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Papers In Press, published online ahead of print February 9, 2004
J. Biol. Chem, 10.1074/jbc.M309916200
Submitted on September 8, 2003
Revised on February 7, 2004
Accepted on February 9, 2004

MDM2 mediates PCAF ubiquitination and degradation

Yetao Jin, Shelya X. Zeng, Hunjoo Lee, and Hua Lu

Biochemistry and Molecular Biology, Oregon Health Sciences University, Portland, OR 97201

Corresponding Author: LUH{at}OHSU.EDU

We recently reported that MDM2, a negative feedback regulator of the tumor suppressor p53, inhibits PCAF-mediated p53 acetylation. Our further study shows that MDM2 also regulates the stability of PCAF. MDM2 ubiquitinated PCAF in vitro and in cells. PCAF ubiquitination occurred at the N-terminus and in the nucleus, as the NLS sequence-deletion mutant of MDM2, which localized in the cytoplasm and degraded p53, was unable to degrade nuclear PCAF, and restriction of PCAF in the nucleus by leptomycin B did not affect MDM2-mediated PCAF degradation. Consistently, overexpression of MDM2 in p53 null cells caused the reduction of the protein, but not mRNA, level of PCAF. Conversely, PCAF levels were higher in MDM2-deficient MEF cells than that in MDM2-containing MEF cells. Furthermore, MDM2 reduced the half-life of PCAF by 50 %. These results demonstrate that MDM2 regulates the stability of PCAF by ubiquitinating and degrading this protein.


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