Phosphoinositide Binding by Par-3 Involved in Par-3 Localization
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- Horikoshi Yosuke
- Laboratory of Membrane and Cytoskeleton Dynamics, Institute of Molecular and Cellular Biosciences, University of Tokyo
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- Hamada Sayaka
- Laboratory of Membrane and Cytoskeleton Dynamics, Institute of Molecular and Cellular Biosciences, University of Tokyo
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- Ohno Shigeo
- Department of Molecular Biology, Yokohama City University Graduate School of Medical Science
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- Suetsugu Shiro
- Laboratory of Membrane and Cytoskeleton Dynamics, Institute of Molecular and Cellular Biosciences, University of Tokyo PRESTO, Japan Science and Technology Agency
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抄録
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.<br>
収録刊行物
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- Cell Structure and Function
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Cell Structure and Function 36 (1), 97-102, 2011
日本細胞生物学会
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詳細情報 詳細情報について
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- CRID
- 1390001204694349440
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- NII論文ID
- 130004053878
- 40019163941
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- NII書誌ID
- AA0060007X
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- ISSN
- 13473700
- 03867196
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- NDL書誌ID
- 023442829
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
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- KAKEN
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- 使用不可