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OTUD1 binds KEAP1. 33 / 33
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"Oikawa et al. (2022) further confirmed KEAP1-OTUD1 interaction and showed that KEAP1 K63 ubiquitination levels were elevated in OTUD1-deficient mouse embryonic fibroblasts, while overexpression of wild-type OTUD1 (but not an ETGE-lacking mutant) reduced KEAP1 ubiquitination in HEK293T cells."
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"Mass spectrometric analysis showed that OTUD1 binds KEAP1, and the N-terminal intrinsically disordered region of OTUD1, which contains an ETGE motif, is indispensable for the KEAP1-binding."
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"OTUD1 directly bound with KEAP1, and PGAM5 co-precipitated with OTUD1 only in the presence of KEAP1 (Supplementary Fig. 5d)."
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"Our mass spectrometric analysis reveals that OTUD1 binds KEAP1, a regulator of the transcription factor Nrf2, during ROS-induced oxidative stress [ xref ] ( xref C)."
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"The E3-ligase KEAP1 binds and ubiquitinates OTUD1."
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"The DLG and ETGE motifs in the Neh2 domain of NRF2 are crucial for KEAP1-binding [26], and the C-terminal Kelch domain of KEAP1 binds NRF2 as well as OTUD1."
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"Thus, the biological relevance of the KEAP1-OTUD1 complex remains to be elucidated."
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"Though KEAP1 directly interacts and ubiquitinates OTUD1, this modification did not alter OTUD1 protein content."
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"The KEAP1-binding of OTUD1 has been independently confirmed [ xref ]."
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"Although the authors identify that OTUD1 binds KEAP1, a substrate adaptor of the CUL3-dependent E3 complex, the cellular function of the association remains to be elucidated."
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"Mass spectrometric analysis showed that OTUD1 binds KEAP1, and the N-terminal intrinsically disordered region of OTUD1, which contains an ETGE motif, is indispensable for the KEAP1-binding."
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"Oikawa D et al. demonstrated through mass spectrometric analysis that OTUD1 can bind to KEAP1 via an ETGE motif (Oikawa et al., 2022)."
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"Given the pivotal role of the ETGE motif in mediating NRF2 binding with KEAP1, our subsequent inquiry aimed to ascertain whether OTUD1 also interacted with KEAP1 through its ETGE motif."
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"Thus, the biological relevance of the KEAP1-OTUD1 complex remains to be elucidated.In summary, our work unveils the OTUD1-PRDX4 axis as a yet undescribed regulatory pathway driving Ig production and PI sensitivity in MM cells and highlights importance of OTUD1 in myeloma proliferation (Fig. 8)."
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"This clearly indicates that KEAP1 and OTUD1 interact at the endogenous level."
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"Our mass spectrometric analysis reveals that OTUD1 binds KEAP1, a regulator of the transcription factor Nrf2, during ROS-induced oxidative stress [19] (Figure 5C)."
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"Co-IP results demonstrated that both OTUD1-WT and M1 mutant interacted with KEAP1, whereas the M2 and M3 mutants did not exhibit any interaction ( xref G), demonstrating that the ETGE motif, rather than the C320 residue of OTUD1, which mediated its binding with KEAP1."
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"The KEAP1-binding of OTUD1 has been independently confirmed [51]."
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"Oikawa D et al. demonstrated through mass spectrometric analysis that OTUD1 can bind to KEAP1 via an ETGE motif ( xref )."
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"The E3-ligase KEAP1 binds and ubiquitinates OTUD1."
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"First, we validated the OTUD1-KEAP1 interaction by reciprocal co-immunoprecipitation using HA-tagged OTUD1 and Flag-tagged KEAP1 (Fig.  xref )."
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"Deletion of this motif completely disrupted the association of OTUD1 with KEAP1 (Fig.  xref ), providing additional evidence for the direct protein-protein binding."
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"We detected the endogenous association of KEAP1 and OTUD1 (Fig. xref )."
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"These results clearly indicated that the OTUD1-KEAP1 interaction exists under physiological conditions."
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"It is highly likely that ROS production and oxidative damage are involved in the regulation of these cell functions and diseases related to OTUD1, and the KEAP1–OTUD1 axis plays an important role."
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"OTUD1 directly bound with KEAP1, and PGAM5 co-precipitated with OTUD1 only in the presence of KEAP1 (Supplementary Fig. xref )."
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