SH3 Search Committee

Abstract

Src-homology 3 domains (SH3 domains) are so named for their similarity to a region in the proto-oncogene protein kinase Src. SH3 domain family members bind to protein domains characterized by paired proline residues, and so mediate protein-protein interactions in cell signaling and cytoskeleton reorganization. Tong et al. (see the Perspective by Gerstein et al.) used phage display to search peptide libraries of random sequences to identify preferred binding motifs for the various SH3 domains. They then searched the predicted proteome of Saccharomyces cerevisiae for potential binding partners, and also used a two-hybrid assay to identify proteins that interacted with the various SH3 domains when expressed in yeast. The common interactions from the networks predicted by each of these procedures were then assessed for likely biological significance. A. H. Y. Tong, B. Drees, G. Nardelli, G. D. Bader, B. Brannetti, L. Castagnoli, M. Evangelista, S. Ferracuti, B. Nelson, S. Paoluzi, M. Quondam, A. Zucconi, C. W. V. Hogue, S. Fields, C. Boone, G. Cesareni, A combined experimental and computational strategy to define protein interaction networks for peptide recognition modules. Science 295, 321-324 (2002). [Abstract] [Full Text] M. Gerstein, N. Lan, R. Jansen, Integrating interactomes. Science 295, 284-287 (2002). [Abstract] [Full Text]