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EMBO J. 2015 Jan 2;34(1):55-66. doi: 10.15252/embj.201488582. Epub 2014 Nov 14.

GRIM REAPER peptide binds to receptor kinase PRK5 to trigger cell death in Arabidopsis.

Author information

1
Plant Biology, Department of Biosciences University of Helsinki, Helsinki, Finland michael.wrzaczek@helsinki.fi jaakko.kangasjarvi@helsinki.fi.
2
Plant Biology, Department of Biosciences University of Helsinki, Helsinki, Finland.
3
Department of Plant Systems Biology, VIB, Ghent, Belgium Department of Plant Biotechnology and Bioinformatics, Ghent University, Ghent, Belgium Department of Medical Protein Research, VIB, Ghent, Belgium Department of Biochemistry, Ghent University, Ghent, Belgium.
4
Plant Biology, Department of Biosciences University of Helsinki, Helsinki, Finland Institute of Biotechnology, University of Helsinki, Helsinki, Finland.
5
Umeå Plant Science Centre, Department of Plant Physiology, Umeå University, Umeå, Sweden.
6
Department of Medical Protein Research, VIB, Ghent, Belgium Department of Biochemistry, Ghent University, Ghent, Belgium.
7
Department of Plant Systems Biology, VIB, Ghent, Belgium Department of Plant Biotechnology and Bioinformatics, Ghent University, Ghent, Belgium.
8
Plant Biology, Department of Biosciences University of Helsinki, Helsinki, Finland Institute of Biotechnology, University of Helsinki, Helsinki, Finland The Sainsbury Laboratory, University of Cambridge, Cambridge, UK.
9
Plant Biology, Department of Biosciences University of Helsinki, Helsinki, Finland Distinguished Scientist Fellowship Program, College of Science, King Saud University, Riyadh, Saudi Arabia michael.wrzaczek@helsinki.fi jaakko.kangasjarvi@helsinki.fi.

Abstract

Recognition of extracellular peptides by plasma membrane-localized receptor proteins is commonly used in signal transduction. In plants, very little is known about how extracellular peptides are processed and activated in order to allow recognition by receptors. Here, we show that induction of cell death in planta by a secreted plant protein GRIM REAPER (GRI) is dependent on the activity of the type II metacaspase METACASPASE-9. GRI is cleaved by METACASPASE-9 in vitro resulting in the release of an 11 amino acid peptide. This peptide bound in vivo to the extracellular domain of the plasma membrane-localized, atypical leucine-rich repeat receptor-like kinase POLLEN-SPECIFIC RECEPTOR-LIKE KINASE 5 (PRK5) and was sufficient to induce oxidative stress/ROS-dependent cell death. This shows a signaling pathway in plants from processing and activation of an extracellular protein to recognition by its receptor.

KEYWORDS:

ligand; protease; receptor‐like kinase; secreted protein

PMID:
25398910
PMCID:
PMC4291480
DOI:
10.15252/embj.201488582
[Indexed for MEDLINE]
Free PMC Article

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