The 26S proteasome is essential for proteostasis and constitutes one of the most conserved molecular machineries in eukaryotes. Its homeostasis is maintained by a mechanistically conserved feedback lo...

Langin et al. find that ER-associated sorting (ERAS) directs NAC53/78 turnover and activation to couple proteasome induction with repression of photosynthesis genes, linking proteostasis to energy met...

Plasma membrane-localized receptors operate as dynamic signaling complexes and integrative networks, yet the spatial and temporal regulation of these interactions remain largely unknown. Here, by analyzing the components of a minimal Arabidopsis leucine-rich repeat receptor kinase network, we describe the differential diffusion and organization of receptor complex components and unveil the nanoscale spatial and temporal logic underlying the formation of receptor kinase complexes. The ligand-binding receptors FLS2 and BRI1, and the accessory receptor BIR3, are organized in plasma membrane nanodomains, within which the co-receptor BAK1 diffuses and is spatially arrested upon ligand perception. BAK1 spatial arrest relies on extracellular domain (ECD)-ECD interactions but does not require receptor complex activation. Mathematical modelling, single molecule imaging and bio-assays infer that accessory receptors maintain a dynamic pool of co-receptors in the vicinity of ligand-binding receptors to promote ligand-induced complex formation and signaling. We propose that ligand-induced receptor kinase complex formation is a deterministic process defined by the relative nanoscale spatial positioning of individual signaling and regulatory components.

Rapid alkalinization factor (RALF) peptides are important signaling molecules binding to Catharanthus roseus receptor-like kinase 1-like (CrRLK1L)—LORELEI/LORELEI-like GPI-anchored protein complexes t...