Receptor kinase signalling of BRI1 and SIRK1 is tightly balanced by their interactomes as revealed from domain-swap chimaera in AE-MS approaches.

ABSTRACT: Plants response to different external and internal stimulation by activation of signal transduction pathways. Receptor kinases are localized at plasma membrane and were characterized to be involved in perception of signals at the cell surface. Here we use affinity enrichment mass spectrometry acquisition (AE-MS) of the LRR receptor kinases BRI1 and SIRK1 to study the stimulus-dependent interactomes in response to brassinolide and/or sucrose. Our results reveal the different recruitment ability of BRI1 and SIRK1 under BL and sucrose treatment. Specifically, BRI1 and SIRK1 are involved in fine-tuning the readiness of the plant to respond to the internal balance of the phytohormone branssinolide and sucrose levels. By using domain-swap chimera, we attribute structural features of the receptors to the interaction with their co-receptors, signaling transduction proteins or substrate transporters. Although SIRK1 and BRI1 regulates cell expansion through different mechanisms, the chimeras could compliment both sirk1 and bri1 phenotype, but not the double mutant. We proposed this mechanism is associated with recruited interactors at the plasma membrane. Our work reveals a tightly controlled balance of signaling cascade activation dependent on the internal status of the plant.

INSTRUMENT(S):

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Plant Cell, Root

SUBMITTER: Lin Xi  

LAB HEAD: Waltraud Schulze

PROVIDER: PXD044354 | Pride | 2025-05-06

REPOSITORIES: Pride