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FEBS Lett. 2004 Nov 5;577(1-2):289-93.

Amino-terminal domain of ATRIP contributes to intranuclear relocation of the ATR-ATRIP complex following DNA damage.

Author information

1
Department of Geriatric Research, National Institute for Longevity Sciences, Obu, Aichi 474-8522, Japan.

Abstract

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.

PMID:
15527801
DOI:
10.1016/j.febslet.2004.10.026
[Indexed for MEDLINE]
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