Jan 2016 FEBS letters

Proteomic peptide phage display uncovers novel interactions of the PDZ1-2 supramodule of syntenin.

Auteurs

Garrido-Urbani S, Garg P, Ghossoub R, Arnold R, Lembo F, Sundell GN, Kim PM, Lopez M, Zimmermann P, Sidhu SS, Ivarsson Y

Résumé

Syntenin has crucial roles in cell adhesion, cell migration and synaptic transmission. Its closely linked postsynaptic density-95, discs large 1, zonula occludens-1 (PDZ) domains typically interact with C-terminal ligands. We profile syntenin PDZ1-2 through proteomic peptide phage display (ProP-PD) using a library that displays C-terminal regions of the human proteome. The protein recognizes a broad range of peptides, with a preference for hydrophobic motifs and has a tendency to recognize cryptic internal ligands. We validate the interaction with nectin-1 through orthogonal assays. The study demonstrates the power of ProP-PD as a complementary approach to uncover interactions of potential biological relevance.

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