What happened to plant caspases?

@article{Bonneau2008WhatHT,
  title={What happened to plant caspases?},
  author={Laurent Bonneau and Yuan Ge and Georgina E. Drury and Patrick Gallois},
  journal={Journal of experimental botany},
  year={2008},
  volume={59 3},
  pages={
          491-9
        }
}
The extent of conservation in the programmed cell death pathways that are activated in species belonging to different kingdoms is not clear. Caspases are key components of animal apoptosis; caspase activities are detected in both animal and plant cells. Yet, while animals have caspase genes, plants do not have orthologous sequences in their genomes. It is 10 years since the first caspase activity was reported in plants, and there are now at least eight caspase activities that have been measured… 
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Programmed Cell Death Regulation by Plant Proteases with Caspase-Like Activity
TLDR
Three plant proteases with caspase-like activity are identified: vacuolar processing enzyme (VPE), a legumain that cleaves caspases-1 synthetic substrates; phytaspase, a subtilisin-like protease that cleves casp enzyme-6 synthetic substrate; and the proteasome subunit PBA1 that has caspasing-3- like activity.
A plant alternative to animal caspases: subtilisin-like proteases
TLDR
Recent data showing that some caspase-like activities are attributable to the plant subtilisin-like proteases, saspases and phytaspases are reviewed, showing both common (D-specific protein fragmentation during PCD) and distinct (enzyme structure and activity regulation) features with animal PCD-related proteases.
Plant phytaspases and animal caspases: structurally unrelated death proteases with a common role and specificity.
TLDR
It is shown that a plant serine-dependent protease, phytaspase, shares cleavage specificity and a role in PCD analogous to that of caspases, however, regulation of phytspase-mediated cleavage of intracellular target proteins appears to be attained not at the level of proenzyme processing/activation, which occurs, in the case ofphytasp enzyme, autocatalytically and constitutively.
Inhibition of cathepsin B by caspase-3 inhibitors blocks programmed cell death in Arabidopsis
TLDR
Cathepsin B triple mutants showed a strong reduction in the PCD induced by ultraviolet (UV), oxidative stress (H2O2, methyl viologen) or endoplasmic reticulum stress, which contributes to explain why caspase-3 inhibitors inhibit plant PCD and provide new tools to further plant PCd research.
Inhibition of cathepsin B by caspase-3 inhibitors blocks programmed cell death in Arabidopsis
TLDR
Cathepsin B triple mutants showed a strong reduction in the PCD induced by ultraviolet (UV), oxidative stress (H2O2, methyl viologen) or endoplasmic reticulum stress, which contributes to explain why caspase-3 inhibitors inhibit plant PCD and provide new tools to further plant PCd research.
DEVDase activity is induced in potato leaves during Phytophthora infestans infection.
Plant life needs cell death, but does plant cell death need Cys proteases?
TLDR
The role of papain‐like Cys proteases, vacuolar processing enzymes, and metacaspases in PCD during the development of tracheary elements, seed coat, suspensor, and tapetum, and during the hypersensitive response is discussed.
Phytaspase, a relocalisable cell death promoting plant protease with caspase specificity
TLDR
The identification and characterisation of a novel PCD‐related subtilisin‐like protease from tobacco and rice named phytaspase (plant aspartate‐specific protease) that possesses caspase specificity distinct from that of other known caspases‐ like proteases is reported.
Protease signaling in animal and plant‐regulated cell death
TLDR
Some similarities are found among animal and plant cell death proteases but, overall, the pathways that they govern are kingdom‐specific with very little overlap.
Vacuolar processing enzyme in plant programmed cell death
TLDR
The current knowledge on the contribution of VPE to plant PCD and its role in vacuole-mediated cell death is summarized, and VPE is compared with the animal cell death executor caspase 1.
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