Am J Cancer Res 2013;3(1):96-106
Original Article
SUMO modification of menin
Zi-Jie Feng, Buddha Gurung, Guang-Hui Jin, Xiao-Lu Yang, Xian-Xin Hua
Department of Basic Medical Sciences, Medical College, Xiamen University, Xiamen, Fujian, China 361005; Abramson Family
Cancer Re-search Institute, Department of Cancer Biology, Abramson Cancer Center, University of Pennsylvania Perelman
School of Medicine, 421 Curie Blvd., Philadelphia, PA 19104, USA
Received November 19, 2012; Accepted December 27, 2012; Epub January 18, 2013; Published January 25, 2013
Abstract: 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. (ajcr0000160).
Keywords: Menin, SUMOylation, SUMO1, K591R
Address all correspondence to:
Dr. Xian-xin Hua
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.
Phone: 215-7465567; Fax: 215-7465525
E-mail: huax@mail.med.upenn.edu
Original Article
SUMO modification of menin
Zi-Jie Feng, Buddha Gurung, Guang-Hui Jin, Xiao-Lu Yang, Xian-Xin Hua
Department of Basic Medical Sciences, Medical College, Xiamen University, Xiamen, Fujian, China 361005; Abramson Family
Cancer Re-search Institute, Department of Cancer Biology, Abramson Cancer Center, University of Pennsylvania Perelman
School of Medicine, 421 Curie Blvd., Philadelphia, PA 19104, USA
Received November 19, 2012; Accepted December 27, 2012; Epub January 18, 2013; Published January 25, 2013
Abstract: 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. (ajcr0000160).
Keywords: Menin, SUMOylation, SUMO1, K591R
Address all correspondence to:
Dr. Xian-xin Hua
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.
Phone: 215-7465567; Fax: 215-7465525
E-mail: huax@mail.med.upenn.edu
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American Journal of Cancer Research
| ISSN: 2156-6976 |