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Science 24 October 2003:
Vol. 302. no. 5645, pp. 636 - 639
DOI: 10.1126/science.1088877
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Reports

BRCT Repeats As Phosphopeptide-Binding Modules Involved in Protein Targeting

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

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.


* These authors contributed equallyto this work.

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

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