کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2048288 | 1074075 | 2012 | 7 صفحه PDF | دانلود رایگان |
Syntenin-1 is a PDZ protein involved in receptor recycling and clustering. Its two PDZ domains interact with various receptors and phosphoinositides, and are flanked by N- and C-terminal regions. Here, we report the identification of an autoinhibitory peptide stretch in the N-terminus that might be regulated by phosphorylation. We further establish that basic residues in the C-terminal region mediate electrostatic interactions with reconstituted liposomes and contribute to the plasma membrane targeting. Our study adds new components to the multi-dentate membrane targeting mechanism and highlights the role of N- and C-terminal PDZ extensions in the regulation of syntenin-1 plasma membrane localization.Structured summary of protein interactionsPDZ1-PDZ2 and peptidebind by fluorescence technology (View Interaction: 1, 2, 3, 4).
► The subcellular distribution of syntenin-1 is regulated by its N- and C-termini.
► A phosphorylation switch may regulate the N-terminal autoinhibition.
► The PDZ tandem and the C-terminus cooperate in membrane targeting of syntenin-1.
► Electrostatic interactions contribute to syntenin-1 membrane targeting.
Journal: FEBS Letters - Volume 586, Issue 10, 21 May 2012, Pages 1445–1451