Palmitoylation is a dynamic regulator of plant receptor localization and function
EMSL Project ID
50753
Abstract
Recent data indicate that competition between plant plasma membrane (PM) receptor palmitoylation and autophosphorylation defines inactive and active states, respectively. Hence, for any given treatment, global monitoring of receptor palmitoylation and phosphorylation provides a read-out of biochemical function allowing functional assignment of orphan receptors. Sustainable management of bioenergy crops will require the development of plants with high yield and the ability to withstand a variety of biotic and abiotic stresses. Unlike mobile animals, which can remove themselves from hostile environments, plants are rooted in place and, hence, have evolved mechanisms to recognize environmental threats and respond. Among the key proteins involved in recognizing the environment are receptor-like kinases (RLKs). Their importance is exemplified by the large expansion of RLK gene families in plants with over 400 RLKs in Arabidopsis, 1200 in soybean and 600 in sorghum. Yet, only a few RLKs have been functionally characterized with the others known only from sequence information. The proposal seeks to demonstrate the utility of using mass spectrometry approaches to examine dynamic palmitoylation and phosphorylation of plant RLKs as a means to functionally annotate these proteins on a genome scale in relation to environmental stress. Data indicate that palmitoylated RLKs reside in PM nanodomains and, hence, we will characterize the protein and lipid composition of these nanodomains. Finally, we will utilize EMSL's confocal fluorescence /FLIM and super resolution fluorescence microscopy systems to confirm and study protein-protein interactions within PM nanodomains.
Project Details
Project type
Large-Scale EMSL Research
Start Date
2019-10-01
End Date
2021-12-31
Status
Closed
Released Data Link
Team
Principal Investigator
Team Members