VPEγ Exhibits a Caspase-like Activity that Contributes to Defense against Pathogens

@article{Rojo2004VPEEA,
  title={VPE$\gamma$ Exhibits a Caspase-like Activity that Contributes to Defense against Pathogens},
  author={E. Rojo and Raquel Mart{\'i}n and C. Carter and J. Zouhar and S. Pan and Julia M. Plotnikova and Hailing Jin and M. Paneque and J. S{\'a}nchez-Serrano and B. Baker and F. Ausubel and N. Raikhel},
  journal={Current Biology},
  year={2004},
  volume={14},
  pages={1897-1906}
}
BACKGROUND Caspases are a family of aspartate-specific cysteine proteases that play an essential role in initiating and executing programmed cell death (PCD) in metazoans. Caspase-like activities have been shown to be required for the initiation of PCD in plants, but the genes encoding those activities have not been identified. VPEgamma, a cysteine protease, is induced during senescence, a form of PCD in plants, and is localized in precursor protease vesicles and vacuoles, compartments… Expand
A cellular suicide strategy of plants: vacuole-mediated cell death
TLDR
Plants might have evolved a VPE-mediated vacuolar system as a cellular suicide strategy through disrupting the vacuole in pathogenesis and development, and there is limited sequence identity between the two enzymes. Expand
Vacuolar Processing Enzyme Is Essential for Mycotoxin-induced Cell Death in Arabidopsis thaliana*
TLDR
In vivo and in vitro analyses demonstrate that γVPE is the proteinase that exhibits a caspase-1 activity that is a key molecule in toxin-induced cell death and suggest that a susceptible response of toxin- induced cell death is caused by the VPE-mediated vacuolar mechanism similar to a resistance response of hypersensitive cell death. Expand
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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. Expand
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TLDR
An unexpected, post-transcriptional up-regulation of γVPE activity is revealed during compatible, but not during incompatible interactions of Arabidopsis with Hyaloperonospora arabidopsidis (Hpa). Expand
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TLDR
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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. Expand
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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. Expand
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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. Expand
A VPE-like protease NtTPE8 exclusively expresses in the integumentary tapetum and is involved in seed development.
TLDR
A novel caspase-like cysteine protease, NtTPE8, exclusively expressed in the integumentary tapetum that is involved in seed development is identified and is the first specific molecular marker reported to date for this cell type. Expand
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