Aurora-A phosphorylates hnRNPK and disrupts its interaction with p53

Kai Wei Hsueh; Shu Ling Fu; Chi Ying F. Huang; Chao Hsiung Lin

doi:10.1016/j.febslet.2011.07.031

Aurora-A phosphorylates hnRNPK and disrupts its interaction with p53

Kai Wei Hsueh, Shu Ling Fu, Chi Ying F. Huang, Chao Hsiung Lin^*

^*Corresponding author for this work

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

22 Scopus citations

Abstract

Amplification of Aurora-A, encoding a cell cycle-regulating kinase, has been reported in human cancers. Although Aurora-A is known to directly phosphorylate and down-regulate p53, the detailed mechanism remains unclear. Here we show that Aurora-A phosphorylates hnRNPK, a transcriptional coactivator of p53, on serine 379. This phosphorylation does not affect the post-transcriptional activity or cellular localization of hnRNPK, but disrupts its interaction with p53. Inverse correlation between Aurora-A activity and hnRNPK-p53 interaction was further demonstrated in DNA-damaged cells. Our results provide an alternative mechanism, whereby via phosphorylating hnRNPK Aurora-A participates in regulating p53 activity during DNA damage.

Original language	English
Pages (from-to)	2671-2675
Number of pages	5
Journal	FEBS Letters
Volume	585
Issue number	17
DOIs	https://doi.org/10.1016/j.febslet.2011.07.031
State	Published - 2 Sep 2011

Keywords

Aurora-A
hnRNPK
p53 Interaction

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.febslet.2011.07.031

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@article{da00471ce21c40cb90e6747c4133b340,

title = "Aurora-A phosphorylates hnRNPK and disrupts its interaction with p53",

abstract = "Amplification of Aurora-A, encoding a cell cycle-regulating kinase, has been reported in human cancers. Although Aurora-A is known to directly phosphorylate and down-regulate p53, the detailed mechanism remains unclear. Here we show that Aurora-A phosphorylates hnRNPK, a transcriptional coactivator of p53, on serine 379. This phosphorylation does not affect the post-transcriptional activity or cellular localization of hnRNPK, but disrupts its interaction with p53. Inverse correlation between Aurora-A activity and hnRNPK-p53 interaction was further demonstrated in DNA-damaged cells. Our results provide an alternative mechanism, whereby via phosphorylating hnRNPK Aurora-A participates in regulating p53 activity during DNA damage.",

keywords = "Aurora-A, hnRNPK, p53 Interaction",

author = "Hsueh, {Kai Wei} and Fu, {Shu Ling} and Huang, {Chi Ying F.} and Lin, {Chao Hsiung}",

note = "Funding Information: We are grateful to Prof. Hirotaka J. Okano for pRL-TK-p21 3′-UTR reporter plasmid and Prof. Fung-Fang Wang for helpful suggestions in DNA damage experiment. This work was supported by grant (NSC 98-2311-B-010-003-MY3) from the National Science Council and “Grant of Aim for Top University Project” from the Ministry of Education in Taiwan.",

year = "2011",

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doi = "10.1016/j.febslet.2011.07.031",

language = "English",

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T1 - Aurora-A phosphorylates hnRNPK and disrupts its interaction with p53

AU - Hsueh, Kai Wei

AU - Fu, Shu Ling

AU - Huang, Chi Ying F.

AU - Lin, Chao Hsiung

N1 - Funding Information: We are grateful to Prof. Hirotaka J. Okano for pRL-TK-p21 3′-UTR reporter plasmid and Prof. Fung-Fang Wang for helpful suggestions in DNA damage experiment. This work was supported by grant (NSC 98-2311-B-010-003-MY3) from the National Science Council and “Grant of Aim for Top University Project” from the Ministry of Education in Taiwan.

PY - 2011/9/2

Y1 - 2011/9/2

N2 - Amplification of Aurora-A, encoding a cell cycle-regulating kinase, has been reported in human cancers. Although Aurora-A is known to directly phosphorylate and down-regulate p53, the detailed mechanism remains unclear. Here we show that Aurora-A phosphorylates hnRNPK, a transcriptional coactivator of p53, on serine 379. This phosphorylation does not affect the post-transcriptional activity or cellular localization of hnRNPK, but disrupts its interaction with p53. Inverse correlation between Aurora-A activity and hnRNPK-p53 interaction was further demonstrated in DNA-damaged cells. Our results provide an alternative mechanism, whereby via phosphorylating hnRNPK Aurora-A participates in regulating p53 activity during DNA damage.

AB - Amplification of Aurora-A, encoding a cell cycle-regulating kinase, has been reported in human cancers. Although Aurora-A is known to directly phosphorylate and down-regulate p53, the detailed mechanism remains unclear. Here we show that Aurora-A phosphorylates hnRNPK, a transcriptional coactivator of p53, on serine 379. This phosphorylation does not affect the post-transcriptional activity or cellular localization of hnRNPK, but disrupts its interaction with p53. Inverse correlation between Aurora-A activity and hnRNPK-p53 interaction was further demonstrated in DNA-damaged cells. Our results provide an alternative mechanism, whereby via phosphorylating hnRNPK Aurora-A participates in regulating p53 activity during DNA damage.

KW - Aurora-A

KW - hnRNPK

KW - p53 Interaction

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DO - 10.1016/j.febslet.2011.07.031

M3 - Article

C2 - 21821029

AN - SCOPUS:80052270230

SN - 0014-5793

VL - 585

SP - 2671

EP - 2675

JO - FEBS Letters

JF - FEBS Letters

IS - 17

ER -

Aurora-A phosphorylates hnRNPK and disrupts its interaction with p53

Abstract

Keywords

UN SDGs

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