IndraLab

Statements

TLN2 binds OTUB1. 7 / 7
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sparser
"In summary, OTUB1 directly interacts with Talin2 and mediates its stabilization through a non‐canonical deubiquitination mechanism."
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sparser
"OTUB1 Interacts with Talin2 and Promotes Its K48‐Linked Non‐Canonical Deubiquitination."
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sparser
"Exogenous coimmunoprecipitation (Co‐IP) was consistent with MD simulations and indicated a direct interaction between OTUB1 and Talin2 (Figure  xref )."
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sparser
"Crucially, we identified a specific interaction between Talin2 and OTUB1, enabling a novel precision therapeutic strategy: targeted small‐molecule inhibitors designed to disrupt Talin2/OTUB1 binding affinity. [ xref ] This approach achieves dual therapeutic effects by accelerating Talin2 degradation, blocking mechano‐inflammatory signal conversion, and promoting ECM synthesis."
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sparser
"Endogenous co‐immunoprecipitation (Co‐IP) assays confirmed the interaction between OTUB1 and Talin2 under intracellular conditions (Figure  xref )."
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reach
"Furthermore, mechanical loading potentiates the Talin2/OTUB1 interaction, resulting in the stabilization of Talin2 and enhances non-canonical deubiquitination."
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reach
"Given that Talin2 is stabilized and deubiquitinated by OTUB1, especially under mechanical load, the Talin2/OTUB1 interaction may be a promising therapeutic target for FJOA."
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