Caspases in plants: metacaspase gene family in plant stress responses

Fagundes, David Gabriel dos Santos; Bohn, Bianca; Cabreira, Caroline; Leipelt, Fábio; Dias, Nathalia de Cassia; Bodanese‐Zanettini, Maria Helena; Cagliari, Alexandro

doi:10.1007/s10142-015-0459-7

Cited by 77 publications

(68 citation statements)

References 103 publications

(141 reference statements)

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“…Finally, in plants, fungi and protists, the caspase-like counterparts known as metacaspases are essential to plant PCD, particularly under several stress conditions [113]. However, despite their functional homology as well as some sequence similarities with caspases, metacaspases also bear striking differences such as cleaving of their substrates after an arginine or lysine residue, instead of aspartate [113], [114].…”

Section: Functional Conservation Of the Caspase-autophagy Cross-regulmentioning

confidence: 99%

“…However, despite their functional homology as well as some sequence similarities with caspases, metacaspases also bear striking differences such as cleaving of their substrates after an arginine or lysine residue, instead of aspartate [113], [114]. Their involvement in controlling autophagic flux has been documented in vacuolar PCD (vPCD) during plant development [113], [115], [116] where activity of type IImetacaspase (mcII-Pa) was detected prior to vPCD of embryo-supporting tissue [116].…”

Section: Functional Conservation Of the Caspase-autophagy Cross-regulmentioning

confidence: 99%

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Caspase involvement in autophagy

2017

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Caspases are a family of cysteine proteases widely known as the principal mediators of the apoptotic cell death response, but considerably less so as the contributors to the regulation of pathways outside cellular demise. In regards to autophagy, the modulatory roles of caspases have only recently begun to be adequately described. In contrast to apoptosis, autophagy promotes cell survival by providing energy and nutrients through the lysosomal degradation of cytoplasmic constituents. Under basal conditions autophagy and apoptosis cross-regulate each other through an elaborate network of interconnections which also includes the interplay between autophagyrelated proteins (ATGs) and caspases. In this review we focus on the effects of this crosstalk at the cellular level, as we aim to concentrate the main observations from research conducted so far on the fine-tuning of autophagy by caspases. Several members of this protease-family have been found to directly interact with key ATGs involved in different tiers across the autophagic cascade. Therefore, we firstly outline the core mechanism of macroautophagy in brief. In an effort to emphasize the importance of the intricate cross-regulation of ATGs and caspases, we also present examples drawn from Drosophila and plant models regarding the contribution of autophagy to apoptotic cell death during normal development. Keywords and abbreviationsautophagy; macroautophagy; mammals; caspases; apoptosis; crosstalk; regulation AMBRA-1Activating-molecule-in-Beclin1-regulated-autophagy-1 AMPK AMP-activated-protein-kinase ATG Autophagy-related gene ATG14L ATG14-likeBcl-2 B-cell lymphoma 2 • Autophagy is implicated in many physiological and pathological processes, where apoptosis is also involved DISC Death-inducing signalling complex FADD Fas-associated protein with death domain Open Questions• Does control of autophagy by caspases represent a central or a supplementary mode of regulation of this pathway?• Is caspase activation required to control autophagy?• To what extent do caspases affect autophagy and how exactly their effects on the pathway vary across different contexts?4

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Section: Functional Conservation Of the Caspase-autophagy Cross-regulmentioning

confidence: 99%

Section: Functional Conservation Of the Caspase-autophagy Cross-regulmentioning

confidence: 99%

Caspase involvement in autophagy

2017

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“…Our results from these structure–function relationship studies indicate that the distinct biochemical profiles for the AtMC4 and AtMC9 subclasses of type‐II MCs are the result of multiple inter‐domain interactions within each of these proteases. Although there are highly conserved motifs that are shared between their p20, linker and p10 domains, as well as with other types of MCs (Coll et al ., ; Lam and Zhang, ; Fagundes et al ., ), we nevertheless would predict that there are distinctive ‘signature’ residues in each of these three domains that are conserved between the homologs of these two proteases in various plant species, but are rarely shared between the two subclasses. Taking this phylogenomic approach, we searched among well‐annotated plant genomes in GenBank for homologs of AtMC4 and AtMC9 at key branch points during the diversification of land plants from moss to seed plants.…”

Section: Resultsmentioning

confidence: 88%

Domain swap between two type‐II metacaspases defines key elements for their biochemical properties

