Our studies of Rvs167 and Abp1 (see cell polarity and other sections), have interested us in a broader analysis of SH3 domain function. Rvs167 contains a C-terminal SH3 domain; we and others have identified a number of ligands that bind the Rvs167 SH3 domain. Our in vitro and in vivo studies suggest that ligand binding to the Rvs167 SH3 domain is regulated by Cdk-dependent phosphorylation adjacent to the SH3 domain. We have embarked on a collaborative study with Dr. Alan Davidson (website: http://lambda.med.utoronto.ca/Davidson/ModelSystem.html) to thoroughly explore the function and regulation of both the Rvs167 and Abp1 SH3 domains. Both Rvs167 and Abp1 have biologically important homologues in mammalian cells and the SH3 domains of these yeast proteins are completely amenable to biophysical and genetic analysis. Our analysis will include an exploration of the effects of alterations in the thermodynamic stability of SH3 domains on in vivo function, and a concerted effort to identify determinants of SH3 domain specificity using genetic, biochemical and structural approaches.

From the site: About SH3 domains, by Fariba Fana