Proteomic peptide phage display uncovers novel interactions of the PDZ1-2 supramodule of syntenin
Research output: Contribution to journal › Article › peer-review
Colleges, School and Institutes
- Aix Marseille University
- University of Toronto
- Terrence Donnelly Centre for Cellular and Biomolecular Research, Toronto, Ontario, Canada.
- University of Uppsala
- Department for Human Genetics, Faculty of Medicine, Catholic University of Leuven, Belgium
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.
|Number of pages||10|
|Early online date||8 Jan 2016|
|Publication status||Published - Jan 2016|
- Amino Acid Motifs, Animals, Binding Sites, COS Cells, Cell Adhesion Molecules, Cercopithecus aethiops, Computational Biology, Humans, Hydrophobic and Hydrophilic Interactions, Immobilized Proteins, Kinetics, Ligands, MCF-7 Cells, Models, Molecular, Nectins, PDZ Domains, Peptide Fragments, Peptide Library, Proteomics, Recombinant Proteins, Syntenins, Two-Hybrid System Techniques, Journal Article, Research Support, Non-U.S. Gov't, Validation Studies