Proteomic peptide phage display uncovers novel interactions of the PDZ1-2 supramodule of syntenin.

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Garrido-Urbani S,Garg P,Ghossoub R,Arnold R,Lembo F,Sundell GN,Kim PM,Lopez M,Zimmermann P,Sidhu SS,Ivarsson Y

doi

10.1002/1873-3468.12037

subject

Has Abstract

pub_date

2016-01-01 00:00:00

pages

3-12

issue

1

eissn

0014-5793

issn

1873-3468

journal_volume

590

pub_type

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