Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5
MS Dai, H Lu - Journal of Biological Chemistry, 2004 - ASBMB
The oncoprotein MDM2 associates with ribosomal proteins L5, L11, and L23. Both L11 and
L23 have been shown to activate p53 by inhibiting MDM2-mediated p53 suppression. Here
we have shown that L5 also activates p53. Overexpression of L5 stabilized ectopic p53 in
H1299 cells and endogenous p53 in U2OS cells. Consequently, L5 enhanced p53
transcriptional activity and induced p53-dependent G 1 cell cycle arrest. Furthermore, like
L11 and L23, L5 also remarkably inhibited MDM2-mediated p53 ubiquitination. The …
L23 have been shown to activate p53 by inhibiting MDM2-mediated p53 suppression. Here
we have shown that L5 also activates p53. Overexpression of L5 stabilized ectopic p53 in
H1299 cells and endogenous p53 in U2OS cells. Consequently, L5 enhanced p53
transcriptional activity and induced p53-dependent G 1 cell cycle arrest. Furthermore, like
L11 and L23, L5 also remarkably inhibited MDM2-mediated p53 ubiquitination. The …
