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- W3174204214 abstract "Dusty, a dual serine/threonine/tyrosine protein kinase is broadly expressed and highly conserved in vertebrates from fish to human. To gain initial insight into its functions, we performed yeast two-hybrid screen to identify its interacting partners. Using the non-kinase domain of human Dusty as bait, Keap1, a member of BTB/Kelch protein family, was identified. We then used in vitro binding and GST pull-down assays to determine the specificity of this interaction and map the binding sites. The data confirmed that Dusty specifically interacted with Keap1, not other members of the Kelch family and that the N2 domain of Dusty and the Kelch domain of Keap1 are both necessary and sufficient to mediate the binding. We further used indirect immunoflurescence microscopy and coimmunoprecipitation to characterize this interaction. The results showed that Dusty and Keap1 were colocalized in cytoplasm, and could be coimmunoprecipitated from the cells expressing both of them. Given the link of Keap1 to Nrf2 in oxidative and xenobiotic stresses, we performed in vitro binding assay to assess the role of Dusty in Nrf2/Keap1 interaction. We found that Dusty competed with Nrf2 in binding to Keap1. These results suggest that Dusty exerts its direct effects on Keap1, thereby participating in Keap1/Nrf2-mediated stress response and in Keap1-involved other signal transduction pathways." @default.
- W3174204214 created "2021-07-05" @default.
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- W3174204214 date "2006-03-01" @default.
- W3174204214 modified "2023-10-16" @default.
- W3174204214 title "Dusty Protein Kinase Interacts Directly with Keap1, a Member of the Kelch Protein Superfamily" @default.
- W3174204214 doi "https://doi.org/10.1096/fasebj.20.4.a104" @default.
- W3174204214 hasPublicationYear "2006" @default.
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