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Amino‐terminal domain of ATRIP contributes to intranuclear relocation of the ATR–ATRIP complex following DNA damage
Author(s) -
Itakura Eisuke,
Takai Kaori Kajihara,
Umeda Kazuyuki,
Kimura Makoto,
Ohsumi Mariko,
Tamai Katsuyuki,
Matsuura Akira
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.10.026
Subject(s) - dna damage , microbiology and biotechnology , nuclear export signal , dna pkcs , replication protein a , chemistry , cancer research , dna , biology , cell nucleus , biochemistry , dna binding protein , cytoplasm , gene , transcription factor
ATM and rad3‐related protein kinase (ATR), a member of the phosphoinositide kinase‐like protein kinase family, plays a critical role in cellular responses to DNA structural abnormalities in conjunction with its interacting protein, ATRIP. Here, we show that the amino‐terminal portion of ATRIP is relocalized to DNA damage‐induced nuclear foci in an RPA‐dependent manner, despite its lack of ability to associate with ATR. In addition, ATR‐free ATRIP protein can be recruited to the nuclear foci. Our results suggest that the N‐terminal domain of the ATRIP protein contributes to the cell cycle checkpoint by regulating the intranuclear localization of ATR.