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International Journal of Endocrinology
Volume 2014, Article ID 535401, 6 pages
http://dx.doi.org/10.1155/2014/535401
Research Article

FBP1 Is an Interacting Partner of Menin

1Metabolic Diseases Branch, National Institute of Diabetes and Digestive and Kidney Diseases, NIH, Building 10, Room 9C-103, 9000 Rockville, Bethesda, MD 20892, USA
2Departments of Biochemistry & Molecular Biology and Molecular & Cellular Biology, Baylor College of Medicine, Houston, TX 77030, USA
3Laboratory of Pathology, National Cancer Institute, NIH, Bethesda, MD 20892, USA

Received 29 April 2014; Revised 30 June 2014; Accepted 1 July 2014; Published 14 July 2014

Academic Editor: Khalid Hussain

Copyright © 2014 Shadia Zaman et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Multiple endocrine neoplasia type 1 (MEN1) is a syndrome characterized by tumors in multiple endocrine tissues such as the parathyroid glands, the pituitary gland, and the enteropancreatic neuroendocrine tissues. MEN1 is usually caused by mutations in the MEN1 gene that codes for the protein menin. Menin interacts with proteins that regulate transcription, DNA repair and processing, and maintenance of cytoskeletal structure. We describe the identification of FBP1 as an interacting partner of menin in a large-scale pull-down assay that also immunoprecipitated RBBP5, ASH2, and LEDGF, which are members of complex proteins associated with SET1 (COMPASS), a protein complex that methylates histone H3. This interaction was confirmed by coimmunoprecipitation and Flag-pull-down assays. Furthermore, menin localized to the FUSE site on the MYC promoter, a site that is transactivated by FBP1. This investigation therefore places menin in a pathway that regulates MYC gene expression and has important implications for the biological function of menin.