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Evolutionary Diversity and Function of Metacaspases in Plants: Similar to but Not Caspases

Journal

Publisher

MDPI
DOI: 10.3390/ijms23094588

Keywords

caspase; metacaspase; programmed cell death; protease; autophagy

Funding

  1. National Research Foundation of Korea (NRF) - Korea government (MEST), Korea [18A18297611]

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Plants have metaCaspases instead of caspases, which play critical roles in programmed cell death during plant development and defense responses. The diversity in the number of metaCaspases in different plant species suggests varying functions due to diverse evolutions.
Caspase is a well-studied metazoan protease involved in programmed cell death and immunity in animals. Obviously, homologues of caspases with evolutionarily similar sequences and functions should exist in plants, and yet, they do not exist in plants. Plants contain structural homologues of caspases called metacaspases, which differ from animal caspases in a rather distinct way. Metacaspases, a family of cysteine proteases, play critical roles in programmed cell death during plant development and defense responses. Plant metacaspases are further subdivided into types I, II, and III. In the type I Arabidopsis MCs, AtMC1 and AtMC2 have similar structures, but antagonistically regulate hypersensitive response cell death upon immune receptor activation. This regulatory action is similar to caspase-1 inhibition by caspase-12 in animals. However, so far very little is known about the biological function of the other plant metacaspases. From the increased availability of genomic data, the number of metacaspases in the genomes of various plant species varies from 1 in green algae to 15 in Glycine max. It is implied that the functions of plant metacaspases will vary due to these diverse evolutions. This review is presented to comparatively analyze the evolution and function of plant metacaspases compared to caspases.

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