Abstract |
Physical damage to cells leads to the release of immunomodulatory peptides to elicit a wound defense response in the surrounding tissue. In Arabidopsis thaliana, the plant elicitor peptide 1 (Pep1) is processed from its protein precursor, PRECURSOR OF PEP1 (PROPEP1). We demonstrate that upon damage, both at the tissue and single-cell levels, the cysteine protease METACASPASE4 (MC4) is instantly and spatiotemporally activated by binding high levels of Ca2+ and is necessary and sufficient for Pep1 maturation. Cytosol-localized PROPEP1 and MC4 react only after loss of plasma membrane integrity and prolonged extracellular Ca2+ entry. Our results reveal that a robust mechanism consisting of conserved molecular components links the intracellular and Ca2+-dependent activation of a specific cysteine protease with the maturation of damage-induced wound defense signals.
|
Authors | Tim Hander, Álvaro D Fernández-Fernández, Robert P Kumpf, Patrick Willems, Hendrik Schatowitz, Debbie Rombaut, An Staes, Jonah Nolf, Robin Pottie, Panfeng Yao, Amanda Gonçalves, Benjamin Pavie, Thomas Boller, Kris Gevaert, Frank Van Breusegem, Sebastian Bartels, Simon Stael |
Journal | Science (New York, N.Y.)
(Science)
Vol. 363
Issue 6433
(Mar 22 2019)
ISSN: 1095-9203 [Electronic] United States |
PMID | 30898901
(Publication Type: Journal Article)
|
Copyright | Copyright © 2019 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. |
Chemical References |
- Arabidopsis Proteins
- Oligopeptides
- PROPEP1 protein, Arabidopsis
- Protein Precursors
- Cysteine Endopeptidases
- metacaspase-4, Arabidopsis
- Calcium
|
Topics |
- Amino Acid Sequence
- Arabidopsis
(enzymology, immunology)
- Arabidopsis Proteins
(metabolism)
- Calcium
(metabolism)
- Cysteine Endopeptidases
(metabolism)
- Cytosol
(enzymology)
- Immunomodulation
- Oligopeptides
(metabolism)
- Plant Immunity
- Protein Precursors
(metabolism)
|