Damage on plants activates Ca
            <sup>2+</sup>
            -dependent metacaspases for release of immunomodulatory peptides

Hander, Tim; Fernández-Fernández, Álvaro Daniel; Kumpf, Robert P.; Willems, Patrick J.; Schatowitz, Hendrik; Rombaut, Dries; Staes, An; Nolf, Jonah; Pottie, Robin; Yao, Panfeng; Gonçalves, Amanda; Pavie, Benjamin; Boller, Thomas; Gevaert, Kris; Breusegem, Frank Van; Bartels, Sebastian; Stael, Simon

doi:10.1126/science.aar7486

Cited by 183 publications

(173 citation statements)

References 51 publications

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“…In Arabidopsis , overexpression of salt‐inducible PROPEP3 and Pep3 application both confer salt tolerance through PEPR1, although the mechanisms downstream of the receptor remain elusive (Nakaminami et al ., ). Furthermore, PROPEP1 cleavage is induced upon cellular injury via a Ca 2+ ‐dependent metacaspase, thereby releasing Pep1 from the vacuolar membranes (Hander et al ., ). Although the steps following this intracellular precursor processing remain undetermined, this work points to the dynamic spatiotemporal control of damage signal generation and also the existence of other components processing PROPEPs.…”

Section: Damage Sensing and Signaling Under Abiotic Stressmentioning

confidence: 99%

Plant immunity in signal integration between biotic and abiotic stress responses

2019

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Summary Plants constantly monitor and cope with the fluctuating environment while hosting a diversity of plant‐inhabiting microbes. The mode and outcome of plant–microbe interactions, including plant disease epidemics, are dynamically and profoundly influenced by abiotic factors, such as light, temperature, water and nutrients. Plants also utilize associations with beneficial microbes during adaptation to adverse conditions. Elucidation of the molecular bases for the plant–microbe–environment interactions is therefore of fundamental importance in the plant sciences. Following advances into individual stress signaling pathways, recent studies are beginning to reveal molecular intersections between biotic and abiotic stress responses and regulatory principles in combined stress responses. We outline mechanisms underlying environmental modulation of plant immunity and emerging roles for immune regulators in abiotic stress tolerance. Furthermore, we discuss how plants coordinate conflicting demands when exposed to combinations of different stresses, with attention to a possible determinant that links initial stress response to broad‐spectrum stress tolerance or prioritization of specific stress tolerance.

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Section: Damage Sensing and Signaling Under Abiotic Stressmentioning

confidence: 99%

Plant immunity in signal integration between biotic and abiotic stress responses

2019

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“…2e), we dissolved wild-type AtMC4 crystals in a buffer containing 0.2 mM Ca 2+ and used mass spectrometry to identify possible cleavage sites. In addition to the previously identified sites of K225, R180, R190, and K210 in the linker-N region 4 , we identified Lys237 and Lys267 in two -helices of the linker-C region ( Fig. 3e, Extended Data Table 2).…”

Section: Mechanism Of Ca 2+ -Dependent Multiple Cleavages and Activationmentioning

confidence: 52%

“…8e). Ca 2+ concentrations of 0.4-0.8 mM can initiate the cleavage at position Arg69 to produce Pep1 peptides that can activate a plant immune response by forming a complex with its receptor PEPR1 4,24 . At a Ca 2+ concentration of 12.5 mM or higher, GST-Δpep1 ( Fig.…”

Section: Ca 2+ -Dependent Self-cleavage and Activationmentioning

confidence: 99%

“…After the release of the linker-N region, the active site of AtMC4 is available to process substrates such as Propep1 ( Fig. 4d) to produce the Pep1 elicitor and trigger the immune response downstream 4 . In addition, the release of the linker-N region will destabilize the β11-β12 hairpin (Fig.…”

Section: Mechanism Of Ca 2+ -Dependent Multiple Cleavages and Activationmentioning

confidence: 99%

“…signals for downstream processes. In Arabidopsis, damage-induced intracellular Ca 2+ flux activates Metacaspase 4 (AtMC4) to process substrate Propep1 very precisely in time and space to initiate the immune response 4 .…”

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confidence: 99%

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Structural Basis for Ca²⁺-Dependent Activation of a Plant Metacaspase

Zhu

Wang

et al. 2020

Preprint

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AbstractPlants metacaspases mediate programmed cell death in development 1,2, biotic and abiotic stresses 3, damage-induced immune response 4, and resistance to pathogen attack 5. Most metacaspases require Ca2+ for their activation and substrate processing 6–8. However, the Ca2+-dependent activation mechanism remains elusive 9–11. Here we report the crystal structure of Metacaspase 4 from Arabidopsis thaliana (AtMC4) that modulates Ca2+-dependent, damage-induced plant immune defense. The AtMC4 structure exhibits an inhibitory conformation in which a large linker domain blocks activation and substrate access. In addition, the side chain of Lys225 in the linker domain blocks the active site by sitting directly between two catalytic residues. We show that the activation of AtMC4 and cleavage of its physiological substrate involve multiple cleavages in the linker domain upon activation by Ca2+. Our analysis provides insight into the Ca2+-dependent activation of AtMC4 and lays the basis for tuning its activity in response to stresses that may help engineer more sustainable crops for production of food and biofuel.

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A mutation in Asparagine‐Linked Glycosylation 12 (ALG12) leads to receptor misglycosylation and attenuated responses to multiple microbial elicitors

et al. 2020

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Changes in cellular calcium levels are one of the earliest signalling events in plants exposed to pathogens or other exogenous factors. In a genetic screen, we identified an Arabidopsis thaliana 'changed calcium elevation 1' (cce1) mutant with attenuated calcium response to the bacterial flagellin flg22 peptide and several other elicitors. Whole-genome resequencing revealed a mutation in asparagine-linked glycosylation 12 that encodes the mannosyltransferase responsible for adding the eighth mannose residue in an a-1,6 linkage to the dolichol-PP-oligosaccharide N-glycosylation glycan tree precursors. While properly targeted to the plasma membrane, misglycosylation of several receptors in the cce1 background suggests that N-glycosylation is required for proper functioning of client proteins.

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Damage on plants activates Ca ²⁺ -dependent metacaspases for release of immunomodulatory peptides

Cited by 183 publications

References 51 publications

Plant immunity in signal integration between biotic and abiotic stress responses

Plant immunity in signal integration between biotic and abiotic stress responses

Structural Basis for Ca²⁺-Dependent Activation of a Plant Metacaspase

A mutation in Asparagine‐Linked Glycosylation 12 (ALG12) leads to receptor misglycosylation and attenuated responses to multiple microbial elicitors

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Damage on plants activates Ca 2+ -dependent metacaspases for release of immunomodulatory peptides

Cited by 183 publications

References 51 publications

Plant immunity in signal integration between biotic and abiotic stress responses

Plant immunity in signal integration between biotic and abiotic stress responses

Structural Basis for Ca2+-Dependent Activation of a Plant Metacaspase

A mutation in Asparagine‐Linked Glycosylation 12 (ALG12) leads to receptor misglycosylation and attenuated responses to multiple microbial elicitors

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Damage on plants activates Ca ²⁺ -dependent metacaspases for release of immunomodulatory peptides

Structural Basis for Ca²⁺-Dependent Activation of a Plant Metacaspase