期刊
FEBS LETTERS
卷 590, 期 1, 页码 3-12出版社
WILEY
DOI: 10.1002/1873-3468.12037
关键词
PDZ domain; peptide interaction; phage display; protein-protein interaction; short linear motif
资金
- Swedish Research Council [C0509201]
- Ake Wiberg foundation [3773397]
- Fund for Scientific Research - Flanders (FWO) [G.0479.12]
- Concerted Actions Program of KU Leuven [GOA/12/016]
- Canadian Institutes for Health Research [MOP-93684]
- INSERM
- ARC French Foundation for Cancer Research
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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