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.
Keywords:
PDZ domain; peptide interaction; phage display; protein-protein interaction; short linear motif.
© 2015 Federation of European Biochemical Societies.
Publication types
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Research Support, Non-U.S. Gov't
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Validation Study
MeSH terms
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Amino Acid Motifs
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Animals
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Binding Sites
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COS Cells
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Cell Adhesion Molecules / chemistry
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Cell Adhesion Molecules / genetics
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Cell Adhesion Molecules / metabolism
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Chlorocebus aethiops
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Computational Biology
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Humans
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Hydrophobic and Hydrophilic Interactions
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Immobilized Proteins / chemistry
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Immobilized Proteins / genetics
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Immobilized Proteins / metabolism
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Kinetics
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Ligands
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MCF-7 Cells
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Models, Molecular*
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Nectins
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PDZ Domains
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Peptide Fragments / chemistry
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Peptide Fragments / classification
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Peptide Fragments / metabolism
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Peptide Library
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Proteomics / methods
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Recombinant Proteins / chemistry
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Recombinant Proteins / classification
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Recombinant Proteins / metabolism
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Syntenins / chemistry
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Syntenins / genetics
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Syntenins / metabolism*
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Two-Hybrid System Techniques
Substances
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Cell Adhesion Molecules
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Immobilized Proteins
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Ligands
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NECTIN1 protein, human
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Nectins
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Peptide Fragments
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Peptide Library
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Recombinant Proteins
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SDCBP protein, human
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Syntenins