the kinase-dead version of LecRK-1.9, which eliminates a significant biological function of this protein, as evidenced by the major differences in expression pattern of wild-type vs kinase-dead LecRK-1.9. Second, controls are essential to document the expression levels of different protein variants and controls, since LecRK-1.9 expression is correlated with Hechtian strand density.
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A molecular glue: LecRKI.9 creates stiff plasma membrane cell wall connections https://www.biorxiv.org/content/10.1101/2025.08.14.670329v1
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A molecular glue: LecRKI.9 creates stiff plasma membrane cell wall connections https://www.biorxiv.org/content/10.1101/2025.08.14.670329v1
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