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- W2599180871 abstract "Significance We have recently reported that glutamine synthetase (GS) is negatively regulated by glutamine through a feedback loop involving the E3 ubiquitin ligase CRL4 CRBN . However, the molecular events that take place at each step of the pathway are not well understood. Here, we show that valosin-containing protein (VCP)/p97, is required for GS degradation. It acts downstream of CRL4 CRBN . p97 extracts ubiquitylated GS subunits from the decamer so that they can be degraded by the proteasome. Interestingly, p97 is also required for immunomodulatory drug-induced degradation of all four known CRL4 CRBN neosubstrates, including Ikaros family zinc finger proteins 1 (IKZF1) and 3 (IKZF3), casein kinase 1α (CK1α), and the translation termination factor GSPT1, which accounts for antitumor activity of these drugs. Our findings could have important implications for patient responsiveness to cancer therapy with immunomodulatory drugs." @default.
- W2599180871 created "2017-04-07" @default.
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- W2599180871 creator A5057194961 @default.
- W2599180871 creator A5057444662 @default.
- W2599180871 creator A5066867755 @default.
- W2599180871 date "2017-03-20" @default.
- W2599180871 modified "2023-10-16" @default.
- W2599180871 title "p97/VCP promotes degradation of CRBN substrate glutamine synthetase and neosubstrates" @default.
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- W2599180871 doi "https://doi.org/10.1073/pnas.1700949114" @default.
- W2599180871 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5389304" @default.
- W2599180871 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28320958" @default.
- W2599180871 hasPublicationYear "2017" @default.
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