hnRNP-U is a specific DNA-dependent protein kinase substrate phosphorylated in response to DNA double-strand breaks

Fredrik M. Berglund; Paul R. Clarke

doi:10.1016/j.bbrc.2009.02.019

hnRNP-U is a specific DNA-dependent protein kinase substrate phosphorylated in response to DNA double-strand breaks

Fredrik M. Berglund, Paul R. Clarke

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

31 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	59-64
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	381
Issue number	1
DOIs	https://doi.org/10.1016/j.bbrc.2009.02.019
Publication status	Published - 27 Mar 2009

Keywords

DNA-PK
hnRNP-U
SAF-A
DNA damage
Etoposide
MESSENGER-RNA
ATM
PK
CHK1
IDENTIFICATION
CHECKPOINT
ACTIVATION
INHIBITOR
RADIATION
MUTATION

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10.1016/j.bbrc.2009.02.019

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title = "hnRNP-U is a specific DNA-dependent protein kinase substrate phosphorylated in response to DNA double-strand breaks",

abstract = "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.",

keywords = "DNA-PK, hnRNP-U, SAF-A, DNA damage, Etoposide, MESSENGER-RNA, ATM, PK, CHK1, IDENTIFICATION, CHECKPOINT, ACTIVATION, INHIBITOR, RADIATION, MUTATION",

author = "Berglund, {Fredrik M.} and Clarke, {Paul R.}",

year = "2009",

month = mar,

day = "27",

doi = "10.1016/j.bbrc.2009.02.019",

language = "English",

volume = "381",

pages = "59--64",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Elsevier",

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}

TY - JOUR

T1 - hnRNP-U is a specific DNA-dependent protein kinase substrate phosphorylated in response to DNA double-strand breaks

AU - Berglund, Fredrik M.

AU - Clarke, Paul R.

PY - 2009/3/27

Y1 - 2009/3/27

N2 - 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.

AB - 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.

KW - DNA-PK

KW - hnRNP-U

KW - SAF-A

KW - DNA damage

KW - Etoposide

KW - MESSENGER-RNA

KW - ATM

KW - PK

KW - CHK1

KW - IDENTIFICATION

KW - CHECKPOINT

KW - ACTIVATION

KW - INHIBITOR

KW - RADIATION

KW - MUTATION

U2 - 10.1016/j.bbrc.2009.02.019

DO - 10.1016/j.bbrc.2009.02.019

M3 - Article

C2 - 19351595

SN - 0006-291X

VL - 381

SP - 59

EP - 64

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 1

ER -

hnRNP-U is a specific DNA-dependent protein kinase substrate phosphorylated in response to DNA double-strand breaks

Abstract

Keywords

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