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USP19 deubiquitinates LRP6. 6 / 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."
27751231
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"We show that folding of the Wnt signaling coreceptor <span class="match term1">LRP6</span> is promoted by ubiquitination of a specific lysine, retaining it in the ER while avoiding degradation. Subsequent ER exit requires removal of ubiquitin from this lysine by the deubiquitinating enzyme <span class="match term0">USP19</span>."
27751231
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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."
39520379
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"After the deubiquitylation of LRP6 by USP19, Wnt signaling was increased, which induced cell migration and invasion [51]."
36646950
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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] ."
34802913