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 Lettjournal_title
FEBS lettersauthors
Garrido-Urbani S,Garg P,Ghossoub R,Arnold R,Lembo F,Sundell GN,Kim PM,Lopez M,Zimmermann P,Sidhu SS,Ivarsson Ydoi
10.1002/1873-3468.12037subject
Has Abstractpub_date
2016-01-01 00:00:00pages
3-12issue
1eissn
0014-5793issn
1873-3468journal_volume
590pub_type
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