Revisiting plant electric signaling: Challenging an old phenomenon with novel discoveries.

Higher plants efficiently orchestrate rapid systemic responses to diverse environmental stimuli through electric signaling. This review explores the mechanisms underlying two main types of electric signals in plants, action potentials (APs) and slow wave potentials (SWPs), and how new discoveries challenge conventional neurophysiological paradigms traditionally forming their theoretical foundations. Animal APs are biophysically well-defined, whereas plant APs are often classified based on their shape, lacking thorough characterization. SWPs are depolarizing electric signals deviating from this shape, leading to an oversimplified classification of plant electric signals. Indeed, investigating the generation and propagation of plant APs and SWPs showcases a complex interplay of mechanisms that sustain self-propagating signals and internally propagating stimuli, resulting in membrane depolarization, cytosolic calcium increase, and alterations in reactive oxygen species and pH. A holistic understanding of plant electric signaling will rely on unraveling the network of ion-conducting proteins, signaling molecules, and mechanisms for signal generation and propagation.

Structure of the Arabidopsis thaliana glutamate receptor-like channel GLR3.4.

Glutamate receptor-like channels (GLRs) play vital roles in various physiological processes in plants, such as wound response, stomatal aperture control, seed germination, root development, innate immune response, pollen tube growth, and morphogenesis. Despite the importance of GLRs, knowledge about their molecular organization is limited. Here we use X-ray crystallography and single-particle cryo-EM to solve structures of the Arabidopsis thaliana GLR3.4. Our structures reveal the tetrameric assembly of GLR3.4 subunits into a three-layer domain architecture, reminiscent of animal ionotropic glutamate receptors (iGluRs). However, the non-swapped arrangement between layers of GLR3.4 domains, binding of glutathione through S-glutathionylation of cysteine C205 inside the amino-terminal domain clamshell, unique symmetry, inter-domain interfaces, and ligand specificity distinguish GLR3.4 from representatives of the iGluR family and suggest distinct features of the GLR gating mechanism. Our work elaborates on the principles of GLR architecture and symmetry and provides a molecular template for deciphering GLR-dependent signaling mechanisms in plants.