SlPRA1A/RAB attenuate EIX immune responses via degradation of LeEIX2 pattern recognition receptor.

Pattern recognition receptors (PRR) are plasma membrane (PM) proteins that recognize microbe-associated molecular patterns (MAMPs), triggering an immune response. PRR are classified as receptor like kinases (RLKs) or receptor like proteins (RLPs). The PM localization of PRRs, which is crucial for their availability to sense MAMPs, depends on their appropriate trafficking through the endomembrane system. Recently, we have identified SlPRA1A, a prenylated RAB acceptor type-1 (PRA1) from S. lycopersicum, as a regulator of RLP-PRR localization and protein levels. SlPRA1A overexpression strongly decreases RLP-PRR protein levels, particularly those of LeEIX2, redirecting it to the vacuole for degradation. Interestingly, SlPRA1A does not affect RLK-PRRs, indicating its activity to be specific to RLP-PRR systems. As PRA1 proteins stabilize RABs on membranes, promoting RABs activity, we aimed to identify a RAB target of SlPRA1A. Screening of a set of A. thaliana RABs revealed that AtRABA1e is able to mimic SlPRA1A activity. Through live cell imaging, we observed that SlPRA1A enhances AtRABA1e localization on SlPRA1A positive punctuated structures. These results indicate that AtRABA1e is a putative target of SlPRA1, and a co-regulator of LeEIX2 trafficking and degradation.