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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adaptor Proteins, Signal Transducing
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Ataxia Telangiectasia Mutated Proteins
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Blotting, Western
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Cell Cycle Proteins / chemistry
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Cell Cycle Proteins / physiology*
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Cell Nucleus / metabolism*
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DNA Damage*
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DNA-Binding Proteins
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Exodeoxyribonucleases / chemistry
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Exodeoxyribonucleases / physiology*
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Fluorescent Antibody Technique
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HeLa Cells
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Humans
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Phosphoproteins / chemistry
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Phosphoproteins / physiology*
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Plasmids
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Protein Serine-Threonine Kinases / chemistry
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Protein Serine-Threonine Kinases / physiology*
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Protein Transport
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RNA, Small Interfering
Substances
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ATRIP protein, human
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Adaptor Proteins, Signal Transducing
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Cell Cycle Proteins
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DNA-Binding Proteins
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Phosphoproteins
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RNA, Small Interfering
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ATR protein, human
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Ataxia Telangiectasia Mutated Proteins
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Protein Serine-Threonine Kinases
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Exodeoxyribonucleases
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three prime repair exonuclease 1