Fortin

Lam

2018

The Plant Journal

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Type-II metacaspases are conserved cysteine proteases found in eukaryotes with oxygenic photosynthesis, including green plants and some algae, such as Chlamydomonas and Volvox. Genetic and biochemical studies showed that some members in this protease family could be involved in oxidative stress-induced cell death in higher plants, but their regulatory mechanisms remain unclear. Biochemically, two distinct classes of type-II metacaspases are exemplified by AtMC4 and AtMC9 from Arabidopsis, with AtMC4 activation dependent on calcium under neutral pH, whereas AtMC9 is active only under mildly acidic pH, regardless of the availability of calcium. Here, we constructed all six possible combinations between the p20, linker, and p10 domains from AtMC4 and AtMC9. Our results show that calcium stimulation of AtMC4 activity is associated with essential amino acids located in its p20 domain. In contrast, the acidic pH optimum trait is lost from AtMC9 if one or two of its domains are replaced by that from AtMC4, suggesting that multiple interactions between domains in AtMC9 may be responsible for this property. Consistent with this, we found conserved 'signature' residues in each of the three domains that distinguish AtMC4- and AtMC9-like classes of metacaspases. Tracing the origin of the AtMC9 class, we found evidence for its appearance between lycophytes and gymnosperms, coincident with the evolution of more complex root archetypes in terrestrial plants. Our work suggests that the distinctive properties of the AtMC9-like protease could be associated with special cellular physiology in the roots of gymnosperms and angiosperms that are distinct from lycophytes.

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“…Nine metacaspases have been identified in Arabidopsis , AtMC1 to AtMC9, and their homologs, i.e., ZmMC1 to ZmMC9, were found in maize (Minina et al, 2013). Though these proteins differ from their animal counterparts, plant metacaspases are markers of PCD (Lam and del Pozo, 2000; Tsiatsiani et al, 2011; Fagundes et al, 2015). Microarray analyses revealed that two type II metacaspases are differentially expressed in maize endosperms: mc7 is up-regulated in MEC, while mc9 is up-regulated in MEP (Table S2), suggesting different PCD pathways in these two areas.…”

Section: Resultsmentioning

confidence: 99%

Responses to Hypoxia and Endoplasmic Reticulum Stress Discriminate the Development of Vitreous and Floury Endosperms of Conventional Maize (Zea mays) Inbred Lines

et al. 2017

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Major nutritional and agronomical issues relating to maize (Zea mays) grains depend on the vitreousness/hardness of its endosperm. To identify the corresponding molecular and cellular mechanisms, most studies have been conducted on opaque/floury mutants, and recently on Quality Protein Maize, a reversion of an opaque2 mutation by modifier genes. These mutant lines are far from conventional maize crops. Therefore, a dent and a flint inbred line were chosen for analysis of the transcriptome, amino acid, and sugar metabolites of developing central and peripheral endosperm that is, the forthcoming floury and vitreous regions of mature seeds, respectively. The results suggested that the formation of endosperm vitreousness is clearly associated with significant differences in the responses of the endosperm to hypoxia and endoplasmic reticulum stress. This occurs through a coordinated regulation of energy metabolism and storage protein (i.e., zein) biosynthesis during the grain-filling period. Indeed, genes involved in the glycolysis and tricarboxylic acid cycle are up-regulated in the periphery, while genes involved in alanine, sorbitol, and fermentative metabolisms are up-regulated in the endosperm center. This spatial metabolic regulation allows the production of ATP needed for the significant zein synthesis that occurs at the endosperm periphery; this finding agrees with the zein-decreasing gradient previously observed from the sub-aleurone layer to the endosperm center. The massive synthesis of proteins transiting through endoplasmic reticulum elicits the unfolded protein responses, as indicated by the splicing of bZip60 transcription factor. This splicing is relatively higher at the center of the endosperm than at its periphery. The biological responses associated with this developmental stress, which control the starch/protein balance, leading ultimately to the formation of the vitreous and floury regions of mature endosperm, are discussed.

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Caspases in plants: metacaspase gene family in plant stress responses

Cited by 77 publications

References 103 publications

Caspase involvement in autophagy

Caspase involvement in autophagy

Domain swap between two type‐II metacaspases defines key elements for their biochemical properties

Responses to Hypoxia and Endoplasmic Reticulum Stress Discriminate the Development of Vitreous and Floury Endosperms of Conventional Maize (Zea mays) Inbred Lines

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