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

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

48 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 (US)
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
Externally published	Yes

Keywords

IRES
hnRNP Q
p53
translation

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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10.1038/cdd.2012.109

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@article{560e37bb9334421f8b21ae448b469869,

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.}",

note = "Funding Information: Acknowledgements. This work was supported by grants from the National Research Foundation of Korea (NRF) (Nos. 20110027957, 20110031234, 20120005830, and 20110031517), the Brain Korea 21 program, and the World Class University program (R31-10105) funded by the Korean Ministry of Education, Science, and Technology (MEST).",

year = "2013",

month = feb,

doi = "10.1038/cdd.2012.109",

language = "English (US)",

volume = "20",

pages = "226--234",

journal = "Cell death and differentiation",

issn = "1350-9047",

publisher = "Nature Publishing Group",

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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.

N1 - Funding Information: Acknowledgements. This work was supported by grants from the National Research Foundation of Korea (NRF) (Nos. 20110027957, 20110031234, 20120005830, and 20110031517), the Brain Korea 21 program, and the World Class University program (R31-10105) funded by the Korean Ministry of Education, Science, and Technology (MEST).

PY - 2013/2

Y1 - 2013/2

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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JO - Cell death and differentiation

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ER -

HnRNP Q regulates translation of p53 in normal and stress conditions

Abstract

Keywords

ASJC Scopus subject areas

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