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Mammalian proapoptotic factor ChaC1 and its homologues function as γ‐glutamyl cyclotransferases acting specifically on glutathione
Author(s) -
Kumar Akhilesh,
Tikoo Shweta,
Maity Shuvadeep,
Sengupta Shantanu,
Sengupta Sagar,
Kaur Amandeep,
Kumar Bachhawat Anand
Publication year - 2012
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/embor.2012.156
Subject(s) - glutathione , endoplasmic reticulum , cytosol , microbiology and biotechnology , mutant , function (biology) , biochemistry , biology , yeast , gpx6 , chemistry , enzyme , gene , glutathione peroxidase
ChaC1 is a mammalian proapoptic protein of unknown function induced during endoplasmic reticulum stress. We show using in vivo studies and novel in vitro assays that the ChaC family of proteins function as γ‐glutamyl cyclotransferases acting specifically to degrade glutathione but not other γ‐glutamyl peptides. The overexpression of these proteins (but not the catalytically dead E>Q mutants) led to glutathione depletion and enhanced apoptosis in yeast. The ChaC family is conversed across all phyla and represents a new pathway for glutathione degradation in living cells, and the first cytosolic pathway for glutathione degradation in mammalian cells.