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HnRNP Q regulates translation of p53 in normal and stress conditions.

ABSTRACT: The responses to numerous stress signals are important for cellular growth and survival. The p53 tumor-suppressor protein is stabilized under stress conditions and induces transcription of several genes to regulate cell cycle and apoptosis. Regarding p53 protein accumulation, inhibition of proteasomal degradation of p53 protein, which is mainly mediated by Mdm2, has received much attention. Here, we demonstrate that regulation of translation initiation is also crucial for p53 protein accumulation. Furthermore, we report that heterogeneous nuclear ribonucleoprotein (hnRNP) Q binds to the 5'-untranslated region (UTR) of mouse p53 mRNA and regulates translation efficiency of p53 and apoptosis progression. We also suggest that changes in cytosolic hnRNP Q levels contribute to cell cycle-dependent translational differences in p53 mRNA.

SUBMITTER: Kim DY

PROVIDER: S-EPMC3554343 | biostudies-literature | 2013 Feb

REPOSITORIES: biostudies-literature

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hnRNP Q regulates translation of p53 in normal and stress conditions.

Kim D-Y DY Kim W W Lee K-H KH Kim S-H SH Lee H-R HR Kim H-J HJ Jung Y Y Choi J-H JH Kim K-T KT

Cell death and differentiation 20120831 2

The responses to numerous stress signals are important for cellular growth and survival. The p53 tumor-suppressor protein is stabilized under stress conditions and induces transcription of several genes to regulate cell cycle and apoptosis. Regarding p53 protein accumulation, inhibition of proteasomal degradation of p53 protein, which is mainly mediated by Mdm2, has received much attention. Here, we demonstrate that regulation of translation initiation is also crucial for p53 protein accumulatio ...[more]

PMID: 22935615

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