The FERONIA receptor kinase maintains cell-wall integrity during salt stress through Ca2+ signaling

Daniel Kita and Alexis Peaucelle contributed equally. Heather N. Cartwright, Vinh Doan, Qiaohong Duan, Ming-Che Liu, Jacob Maman, Leonie Steinhorst, Ina Schmitz-Thom and Robert Yvon contributed equally.

International audience

Inglés. Cells maintain integrity despite changes in their mechanical properties elicited during growth and environmental stress. How cells sense their physical state and compensate for cell-wall damage is poorly understood, particularly in plants. Here we report that FERONIA (FER), a plasma-membrane-localized receptor kinase from <em>Arabidopsis</em>, is necessary for the recovery of root growth after exposure to high salinity, a widespread soil stress. The extracellular domain of FER displays tandem regions of homology with malectin, an animal protein known to bind di-glucose <em>in vitro</em> and important for protein quality control in the endoplasmic reticulum. The presence of malectin-like domains in FER and related receptor kinases has led to widespread speculation that they interact with cell-wall polysaccharides and can potentially serve a wall-sensing function. Results reported here show that salinity causes softening of the cell wall and that FER is necessary to sense these defects. When this function is disrupted in the <em>fer</em> mutant, root cells explode dramatically during growth recovery. Similar defects are observed in the <em>mur1</em> mutant, which disrupts pectin cross-linking. Furthermore, <em>fer</em> cell-wall integrity defects can be rescued by treatment with calcium and borate, which also facilitate pectin cross-linking. Sensing of these salinity-induced wall defects might therefore be a direct consequence of physical interaction between the extracellular domain of FER and pectin. FER-dependent signaling elicits cell-specific calcium transients that maintain cell-wall integrity during salt stress. These results reveal a novel extracellular toxicity of salinity, and identify FER as a sensor of damage to the pectin-associated wall.