SUMO modification of menin.
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.
Department 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.
Zi-Jie
ZJ
Feng
Buddha
B
Gurung
Guang-Hui
GH
Jin
Xiao-Lu
XL
Yang
Xian-Xin
XX
Hua
K591R; Menin; SUMO1; SUMOylation