PIP2-PDZ Domain Binding Controls the Association of Syntenin with the Plasma Membrane
| Autor: | Jan Gettemans, J. Victor Small, Pascale Zimmermann, Guido David, Iris Leenaerts, Gunter Reekmans, Joël Vandekerckhove, Kris Meerschaert |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
Phosphatidylinositol 4
5-Diphosphate Syntenins Recombinant Fusion Proteins PDZ domain Plasma protein binding Biology Cell Line Cell membrane Protein structure medicine Animals Binding site Molecular Biology Micelles Calcium-Calmodulin-Dependent Protein Kinases Nucleoside-phosphate kinase Cell Membrane Intracellular Signaling Peptides and Proteins Membrane Proteins Proteins Cell Biology Immunohistochemistry Cell biology Protein Structure Tertiary medicine.anatomical_structure Biochemistry Membrane protein lipids (amino acids peptides and proteins) sense organs Protein Tyrosine Phosphatases Carrier Proteins Nucleoside-Phosphate Kinase Guanylate Kinases Protein Binding |
| Zdroj: | Molecular Cell. 9(6):1215-1225 |
| ISSN: | 1097-2765 |
| DOI: | 10.1016/s1097-2765(02)00549-x |
| Popis: | PDZ proteins organize multiprotein signaling complexes. According to current views, PDZ domains engage in protein-protein interactions. Here we show that the PDZ domains of several proteins bind phosphatidylinositol 4,5-bisphosphate (PIP(2)). High-affinity binding of syntenin to PIP(2)-containing lipid layers requires both PDZ domains of this protein. Competition and mutagenesis experiments reveal that the protein and the PIP(2) binding sites in the PDZ domains overlap. Overlay assays indicate that the two PDZ domains of syntenin cooperate in binding to cognate peptides and PIP(2). Experiments on living cells demonstrate PIP(2)-dependent and peptide-dependent modes of plasma membrane association of the PDZ domains of syntenin. These observations suggest that local changes in phosphoinositide concentration control the association of PDZ proteins with their target receptors at the plasma membrane. |
| Databáze: | OpenAIRE |
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