ATRIP binding to replication protein A-single-stranded DNA promotes ATR-ATRIP localization but is dispensable for Chk1 phosphorylation

Mol Biol Cell. 2005 May;16(5):2372-81. doi: 10.1091/mbc.e04-11-1006. Epub 2005 Mar 2.

Abstract

ATR associates with the regulatory protein ATRIP that has been proposed to localize ATR to sites of DNA damage through an interaction with single-stranded DNA (ssDNA) coated with replication protein A (RPA). We tested this hypothesis and found that ATRIP is required for ATR accumulation at intranuclear foci induced by DNA damage. A domain at the N terminus of ATRIP is necessary and sufficient for interaction with RPA-ssDNA. Deletion of the ssDNA-RPA interaction domain of ATRIP greatly diminished accumulation of ATRIP into foci. However, the ATRIP-RPA-ssDNA interaction is not sufficient for ATRIP recognition of DNA damage. A splice variant of ATRIP that cannot bind to ATR revealed that ATR association is also essential for proper ATRIP localization. Furthermore, the ATRIP-RPA-ssDNA interaction is not absolutely essential for ATR activation because ATR phosphorylates Chk1 in cells expressing only a mutant of ATRIP that does not bind to RPA-ssDNA. These data suggest that binding to RPA-ssDNA is not the essential function of ATRIP in ATR-dependent checkpoint signaling and ATR has an important function in properly localizing the ATR-ATRIP complex.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Ataxia Telangiectasia Mutated Proteins
  • Base Sequence
  • Binding Sites / genetics
  • Cell Cycle Proteins / metabolism*
  • Cell Line
  • Cell Nucleus / metabolism
  • Checkpoint Kinase 1
  • DNA Damage
  • DNA, Single-Stranded / metabolism*
  • DNA-Binding Proteins / metabolism*
  • Exodeoxyribonucleases / chemistry
  • Exodeoxyribonucleases / genetics
  • Exodeoxyribonucleases / metabolism*
  • Humans
  • In Vitro Techniques
  • Phosphoproteins / chemistry
  • Phosphoproteins / genetics
  • Phosphoproteins / metabolism*
  • Phosphorylation
  • Protein Binding
  • Protein Kinases / metabolism*
  • Protein Serine-Threonine Kinases / metabolism*
  • Protein Structure, Tertiary
  • RNA, Small Interfering / genetics
  • Replication Protein A
  • Signal Transduction
  • Transfection
  • Two-Hybrid System Techniques

Substances

  • ATRIP protein, human
  • Adaptor Proteins, Signal Transducing
  • Cell Cycle Proteins
  • DNA, Single-Stranded
  • DNA-Binding Proteins
  • Phosphoproteins
  • RNA, Small Interfering
  • RPA1 protein, human
  • Replication Protein A
  • Protein Kinases
  • ATR protein, human
  • Ataxia Telangiectasia Mutated Proteins
  • CHEK1 protein, human
  • Checkpoint Kinase 1
  • Protein Serine-Threonine Kinases
  • Exodeoxyribonucleases
  • three prime repair exonuclease 1