IndraLab

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USP19 deubiquitinates LRP6. 5 / 6
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"Co-receptor LRP6 is deubiquitinated by USP19 to regulate its protein maturation and expression on the cell surface, whereas its ubiquitin ligases remained unidentified (Perrody et al. 2016)."

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"Upon release from this putative ubiquitin binding chaperone, LRP6 is deubiquitinated by USP19."

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"USP8 and USP6 constitutively deubiquitylate Fz, 65 , 66 , 67 , 68 whereas USP19 deubiquitylates LRP6 in the endoplasmic reticulum, facilitating its transport."

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"After the deubiquitylation of LRP6 by USP19, Wnt signaling was increased, which induced cell migration and invasion [51]."

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"Before ER exit, LRP6 is deubiquitinated by USP19 and palmitoylated, then transported through the Golgi to the plasma membrane where it acts as a Wnt signaling coreceptor [66,67] ."