Phosphoinositide Binding by Par-3 Involved in Par-3 Localization
| Autor: | Shigeo Ohno, Yosuke Horikoshi, Shiro Suetsugu, Sayaka Hamada |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
Physiology
Molecular Sequence Data Mutant Nerve Tissue Proteins Biology Phosphatidylinositols medicine.disease_cause Cell Line Phosphatidylinositol 3-Kinases chemistry.chemical_compound Dogs Lipid binding Cell polarity medicine Animals Humans Amino Acid Sequence Phosphatidylinositol Molecular Biology Phosphoinositide-3 Kinase Inhibitors Mutation Phosphoinositide binding Cell Biology General Medicine Fluorescence Recombinant Proteins Rats Cell biology Intercellular Junctions chemistry Liposomes Phospholipid Binding Carrier Proteins Sequence Alignment Fluorescence Recovery After Photobleaching Protein Binding |
| Zdroj: | Cell Structure and Function. 36:97-102 |
| ISSN: | 1347-3700 0386-7196 |
| DOI: | 10.1247/csf.11005 |
| Popis: | Electrostatic interactions between lipids and proteins control many cellular events. We found that phospholipids, including phosphatidylinositol 3-phosphate, phosphatidylinositol 4,5-bisphosphate, and phosphatidylinositol 3,4,5-triphosphate, bound to the C-terminal coiled-coil region of par-3 at conserved, basic residues. We identified K1013 and K1014 as the phosphoinositide binding site, because the K1013E/K1014E mutation of rat par-3 abolished its lipid binding. Importantly, the K1013E/K1014E par-3 mutant exhibited significantly weaker localization at the cell-cell junctions than the wild-type par-3. Fluorescence recovery after photo-bleaching analyses confirmed the faster turnover of mutant par-3 at cell-cell junctions. The treatment of cells with an inhibitor of phosphatidylinositol 3-kinases partially increased the turnover of par-3. These data suggested that the putative phospholipid binding by par-3 is important for its localization at cell-cell junctions. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|