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Extensions of PSD-95/discs large/ZO-1 (PDZ) domains influence lipid binding and membrane targeting of syntenin-1
KU Leuven. (Ivarsson)
2012 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 586, no 10, 1445-1451 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2012. Vol. 586, no 10, 1445-1451 p.
National Category
Natural Sciences
URN: urn:nbn:se:uu:diva-203341DOI: 10.1016/j.febslet.2012.04.024PubMedID: 22673509OAI: oai:DiVA.org:uu-203341DiVA: diva2:636289
Available from: 2013-07-09 Created: 2013-07-09 Last updated: 2013-07-18Bibliographically approved

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