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Menin associates with a trithorax family histone methyltransferase complex and with the Hoxc8 locus

  1. Author:
    Hughes, C. M.
    Rozenblatt-Rosen, O.
    Milne, T. A.
    Copeland, T. D.
    Levine, S. S.
    Lee, J. C.
    Hayes, D. N.
    Shanmugam, K. S.
    Bhattacharjee, A.
    Biondi, C. A.
    Kay, G. F.
    Hayward, N. K.
    Hess, J. L.
    Meyerson, M.

  2. Author Address

    Meyerson, M, Dana Farber Canc Inst, Dept Med Oncol, Boston, MA 02115 USA Dana Farber Canc Inst, Dept Med Oncol, Boston, MA 02115 USA. Harvard Univ, Sch Med, Dept Pathol, Boston, MA 02115 USA. Univ Penn, Sch Med, Dept Pathol & Lab Med, Philadelphia, PA 19104 USA. NCI, Basic Res Labs, Frederick, MD 21702 USA. Massachusetts Gen Hosp, Dept Mol Biol, Boston, MA 02115 USA. Queensland Inst Med Res, Herston, Qld 4006, Australia.
    1. Year: 2004
  2. Journal: Molecular Cell
    1. 13
    2. 4
    3. Pages: 587-597
  4. Type of Article: Article
  1. Abstract:

    The cellular function of the menin tumor suppressor protein, product of the MEN1 gene mutated in familial multiple endocrine neoplasia type 1, has not been defined. We now show that menin is associated with a histone methyltransferase complex containing two trithorax family proteins, MLL2 and Ash2L, and other homologs of the yeast Set1 assembly. This menin-associated complex methylates histone H3 on lysine 4. A subset of tumor-derived menin mutants lacks the associated histone methyltransferase activity. In addition, menin is associated with RNA polymerase II whose large subunit carboxyl-terminal domain is phosphorylated on Ser5. Men1 knockout embryos and cells show decreased expression of the homeobox genes Hoxc6 and Hoxc8. Chromatin immunoprecipitation experiments reveal that menin is bound to the Hoxc8 locus. These results suggest that menin activates the transcription of differentiation-regulating genes by covalent histone modification, and that this activity is related to tumor suppression by MEN1

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