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Am J Cancer Res. 2013;3(1):96-106. Epub 2013 Jan 18.

SUMO modification of menin.

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  • 1Department of Basic Medical Sciences, Medical College, Xiamen University Xiamen, Fujian, China 361005 ; Abramson Family Cancer Research Institute, Department of Cancer Biology, Abramson Cancer Center, University of Pennsylvania Perelman School of Medicine 421 Curie Blvd., Philadelphia, PA 19104, USA.


Menin acts as contextual a tumor suppressor and a tumor promoter, partly via epigenetic regulation of gene transcription. While menin is phosphorylated, it remains unclear whether wild type menin has other post-translational modifications. Here, we report that menin is SUMOylated by SUMO1 in vivo and in vitro, and the SUMOylation is reduced by a SUMO protease. Lysine 591 of menin was covalently modified by SUMO1 and K591R mutation in menin blocked SUMOylation of the C-terminal part of menin in transfected cells. Full-length menin with K591 mutation was still SUMOylated in vivo, suggesting the existence of multiple SUMOylation sites. Menin K591R mutant or menin-SUMO fusion protein still retains the ability to regulate cell proliferation and the expression of the examined menin target genes.


K591R; Menin; SUMO1; SUMOylation

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