共 29 条
hnRNP-U is a specific DNA-dependent protein kinase substrate phosphorylated in response to DNA double-strand breaks
被引:30
作者:

Berglund, Fredfk M.
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机构:
Univ Dundee, Biomed Res Inst, Coll Med Dent & Nursing, Ninewells Hosp & Med Sch, Dundee DD1 9SY, Scotland Univ Dundee, Biomed Res Inst, Coll Med Dent & Nursing, Ninewells Hosp & Med Sch, Dundee DD1 9SY, Scotland

Clarke, Paul R.
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机构:
Univ Dundee, Biomed Res Inst, Coll Med Dent & Nursing, Ninewells Hosp & Med Sch, Dundee DD1 9SY, Scotland Univ Dundee, Biomed Res Inst, Coll Med Dent & Nursing, Ninewells Hosp & Med Sch, Dundee DD1 9SY, Scotland
机构:
[1] Univ Dundee, Biomed Res Inst, Coll Med Dent & Nursing, Ninewells Hosp & Med Sch, Dundee DD1 9SY, Scotland
关键词:
DNA-PK;
hnRNP-U;
SAF-A;
DNA damage;
Etoposide;
MESSENGER-RNA;
ATM;
PK;
CHK1;
IDENTIFICATION;
CHECKPOINT;
ACTIVATION;
INHIBITOR;
RADIATION;
MUTATION;
D O I:
10.1016/j.bbrc.2009.02.019
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
Cellular responses to DNA damage are orchestrated by the large phosphoinositol-3-kinase related kinases ATM, ATR and DNA-PK. We have developed a cell-free system to dissect the biochemical mechanisms of these kinases. Using this system, we identify heterogeneous nuclear ribonucleoprotein U (hnRNP-U), also termed scaffold attachment factor A (SAF-A), as a specific substrate for DNA-PK. We show that hnRNP-U is phosphorylated at Ser59 by DNA-PK in vitro and in cells in response to DNA double-strand breaks. Phosphorylation of hnRNP-U suggests novel functions for DNA-PK in the response to DNA damage. (C) 2009 Elsevier Inc. All rights reserved.
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收藏
页码:59 / 64
页数:6
相关论文
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