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Judging from the fact that γ-GCS and GS proteins do not associate and that their gene expression is controlled differently [141], it is reasonable to consider that in certain situations, γ-GCS acts dominantly compared with GS and produces γ-glutamyl peptides other than glutathione

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Mutations in the DLG motif disrupt the low-affinity binding of Keap1 with Nrf2, resulting in the stabilization of Nrf2, although the association between Keap1 and Nrf2 through the high-affinity binding site, ETGE, is retained