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

Kim Orth, Arul M. Chinnaiyan, Manish Garg, Christopher J. Froelich, Vishva M. Dixit

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Abstract

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-X(L), 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.

Original languageEnglish (US)
Pages (from-to)16443-16446
Number of pages4
JournalJournal of Biological Chemistry
Volume271
Issue number28
DOIs
StatePublished - Jul 30 1996

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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