Arabidopsis EXO70B2 exocyst subunit contributes to papillae and encasement formation in antifungal defence

J Exp Bot. 2022 Jan 27;73(3):742-755. doi: 10.1093/jxb/erab457.

Abstract

In the reaction to non-adapted Blumeria graminis f. sp. hordei (Bgh), Arabidopsis thaliana leaf epidermal cells deposit cell wall reinforcements called papillae or seal fungal haustoria in encasements, both of which involve intensive exocytosis. A plant syntaxin, SYP121/PEN1, has been found to be of key importance for the timely formation of papillae, and the vesicle tethering complex exocyst subunit EXO70B2 has been found to contribute to their morphology. Here, we identify a specific role for the EXO70B2-containing exocyst complex in the papillae membrane domains important for callose deposition and GFP-SYP121 delivery to the focal attack sites, as well as its contribution to encasement formation. The mRuby2-EXO70B2 co-localizes with the exocyst core subunit SEC6 and GFP-SYP121 in the membrane domain of papillae, and EXO70B2 and SYP121 proteins have the capacity to directly interact. The exo70B2/syp121 double mutant produces a reduced number of papillae and haustorial encasements in response to Bgh, indicating an additive role of the exocyst in SYP121-coordinated non-host resistance. In summary, we report cooperation between the plant exocyst and a SNARE protein in penetration resistance against non-adapted fungal pathogens.

Keywords: Callose; SNARE; exocyst; non-host resistance; penetration; secretion.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arabidopsis Proteins* / metabolism
  • Arabidopsis* / metabolism
  • Cell Wall / metabolism
  • Qa-SNARE Proteins / genetics
  • Qa-SNARE Proteins / metabolism
  • Vesicular Transport Proteins

Substances

  • Arabidopsis Proteins
  • Exo70B2 protein, Arabidopsis
  • Qa-SNARE Proteins
  • Vesicular Transport Proteins