Plant phytaspases and animal caspases: structurally unrelated death proteases with a common role and specificity

Nina V. Chichkova, Alexander I. Tuzhikov, Michael Taliansky, Andrey B. Vartapetian

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    28 Citations (Scopus)


    Proteases with an aspartate cleavage specificity are known to contribute to programmed cell death (PCD) in animals and plants. In animal cells this proteolytic activity belongs to caspases, a well-characterized family of cysteine-dependent death proteases. Plants, however, lack caspase homologs and thus the origin of this type of proteolytic activity in planta was poorly understood. Here, we review recent data demonstrating that a plant serine-dependent protease, phytaspase, shares cleavage specificity and a role in PCD analogous to that of caspases. However, unlike caspases, regulation of phytaspase-mediated cleavage of intracellular target proteins appears to be attained not at the level of proenzyme processing/activation, which occurs, in the case of phytaspase, autocatalytically and constitutively. Rather, the mature phytaspase is excluded from healthy cells into the apoplast and is allowed to re-enter cells upon the induction of PCD. Thus, PCD-related proteases in animals and plants display both common features and important distinctions.

    Original languageEnglish
    Pages (from-to)77-84
    Number of pages8
    JournalPhysiologia Plantarum
    Issue number1
    Publication statusPublished - May 2012

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