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Updated: Jun 3, 2026

Modeling Paracrine Noncanonical Wnt Signaling In Vitro
Published on: December 10, 2021
Mest/Peg1 inhibits Wnt signalling through regulation of LRP6 glycosylation
Hwajin Jung1, Suk Kyung Lee, Eek-hoon Jho
1Department of Life Science, The University of Seoul, 90 Jeonnong-dong, Dongdaemun-gu, Seoul 130-743, Korea.
Abstract:
Mest (mesoderm-specific transcript)/Peg1 (paternally expressed gene 1) is an imprinted gene that plays important roles in embryo development, although its biochemical role has not been determined. Ectopic expression of Mest/Peg1 inhibited Wnt-mediated reporter activity by enhancing the ubiquitination of β-catenin. The maturation and plasma membrane localization of the Wnt co-receptor LRP6 [LDLR (low-density lipoprotein receptor)-related protein 6], which are both necessary for Wnt signalling, were blocked by the expression of Mest/Peg1. Mest/Peg1 inhibited maturation of LRP6 by controlling the glycosylation of LRP6. Knockdown of Mest/Peg1, which might enhance Wnt signalling, blocked adipogenic differentiation of 3T3-L1 cells. Overall, our results suggest that Mest/Peg1 is a novel regulator of Wnt/β-catenin signalling during adipogenic differentiation.
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