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A mismatched role for Bcl-2

Bcl-2 has previously been characterized as an anti-apoptotic protein. However, it has now been linked to DNA mismatch repair (MMR). By retaining E2F-1 in a transcriptionally inactive state, through the induction of hypophosphorylated retinoblastoma protein, Bcl-2 hinders the expression of a key component of mismatch repair, MSH2. This study could therefore help to explain the mutagenicity that is associated with Bcl-2.

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References

  1. 1

    Youn, C.-K. et al. Nature Cell Biol. 7, 137–147 (2005).

  2. 2

    Reed, J. C. Oncogene 17, 3225–3236 (1998).

  3. 3

    Cory, S. & Adams, J. M. Nature Rev. Cancer 2, 647–656 (2002).

  4. 4

    Hsieh, P. Mutat. Res. 486, 71–87 (2001).

  5. 5

    Papadopoulos, H. & Lindblom, A. Hum. Mutat. 10, 89–99 (1997).

  6. 6

    de Wind, N. et al. Cell 82, 321–330 (1995).

  7. 7

    Stevens, C. & La Thangue, N. B. Arch. Biochem. Biophys. 412, 157–169 (2003).

  8. 8

    Stevaux, O. & Dyson, N. Curr. Opin. Cell Biol. 14, 684–691 (2002).

  9. 9

    Huang, D. C., O'Reilly, L. A., Strasser, A. & Cory, S. EMBO J. 16, 4628–4638 (1997).

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Figure 1: Regulation of MMR activity by Bcl-2.