MID1 and MID2 regulate cell migration and epithelial-mesenchymal transition via modulating Wnt/β-catenin signaling.

ABSTRACT:

Background

The ubiquitin E3 ligase activity has been ascribed to MID1, the causative gene of X-linked OS, and its homologue, MID2. Both alpha4, the common MID protein partner, and PP2Ac in MID-alpha4-PP2Ac complexes can be ubiquitylated. Ubiquitylation of alpha4 converted its function toward PP2Ac from protective to destructive, while PP2A also affected MID protein phosphorylation and their subsequent trafficking on microtubules. It was believed that disruption of the function of MID1-alpha4-PP2A complex was vital to the pathogenesis of craniofacial malformation, the most prominent clinical manifestation of OS, although the detailed molecular mechanisms was not unravelled.

Methods

The cellular level of PP2A and phosphor-PP2A in cells overexpressing MID1/MID2 or in cells with

SUBMITTER: Qiao Y 

PROVIDER: S-EPMC7475493 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature