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Subcellular localization of truncated MAGEL2 proteins: insight into the molecular pathology of Schaaf-Yang syndrome

Centeno-Pla, M.; Alcaide-Consuegra, E.; Gibson, S.; Prat-Planas, A.; Gutierrez-Avila, J. D.; Grinberg, D.; Urreizti, R.; Rabionet, R.; Balcells, S.

2024-01-23 molecular biology
10.1101/2024.01.22.576607 bioRxiv
Show abstract

Schaaf-Yang syndrome (SYS) is an ultra-rare neurodevelopmental disorder caused by truncating mutations in MAGEL2. Heterologous expression of wild-type (WT) or a truncated (p.Gln638*) C-terminal HA-tagged MAGEL2 revealed a shift from a primarily cytoplasmic to a more nuclear localization for the truncated protein variant. We now extend this analysis to six additional SYS mutations on a N-terminal FLAG-tagged MAGEL2. Our results replicate and extend our previous findings, showing that all the truncated MAGEL2 proteins consistently display a predominant nuclear localization, irrespective of the C-terminal or N-terminal position and the chemistry of the tag. The variants associated with arthrogryposis multiplex congenita (AMC) display a more pronounced nuclear retention phenotype, suggesting a correlation between clinical severity and the degree of nuclear mis-localization. These results point to a neomorphic effect of truncated MAGEL2, which might contribute to the pathogenesis of SYS.

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