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Science 302 (5645): 636-639

Copyright © 2003 by the American Association for the Advancement of Science

BRCT Repeats As Phosphopeptide-Binding Modules Involved in Protein Targeting

Isaac A. Manke, Drew M. Lowery,* Anhco Nguyen,* Michael B. Yaffe{dagger}

Abstract: We used a proteomic approach to identify phosphopeptide-binding modules mediating signal transduction events in the DNA damage response pathway. Using a library of partially degenerate phosphopeptides, we identified tandem BRCT (BRCA1 carboxyl-terminal) domains in PTIP (Pax transactivation domain-interacting protein) and in BRCA1 as phosphoserine- or phosphothreonine-specific binding modules that recognize substrates phosphorylated by the kinases ATM (ataxia telangiectasia–mutated) and ATR(ataxia telangiectasia– and RAD3-related) in response to {gamma}-irradiation. PTIP tandem BRCT domains are responsible for phosphorylation-dependent protein localization into 53BP1- and phospho-H2AX ({gamma}-H2AX)–containing nuclear foci, a marker of DNA damage. These findings provide a molecular basis for BRCT domain function in the DNA damage response and may help to explain why the BRCA1 BRCT domain mutation Met1775 -> Arg, which fails to bind phosphopeptides, predisposes women to breast and ovarian cancer.

Center for Cancer Research, Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.

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* These authors contributed equallyto this work.

{dagger} To whom correspondence should be addressed. E-mail: myaffe{at}mit.edu

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H. Keilhack, F. S. David, M. McGregor, L. C. Cantley, and B. G. Neel (2005)
J. Biol. Chem. 280, 30984-30993
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Specificity of Protein Interactions Mediated by BRCT Domains of the XRCC1 DNA Repair Protein.
P. T. Beernink, M. Hwang, M. Ramirez, M. B. Murphy, S. A. Doyle, and M. P. Thelen (2005)
J. Biol. Chem. 280, 30206-30213
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