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

FEBS Lett. 2004 Nov 5;577(1-2):289-93. doi: 10.1016/j.febslet.2004.10.026.


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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Ataxia Telangiectasia Mutated Proteins
  • Blotting, Western
  • Cell Cycle Proteins / chemistry
  • Cell Cycle Proteins / physiology*
  • Cell Nucleus / metabolism*
  • DNA Damage*
  • DNA-Binding Proteins
  • Exodeoxyribonucleases / chemistry
  • Exodeoxyribonucleases / physiology*
  • Fluorescent Antibody Technique
  • HeLa Cells
  • Humans
  • Phosphoproteins / chemistry
  • Phosphoproteins / physiology*
  • Plasmids
  • Protein Serine-Threonine Kinases / chemistry
  • Protein Serine-Threonine Kinases / physiology*
  • Protein Transport
  • RNA, Small Interfering


  • ATRIP protein, human
  • Adaptor Proteins, Signal Transducing
  • Cell Cycle Proteins
  • DNA-Binding Proteins
  • Phosphoproteins
  • RNA, Small Interfering
  • ATR protein, human
  • Ataxia Telangiectasia Mutated Proteins
  • Protein Serine-Threonine Kinases
  • Exodeoxyribonucleases
  • three prime repair exonuclease 1