胞浆
拟南芥
细胞内
细胞外
半胱氨酸
蛋白酶
半胱氨酸蛋白酶
细胞生物学
肽
蛋白酵素
蛋白质水解
化学
激发子
生物物理学
生物
生物化学
酶
基因
突变体
作者
Tim Hander,Álvaro D. Fernández-Fernández,Robert P. Kumpf,Patrick J. 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
出处
期刊:Science
[American Association for the Advancement of Science]
日期:2019-03-21
卷期号:363 (6433)
被引量:213
标识
DOI:10.1126/science.aar7486
摘要
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.
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