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

L Pizarro1, M Leibman-Markus1, S Schuster1

  • 1a School of Plant Sciences and Food Security , Tel Aviv University , Tel Aviv , Israel.

Plant Signaling & Behavior
|June 27, 2018
PubMed

Insights

Prenylated RAB acceptor type-1 (PRA1) regulates plant immune receptor levels. SlPRA1A specifically targets receptor-like proteins (RLPs), promoting their degradation and impacting plant immunity.

Area of Science:

  • Plant immunology
  • Cellular trafficking

Background:

  • Pattern recognition receptors (PRRs) are crucial for plant immunity, recognizing microbial patterns.
  • PRRs, including receptor-like kinases (RLKs) and receptor-like proteins (RLPs), require proper plasma membrane localization for function.
  • Endomembrane system trafficking is essential for maintaining PRR localization and availability.

Purpose of the Study:

  • To investigate the role of SlPRA1A, a prenylated RAB acceptor type-1 (PRA1) from *S. lycopersicum*, in regulating receptor-like protein PRR (RLP-PRR) localization and levels.
  • To identify the specific RAB GTPase targeted by SlPRA1A.
  • To elucidate the mechanism by which SlPRA1A influences RLP-PRR trafficking and degradation.

Main Methods:

  • Overexpression of SlPRA1A in *S. lycopersicum* to assess its effect on RLP-PRR protein levels.
  • Comparative analysis of SlPRA1A's impact on RLK-PRRs versus RLP-PRRs.
  • Screening of *A. thaliana* RAB GTPases for functional mimicry of SlPRA1A activity.
  • Live cell imaging to visualize the interaction and localization of SlPRA1A and its putative RAB target.

Main Results:

  • SlPRA1A overexpression significantly reduced RLP-PRR protein levels, notably LeEIX2, by promoting vacuolar degradation.
  • SlPRA1A's effect was specific to RLP-PRRs, with no impact observed on RLK-PRRs.
  • AtRABA1e from *A. thaliana* was identified as a functional homolog of SlPRA1A, mimicking its activity.
  • Live cell imaging confirmed that SlPRA1A enhances the localization of AtRABA1e on specific cellular structures.

Conclusions:

  • SlPRA1A acts as a specific regulator of RLP-PRR trafficking and protein stability.
  • AtRABA1e is a putative target of SlPRA1, suggesting a conserved mechanism for RAB regulation in plants.
  • The SlPRA1A-AtRABA1e interaction mediates the trafficking and degradation of LeEIX2, impacting plant immune signaling pathways.
Keywords:
PRRRabsintracellular traffickingplant immunity

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