Journal
CELL STRUCTURE AND FUNCTION
Volume 36, Issue 1, Pages 97-102Publisher
JAPAN SOC CELL BIOLOGY
DOI: 10.1247/csf.11005
Keywords
membrane binding protein; phosphoinositides; cell polarity; par-3
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Funding
- Ministry of Education, Culture, Sports, Science and Technology of Japan
- Japan Science and Technology Corporation (JST)
- Uehara Memorial Foundation
- Mochida Memorial Foundation for Medical and Pharmaceutical Research
- Inamori Foundation
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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.
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