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Proteomic peptide phage display uncovers novel interactions of the PDZ1-2 supramodule of syntenin
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2016 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 590, no 1, 3-12 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2016. Vol. 590, no 1, 3-12 p.
National Category
Biochemistry and Molecular Biology
Research subject
URN: urn:nbn:se:uu:diva-275039DOI: 10.1002/1873-3468.12037ISI: 000368808900001PubMedID: 26787460OAI: oai:DiVA.org:uu-275039DiVA: diva2:898513
Åke Wiberg Foundation, 3773397Swedish Research Council, C0509201
Available from: 2016-01-28 Created: 2016-01-28 Last updated: 2016-03-08Bibliographically approved

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Sundell, Gustav NIvarsson, Ylva
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