BEACH-domain proteins act together in a cascade to mediate vacuolar protein trafficking and disease resistance in arabidopsis

Abstract

Membrane trafficking to the protein storage vacuole (PSV) is a specialized process in seed plants. However, this trafficking mechanism to PSV is poorly understood. Here, we show that three types of Beige and Chediak-Higashi (BEACH)-domain proteins contribute to both vacuolar protein transport and effector-triggered immunity (ETI). We screened a green fluorescent seed (GFS) library of Arabidopsis mutants with defects in vesicle trafficking and isolated two allelic mutants gfs3 and gfs12 with a defect in seed protein transport to PSV. The gene responsible for the mutant phenotype was found to encode a putative protein belonging to group D of BEACH-domain proteins, which possess kinase domains. Disruption of other BEACH-encoding loci in the gfs12 mutant showed that BEACH homologs acted in a cascading manner for PSV trafficking. The epistatic genetic interactions observed among BEACH homologs were also found in the ETI responses of the gfs12 and gfs12 bchb-1 mutants, which showed elevated avirulent bacterial growth. The GFS12 kinase domain interacted specifically with the pleckstrin homology domain of BchC1. These results suggest that a cascade of multiple BEACH-domain proteins contributes to vacuolar protein transport and plant defense.

Keywords

Arabidopsis thaliana; BEACH-domain protein; plant immunity; protein storage vacuoles; vacuolar protein transport

Published in

Molecular Plant
2015, volume: 8, number: 3, pages: 389-398
Publisher: Cell Press

SLU Authors

• Kock, Teh Ooi

  • Department of Plant Biology, Swedish University of Agricultural Sciences
    

• Teh, Ooi Kock

  • Kyoto University

UKÄ Subject classification

Biochemistry and Molecular Biology

Publication identifier

• DOI: https://doi.org/10.1016/j.molp.2014.11.015

Permanent link to this page (URI)

https://res.slu.se/id/publ/132044