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

• Teh, Ooi-kock

• Hatsugai, Noriyuki

• Tamura, Kentaro

• Fuji, Kentaro

• Tabata, Ryo

• Yamaguchi, Katsushi

• Shingenobu, Shuji

• Yamada, Masashi

• Hasebe, Mitsuyasu

• Sawa, Shinichiro

• Shimada, Tomoo

• Hara-Nishimura, Ikuko

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.

Journal

• Molecular plant

  Molecular plant 8 (3), 389-398, 2015-03

  Elsevier Inc.

Keywords

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

Details

• CRID: 1050282810790271872
• NII Article ID: 120005646465
• ISSN: 16742052
• HANDLE: 2433/199249
• Text Lang: en
• Article Type: journal article
• Data Source:
  • IRDB
  • CiNii Articles