IndraLab

Statements


USP46 deubiquitinates LRP6. 8 / 8
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"These results indicate that the USP46 complex promotes the deubiquitylation of LRP6 at the plasma membrane, thereby increasing its stabilization and opposing the action of the Wnt receptor ubiquitin ligases, RNF43 and ZNRF."

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"By reducing Arrow/LRP6 ubiquitylation, the Usp46 complex increases Arrow/LRP6 stability and cell surface levels, thereby enhancing the sensitivity of target cells to Wingless stimulation."

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"By reducing Arrow/LRP6 ubiquitylation and turnover and thus increasing cell surface Arrow levels, Usp46 enhances the sensitivity of target cells to Wingless stimulation."

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"The USP46 complex deubiquitylates LRP6 to promote Wnt/beta-catenin signaling."

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"Knockdown of USP46 decreases steady-state levels of LRP6 and increases the level of ubiquitylated LRP6."

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"Herein, we demonstrate that the USP46 complex is required for Wnt signaling in cultured human cells, Xenopus embryos, zebrafish embryos, and mouse intestinal organoids, indicating evolutionary conservation of function.We show that in response to Wnt pathway activation, the USP46 complex is recruited to and deubiquitylates cell surface LRP6, blocking its turnover."

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"USP46 inhibits the ubiquitylation of LRP6."

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"The USP46 complex blocks ubiquitylation/degradation of the Wnt co-receptor LRP6 [33]."