Immunity in plants is mediated a group of receptor proteins, a majority of which belongs to the family of Nucleotide-Binding Leucine Rich Repeat (NB-LRR). In the cell, the activity of NB-LRR receptors is fine-tuned by interactions with their interacting partners.
Identifying NB-LRR interacting proteins is, therefore, crucial to advance our understanding of how these receptors function. In this study, we performed a Co-IP/MS screening to screen for novel interactors of the potato Gpa2 and Rx1 CC-NB-LRRs receptors. The Glycine-Rich RNA-Binding Protein 7 (NbGRP7) was identified as a novel interactor of both Gpa2 and Rx1 that potentiates their immune receptors. In further characterization, we show that NbGRP7 regulates the transcript and protein stabilities of Rx1. Our data combined shows that NbGRP7 is crucial pro-immune component of Rx1/Gpa2 immunities functioning at a post-transcriptional level.