The acetylase activity of p300 is dispensable for MDM2 stabilization

Shelya X. Zeng, Yetao Jin, David T. Kuninger, Peter Rotwein, Hua Lu

    Research output: Contribution to journalArticlepeer-review

    16 Scopus citations

    Abstract

    It has been shown that p300 binds to NMM2 and leads to down-regulation of the p53 function. However, it remains unclear whether the acetylase activity of p300 is necessary for regulating NMM2 stability. In this study, we address this issue. First, p300 did not acetylate NMM2 in solution and in cells. Second, overexpression of p300 in cells increased the level of the NMM2 protein but not its mRNA. Similarly, the acetylase-defective p300 AT2 mutant stabilized the NMM2 protein as well. Consistently, the deacetylase inhibitor, trichostatin A, did not significantly affect the half-life of the endogenous NMM2 protein, whereas p300 enhanced the half-life of NMM2. Finally, both wild type and acetylase-defective mutant p300 proteins associated with NMM2 in nuclear body-like structures where NMM2 might be protected from proteasomal degradation. Thus, these results suggest that p300 appears to stabilize NMM2 by retaining this protein in a specific nuclear structure rather than by acetylating it.

    Original languageEnglish (US)
    Pages (from-to)7453-7458
    Number of pages6
    JournalJournal of Biological Chemistry
    Volume278
    Issue number9
    DOIs
    StatePublished - Feb 28 2003

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Cell Biology

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