Reference: Durocher D, et al. (1999) The FHA domain is a modular phosphopeptide recognition motif. Mol Cell 4(3):387-94

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Abstract

FHA domains are conserved sequences of 65-100 amino acid residues found principally within eukaryotic nuclear proteins, but which also exist in certain prokaryotes. The FHA domain is thought to mediate protein-protein interactions, but its mode of action has yet to be elucidated. Here, we show that the two highly divergent FHA domains of Saccharomyces cerevisiae Rad53p, a protein kinase involved in cell cycle checkpoint control, possess phosphopeptide-binding specificity. We also demonstrate that other FHA domains bind peptides in a phospho-dependent manner. These findings indicate that the FHA domain is a phospho-specific protein-protein interaction motif and have important implications for mechanisms of intracellular signaling in both eukaryotes and prokaryotes.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Durocher D, Henckel J, Fersht AR, Jackson SP
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