The receptor kinase FERONIA regulates phosphatidylserine localization at the cell surface to modulate ROP signaling

Cells maintain a constant dialog between the extracellular matrix and their plasma membrane to fine tune signal transduction processes. We found that the receptor kinase FERONIA (FER), which is a proposed cell wall sensor, modulates phosphatidylserine plasma membrane accumulation and nano-organization, a key regulator of Rho GTPase signaling in Arabidopsis. We demonstrate that FER is required for both Rho-of-Plant 6 (ROP6) nano-partitioning at the membrane and downstream production of reactive oxygen species upon hyperosmotic stimulus. Genetic and pharmacological rescue experiments indicate that phosphatidylserine is required for a subset of, but not all, FER functions. Furthermore, application of FER ligand shows that its signaling controls both phosphatidylserine membrane localization and nanodomains formation, which, in turn, tunes ROP6 signaling. Together, we propose that a cell wall-sensing pathway controls via the regulation of membrane phospholipid content, the nano-organization of the plasma membrane, which is an essential cell acclimation to environmental perturbations.

Automated summary

Cells communicate between the extracellular matrix and plasma membrane to regulate signal transduction. The receptor kinase FER plays a role in this process by modulating the accumulation and organization of phosphatidylserine on the plasma membrane, which affects Rho GTPase signaling in Arabidopsis. FER is essential for the partitioning of ROP6 at the membrane and the production of reactive oxygen species. The regulation of phosphatidylserine content and membrane organization by FER allows cells to adapt to environmental changes.