Journal
CELL DEATH AND DIFFERENTIATION
Volume 20, Issue 2, Pages 226-234Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/cdd.2012.109
Keywords
hnRNP Q; IRES; p53; translation
Categories
Funding
- National Research Foundation of Korea (NRF) [20110027957, 20110031234, 20120005830, 20110031517]
- Brain Korea 21 program
- World Class University program [R31-10105]
- Korean Ministry of Education, Science, and Technology (MEST)
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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. Cell Death and Differentiation (2013) 20, 226-234; doi:10.1038/cdd.2012.109; published online 31 August 2012
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