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-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.

Keywords

LaminProteaseCell biologyApoptosisSubstrate (aquarium)ChemistryBiologyBiochemistryEnzymeNucleusEcology

MeSH Terms

AlkaloidsAmino Acid SequenceApoptosisCaspase 6Cell LineCysteine EndopeptidasesEnzyme ActivationHumansHydrolysisLamin Type ALaminsMolecular Sequence DataNuclear ProteinsStaurosporineSubstrate Specificity

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Publication Info

Year
1996
Type
article
Volume
271
Issue
28
Pages
16443-16446
Citations
459
Access
Closed

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Cite This

Kim Orth, Arul M. Chinnaiyan, Manish Garg et al. (1996). The CED-3/ICE-like Protease Mch2 Is Activated during Apoptosis and Cleaves the Death Substrate Lamin A. Journal of Biological Chemistry , 271 (28) , 16443-16446. https://doi.org/10.1074/jbc.271.28.16443

Identifiers

DOI
10.1074/jbc.271.28.16443
PMID
8663580

Data Quality

Data completeness: 86%