HnRNP Q regulates translation of p53 in normal and stress conditions

D. Y. Kim; W. Kim; K. H. Lee; S. H. Kim; H. R. Lee; H. J. Kim; Y. Jung; J. H. Choi; K. T. Kim

doi:10.1038/cdd.2012.109

HnRNP Q regulates translation of p53 in normal and stress conditions

D. Y. Kim, W. Kim, K. H. Lee, S. H. Kim, H. R. Lee, H. J. Kim, Y. Jung, J. H. Choi, K. T. Kim

Department of Dentistry

Pohang University of Science and Technology

Research output: Contribution to journal › Article › peer-review

50 Scopus citations

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.

Original language	English
Pages (from-to)	226-234
Number of pages	9
Journal	Cell Death and Differentiation
Volume	20
Issue number	2
DOIs	https://doi.org/10.1038/cdd.2012.109
State	Published - Feb 2013

Keywords

IRES
hnRNP Q
p53
translation

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10.1038/cdd.2012.109

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title = "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.",

keywords = "IRES, hnRNP Q, p53, translation",

author = "Kim, {D. Y.} and W. Kim and Lee, {K. H.} and Kim, {S. H.} and Lee, {H. R.} and Kim, {H. J.} and Y. Jung and Choi, {J. H.} and Kim, {K. T.}",

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doi = "10.1038/cdd.2012.109",

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T1 - HnRNP Q regulates translation of p53 in normal and stress conditions

AU - Kim, D. Y.

AU - Kim, W.

AU - Lee, K. H.

AU - Kim, S. H.

AU - Lee, H. R.

AU - Kim, H. J.

AU - Jung, Y.

AU - Choi, J. H.

AU - Kim, K. T.

PY - 2013/2

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N2 - 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.

AB - 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.

KW - IRES

KW - hnRNP Q

KW - p53

KW - translation

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DO - 10.1038/cdd.2012.109

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SN - 1350-9047

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JO - Cell Death and Differentiation

JF - Cell Death and Differentiation

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HnRNP Q regulates translation of p53 in normal and stress conditions

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