Publication Date:
2019
Description:
〈p〉Physical damage to cells leads to the release of immunomodulatory peptides to elicit a wound defense response in the surrounding tissue. In 〈i〉Arabidopsis thaliana〈/i〉, 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 Ca〈sup〉2+〈/sup〉 and is necessary and sufficient for Pep1 maturation. Cytosol-localized PROPEP1 and MC4 react only after loss of plasma membrane integrity and prolonged extracellular Ca〈sup〉2+〈/sup〉 entry. Our results reveal that a robust mechanism consisting of conserved molecular components links the intracellular and Ca〈sup〉2+〈/sup〉-dependent activation of a specific cysteine protease with the maturation of damage-induced wound defense signals.〈/p〉
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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