{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Egea-Jimenez AL"],"funding":["European Research Council"],"pagination":["12101"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5515355"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["7"],"pubmed_abstract":["PDZ domain-containing proteins work as intracellular scaffolds to control spatio-temporal aspects of cell signalling. This function is supported by the ability of their PDZ domains to bind other proteins such as receptors, but also phosphoinositide lipids important for membrane trafficking. Here we report a crystal structure of the syntenin PDZ tandem in complex with the carboxy-terminal fragment of Frizzled 7 and phosphatidylinositol 4,5-bisphosphate (PIP2). The crystal structure reveals a tripartite interaction formed via the second PDZ domain of syntenin. Biophysical and biochemical experiments establish co-operative binding of the tripartite complex and identify residues crucial for membrane PIP2-specific recognition. Experiments with cells support the importance of the syntenin-PIP2 i"],"journal":["Nature communications"],"pubmed_title":["Frizzled 7 and PIP2 binding by syntenin PDZ2 domain supports Frizzled 7 trafficking and signalling."],"pmcid":["PMC5515355"],"funding_grant_id":["647458"],"pubmed_authors":["Gallardo R","Loris R","Zimmermann P","Schymkowitz J","Wawrzyniak AM","Kashyap R","Rousseau F","Garcia-Pino A","Egea-Jimenez AL","Ivarsson Y"],"additional_accession":[]},"is_claimable":false,"name":"Frizzled 7 and PIP2 binding by syntenin PDZ2 domain supports Frizzled 7 trafficking and signalling.","description":"PDZ domain-containing proteins work as intracellular scaffolds to control spatio-temporal aspects of cell signalling. This function is supported by the ability of their PDZ domains to bind other proteins such as receptors, but also phosphoinositide lipids important for membrane trafficking. Here we report a crystal structure of the syntenin PDZ tandem in complex with the carboxy-terminal fragment of Frizzled 7 and phosphatidylinositol 4,5-bisphosphate (PIP2). The crystal structure reveals a tripartite interaction formed via the second PDZ domain of syntenin. Biophysical and biochemical experiments establish co-operative binding of the tripartite complex and identify residues crucial for membrane PIP2-specific recognition. Experiments with cells support the importance of the syntenin-PIP2 i","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Jul","modification":"2026-05-05T11:03:53.386Z","creation":"2019-03-27T02:50:47Z"},"accession":"S-EPMC5515355","cross_references":{"pubmed":["27386966"],"doi":["10.1038/ncomms12101"]}}