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Canut, H.

Publications and source records attributed to Canut, H..

3 recordsLinked to original sources

A molecular glue: LecRKI.9 creates stiff plasma membrane cell wall connections

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. SIGNIFICANCE STATEMENTAs observed since the mid-19th century, when placed in hyperosmotic conditions, plant cells undergo plasmolysis and form thin membraneous threads called Hechtian strands. These structures reflect the presence of persistent plasma membrane - cell wall attachment sites. Yet, the molecular components behind these sites are unknown. Through a candidate screen approach, we identify and demonstrate that the lectin domain of a receptor-like kinase provides such molecular glue. We also show that the clustering of the receptor is patterned and correlate with mechanically reinforced cell walls. Conversely, we find that the promotion of attachment increases resistance to water stress. This work revisits an old plant cell biology classic, and opens new avenues of research for plant adaptation to their environment.

plant biology↗

Receptor kinase LecRK-I.9 regulates cell wall remodelling and signalling during lateral root formation in Arabidopsis

Assembling and remodelling the cell wall is essential for plant development. Cell wall dynamic is controlled by cell wall proteins and a variety of sensor and receptor systems. LecRK-I.9, an Arabidopsis thaliana plasma membrane-localised lectin receptor kinase, was previously shown to be involved in cell wall-plasma membrane contacts and to play roles in plant-pathogen interactions, but so far, its role in development was unknown. LecRK-I.9 is transcribed at a high level in root tissues including the pericycle. Comparative transcript profiling of a loss-of-function mutant vs wild type identifies LecRK-I.9 as a regulator of cell wall metabolism. Consistently, lecrk-I.9 mutants display an increased pectin methylesterification level correlated with decreased pectin methylesterase and increased polygalacturonase activities. Also, LecRK-I.9 impacts lateral root development through the regulation of genes encoding (i) cell wall remodelling proteins during early events of lateral root initiation, and (ii) cell wall signalling peptides (CLE2, CLE4) repressing lateral root emergence and growth. Besides, low nitrate reduces LecRK-I.9 expression in pericycle and interferes with its regulatory network: however, the control of CLE2 and CLE4 expression is maintained. Altogether, the results show that LecRK-I.9 is a key player in a signalling network regulating both pre-branch site formation and lateral root emergence. HighlightThe lectin receptor kinase LecRK-I.9 regulates the molecular events leading to lateral root formation in both the initiation and emergence processes in Arabidopsis through cell wall remodelling enzymes and signalling peptides.

plant biology↗

The PROSCOOP10 gene encodes two extracellular hydroxylated peptides and impacts flowering time in Arabidopsis

AO_SCPLOWBSTRACTC_SCPLOWThe Arabidopsis PROSCOOP genes belong to a family predicted to encode secreted propeptides which undergo maturation steps to produce peptides named SCOOP. Some of them are involved in defence signalling through their perception by a receptor complex including MIK2, BAK1 and BKK1. Here, we focused on the PROSCOOP10 gene which is highly and constitutively expressed in the aerial organs. The MS/MS analyses of leaf apoplastic fluids allowed the identification of two distinct peptides, named SCOOP10#1 and SCOOP10#2, covering two different regions of PROSCOOP10. They both possess the canonical S-X-S family motif and have hydroxylated prolines. This identification in apoplastic fluids confirms for the first time the biological reality of SCOOP peptides. NMR and molecular dynamics studies showed that the SCOOP10 peptides, although largely unstructured in solution, tend to assume a hairpin-like fold exposing the two serine residues previously identified as essential for the peptide activity. Furthermore, PROSCOOP10 mutations led to an early flowering phenotype and an increased expression of the floral integrators SOC1 and LEAFY, consistent with the transcription of PROSCOOP10 in several mutants displaying an early or late flowering phenotype. These results suggest a role of PROSCOOP10 in flowering time, illustrating the functional complexity of the PROSCOOP family. HO_SCPLOWIGHLIGHTC_SCPLOWThe PROSCOOP10 gene encodes two post-translationally modified extracellular SCOOP10 peptides and acts upstream of SOC1 and LFY to delay flowering.

plant biology↗