Dissection of the role of a Src homology 3 domain in the evolution of binding preference of paralogous proteins.

ABSTRACT: Protein-protein interactions (PPIs) drive many cellular processes. Some interactions are directed by Src homology 3 (SH3) domains that bind proline-rich motifs on other proteins. The evolution of the binding specificity of SH3 domains is not completely understood, particularly following gene duplication. Paralogous genes accumulate mutations that can modify protein functions and, for SH3 domains, their binding preferences. Here, we examined how the binding of the SH3 domains of 2 paralogous yeast type I myosins, Myo3 and Myo5, evolved following duplication. We found that the paralogs have subtly different SH3-dependent interaction profiles. However, by swapping SH3 domains between the paralogs and characterizing the SH3 domains freed from their protein context, we find that very few of the

SUBMITTER: Lemieux P 

PROVIDER: S-EPMC10763533 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature