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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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The CED-3/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A.

Phylogenetic analysis of the CED-3/ICE family of cysteine proteases suggests the existence of a subfamily most related to the Caenorhabditis elegans death gene ced-3 and includes Yama (CPP32, apopain), LAP3 (Mch3, CMH1), and Mch2. Here, we show that Mch2 is processed from its zymogen form to a proteolytically active dimeric species during execution of the apoptotic program and by the cytotoxic T cell death protease granzyme B. Additionally, like Yama and LAP3, Mch2 functions downstream of the death inhibitors Bcl-2, Bcl-xL, and CrmA. Importantly, Mch2, but not Yama or LAP3, is capable of cleaving lamin A to its signature apoptotic fragment, indicating that Mch2 is an apoptotic laminase.[1]

References

  1. The CED-3/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A. Orth, K., Chinnaiyan, A.M., Garg, M., Froelich, C.J., Dixit, V.M. J. Biol. Chem. (1996) [Pubmed]
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