As many as half of familial breast cancers can be attributed to germline defects in the notorious breast cancer-associated gene 1 (BRCA1). These defects generally affect the gene product's carboxyl-terminal domain, known as BRCT, a ~100 amino-acid tandem repeat that's found alone or in multiples in a large number of proteins involved in DNA repair and checkpoint control. Yet despite such obvious links with cancer, the exact function of the BRCT domain has remained elusive.
This issue's Hot Papers revealed the BRCT domain's affinity for phosphorylated peptides associated with cell-cycle checkpoints. Michael Yaffe, a biochemist and surgeon at Massachusetts Institute of Technology, and colleagues used a proteomic screening approach to characterize BRCT domain function, stemming from their interest in protein kinases and signaling networks in general.1 In an accompanying paper, Junjie Chen and colleagues at the Mayo Clinic and Foundation took a more tailored approach, focusing specifically on the interaction ...
