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- W60233694 abstract "Keap1 is a BTB-Kelch substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex that functions as a sensor for thiol-reactive chemopreventive compounds and oxidative stress. Inhibition of Keap1-dependent ubiquitination of the bZIP transcription factor Nrf2 enables Nrf2 to activate a cytoprotective transcriptional program that counters the damaging effects of oxidative stress. In this report, we have identified a member of the phosphoglycerate mutase family, PGAM5, as a novel substrate for Keap1. The N-terminus of the PGAM5 protein contains a conserved NxESGE motif that binds to the substrate-binding pocket in the Kelch domain of Keap1, while the C-terminal PGAM domain binds Bcl-XL. Keap1-dependent ubiquitination of PGAM5 results in proteosome-dependent degradation of PGAM5. Quinone-induced oxidative stress and the chemopreventive agent sulforaphane inhibit Keap1-dependent ubiquitination of PGAM5. The identification of PGAM5 as a novel substrate of Keap1 suggests that Keap1 regulates both transcriptional and post-transcriptional responses of mammalian cells to oxidative stress." @default.
- W60233694 created "2016-06-24" @default.
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- W60233694 date "2007-01-01" @default.
- W60233694 modified "2023-10-16" @default.
- W60233694 title "PGAM5, a Bcl‐XL‐interacting protein, is a novel substrate for the redox‐regulated Keap1‐dependent ubiquitin ligase complex." @default.
- W60233694 doi "https://doi.org/10.1096/fasebj.21.6.a1022" @default.
- W60233694 hasPublicationYear "2007" @default.
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