Geriatric Psychiatry

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Interplay between ribosomal protein S27a and MDM2 protein in p53 activation in response to ribosomal stress

Xiao-Xin Sun; Tiffany DeVine; Kishore B. Challagundla; Mu-Shui Dai (Profiled Author: Mushui Dai)

Journal of Biological Chemistry. 2011;286(26):22730-22741.

Ribosomal proteins play a critical role in tightly coordinating p53 signaling with ribosomal biogenesis. Several ribosomal proteins have been shown to induce and activate p53 via inhibition of MDM2. Here, we report that S27a, a small subunit ribosomal protein synthesized as an 80-amino acid ubiquitin C-terminal extension protein (CEP80), functions as a novel regulator of the MDM2-p53 loop. S27a interacts with MDM2 at the central acidic domain of MDM2 and suppresses MDM2-mediated p53 ubiquitination, leading to p53 activation and cell cycle arrest. Knockdown of S27a significantly attenuates the p53 activation in cells in response to treatment with ribosomal stress-inducing agent actinomycin D or 5-fluorouracil. Interestingly, MDM2 in turn ubiquitinates S27a and promotes proteasomal degradation of S27a in response to actinomycin D treatment, thus forming a mutual-regulatory loop. Altogether, our results reveal that S27a plays a non-redundant role in mediating p53 activation in response to ribosomal stress via interplaying with MDM2. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.

PMID: 21561866     PMCID: PMC3123040

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