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USP15 deubiquitinates KEAP1. 8 / 9
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"Here we report that the deubiquitinating enzyme, USP15, specifically deubiquitinates Keap1, which suppresses the Nrf2 pathway."

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"For example, USP15 is able to deubiquitinate KEAP1 (that can be ubiquitinated by the same E3 ligase complex that ubiquitinates NRF2), resulting in lower protein levels of NRF2 [99]."

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"A previous study reported that KEAP1 could be deubiquitinated and stabilized by USP15 and thus promotes NRF2 degradation [38]."

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"45 In addition, USP15 mediates the deubiquitination of Keap1–Cul3, a E3-ligase of NRF2, which increases degradation of NRF2 and reverses the resistance of cancer cells to radiotherapy and chemotherapy[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"USP15 deubiquitinates Keap1."

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"Zhang et al.'s research demonstrated that USP15 deubiquitinates Keap1, enhancing its E3 ligase activity and prolonging Nrf2 ubiquitination, thus suppressing the Nrf2-dependent antioxidant response."

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"Keap1 is deubiquitinated by USP15, which also stabilizes and improves the E3 ligase activity of the Keap1–Cul3–E3 complex [39,45]."

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"USP15 activates ubiquitin ligase activity by deubiquitinating Keap1 as its adaptor, promoting the proteasomal degradation of Nrf2."