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Submitted on September 21, 2005
Revised on November 21, 2005
Accepted on November 30, 2005

Construction and application of a yeast surface-displayed human cDNA library to identify post-translational modification-dependent protein-protein interactions

Scott Bidlingmaier and Bin Liu

Department of Anesthesia, UCSF, San Francisco, CA 94110

Corresponding Author: liub{at}anesthesia.ucsf.edu

Although post-translational modifications such as phosphorylation mediate fundamental biological processes within the cell, relatively few methods exist that allow proteome-wide identification of proteins that interact with these modifications. We have constructed a yeast surface-displayed human cDNA library and utilized it to identify protein fragments with affinity for phosphorylated peptides derived from the major tyrosine autophosphorylation sites of the epidermal growth factor receptor (EGFR) or focal adhesion kinase (FAK). We identified cDNAs encoding the SH2 (Src-homology 2) domains from adapter protein APS, phosphoinositide-3-kinase regulatory subunit 3 (PIK3R3), SH2B, and tensin, demonstrating the effectiveness of this approach. Our results suggest that large libraries of functional human protein fragments can be efficiently displayed on the yeast surface. In addition to the analysis of post-translational modifications, yeast surface-displayed human cDNA libraries have many potential applications, including identifying targets and defining potential cross-reactive proteins for small molecules or drugs.


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