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ArtikelAbraxas and RAP80 Form a BRCA1 Protein Complex Required for the DNA Damage Response  
Oleh: Bin Wang ; Matsuoka, Shuhei ; Ballif, Bryan A. ; Zhang, Dong ; Smogorzewska, Agata ; Gygi, Steven P. ; Elledge, Stephen J.
Jenis: Article from Bulletin/Magazine
Dalam koleksi: SCIENCE (keterangan: ada di Proquest) vol. 316 no. 5828 (May 2007), page 1194.
Ketersediaan
  • Perpustakaan FK
    • Nomor Panggil: S01.K.2007.05
    • Non-tandon: 1 (dapat dipinjam: 0)
    • Tandon: tidak ada
    Lihat Detail Induk
Isi artikelThe BRa repeats of the breast and ovarian cancer predisposition protein BRCAl are essential for tumor suppression. Phosphopeptide affinity proteomic analysis identified a protein, Abraxas, that directly binds the BRCAl BRa repeats through a phospho-Ser-X-X-Phe motif. Abraxas binds BRCAl to the mutual exclusion of BACHl (BRCA1-associated C-terminal helicase) and CtiP (CtBP-interacting protein), forming a third type of BRCAl complex. Abraxas recruits the ubiquitin¬interacting motif (UIM)-containing protein RAP80 to BRCA1. Both Abraxas and RAP80 were required for DNA damage resistance, G2-M checkpoint control, and DNA repair. RAP80 was required for optimal accumulation of BRCAl on damaged DNA (foci) in response to ionizing radiation, and the UIM domains alone were capable of foci formation. The RAP80-Abraxas complex may help recruit BRCAl to DNA damage sites in part through recognition of ubiquitinated proteins.
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