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USP46 increases the amount of LRP6. 8 / 8
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"We propose a model in which the USP46 complex increases the steady-state level of cell surface LRP6 and facilitates the assembly of LRP6 into signalosomes via a pruning mechanism that removes sterically hindering ubiquitin chains."
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"The USP46 complex acts upstream of the destruction complex to increase the steady-state levels of LRP6."
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"We observed that expression of the USP46 complex increased the cell-surface levels of LRP6 but not the insulin receptor control (Fig. 3F)."
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"The enzymatic activity of USP46 is required for Wnt activity as a catalytically inactive version of USP46, USP46 , did not increase LRP6 levels (Fig. 5A) or potentiate Wnt signaling in HEK293 STF cells (Supplementary Fig. 6A)."
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"Thus, the enzymatic activity of the USP46 complex is required for its regulation of LRP6 levels.We next examined if the USP46 complex increases LRP6 levels by promoting its deubiquitylation and opposing the activity of RNF43, an E3 ligase for Wnt receptors."
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"Similarly, we found that treatment with Bafilomycin A blocked the decrease in LRP6 levels following knockdown of USP46 in LF203 cells (Supplementary Fig. 6F)."
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"We found that knockdown of USP46 decreased the viability of intestinal organoids and LRP6 and β-catenin levels (Fig. 5F and Supplementary Fig. 7A, B) and that this effect was more evident at lower concentrations of RSPO (corresponds to higher RNF43/ZNRF3 activities)."
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"Knockdown of USP46 decreases steady-state levels of LRP6 and increases the level of ubiquitylated LRP6."
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