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^*

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21 引文斯高帕斯（Scopus）

摘要

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.

原文	English
頁（從 - 到）	2671-2675
頁數	5
期刊	FEBS Letters
卷	585
發行號	17
DOIs	https://doi.org/10.1016/j.febslet.2011.07.031
出版狀態	Published - 2 9月 2011

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10.1016/j.febslet.2011.07.031

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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.",

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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

UR - http://www.scopus.com/inward/record.url?scp=80052270230&partnerID=8YFLogxK

U2 - 10.1016/j.febslet.2011.07.031

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

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