IndraLab

Statements

OTUD1 binds CTNNB1. 11 / 11
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"A direct interaction between OTUD1 and β-catenin was confirmed by BLI assay (KD = 2.10 × 10 −8 M; xref D)."
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"OTUD1 directly interacts with β-catenin."
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sparser
"These findings elucidate the OTUD1-β-catenin pathway’s role in endothelial dysfunction-associated angiogenesis and suggest OTUD1 as a promising therapeutic target for diabetic non-healing wounds."
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sparser
"Mechanistically, OTUD1 directly interacted with β-catenin, reducing its K63-linked ubiquitination at residues K496, K508, and K625 via its catalytic site C320."
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sparser
"To further refine the understanding of how β-catenin interacts with OTUD1, additional deletion mutants were constructed: His-β-catenin-Δ1-223 (aa 1–223), His-β-catenin-Δ1-330 (aa 1–330), and His-β-catenin-Δ1-473 (aa 1–473; xref H)."
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sparser
"Consistent with these results, immunofluorescence staining further demonstrated that the OTUD1-β-catenin interaction was significantly enhanced under HG + PA conditions and primarily colocalized in the cytoplasm of HUVECs ( xref E and F)."
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sparser
"To pinpoint the specific β-catenin motif that interacts with OTUD1, a series of β-catenin mutant plasmids was created, which lacked the NTD and CTD, retaining only the ARM domain ( xref H)."
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biogrid
No evidence text available
30323974
sparser
"In this study, we identified β-catenin as a novel substrate protein for OTUD1-mediated deubiquitination, demonstrated by the binding of both endogenous and exogenous β-catenin to OTUD1."
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sparser
"These findings suggest that OTUD1 interacts directly with the aa 473–664 region of the ARM domain of β-catenin."
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sparser
"Mechanistically, OTUD1 interacted with β-catenin and reduced its K63-linked ubiquitination at lysine residues K496, K508, and K625 through its catalytic site C320."
40300668