Abstract
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.
Original language | English |
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Pages (from-to) | 3-12 |
Number of pages | 10 |
Journal | FEBS Letters |
Volume | 590 |
Issue number | 1 |
Early online date | 8 Jan 2016 |
DOIs | |
Publication status | Published - Jan 2016 |
Keywords
- 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