2009年10月
Membrane Protein Location-Dependent Regulation by PI3K (III) and Rabenosyn-5 in Drosophila Wing Cells
PLOS ONE
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- 巻
- 4
- 号
- 10
- 開始ページ
- e7306
- 終了ページ
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1371/journal.pone.0007306
- 出版者・発行元
- PUBLIC LIBRARY SCIENCE
The class III phosphatidylinositol-3 kinase (PI3K (III)) regulates intracellular vesicular transport at multiple steps through the production of phosphatidylinositol-3-phosphate (PI(3)P). While the localization of proteins at distinct membrane domains are likely regulated in different ways, the roles of PI3K (III) and its effectors have not been extensively investigated in a polarized cell during tissue development. In this study, we examined in vivo functions of PI3K (III) and its effector candidate Rabenosyn-5 (Rbsn-5) in Drosophila wing primordial cells, which are polarized along the apical-basal axis. Knockdown of the PI3K (III) subunit Vps15 resulted in an accumulation of the apical junctional proteins DE-cadherin and Flamingo and also the basal membrane protein beta-integrin in intracellular vesicles. By contrast, knockdown of PI3K (III) increased lateral membrane-localized Fasciclin III (Fas III). Importantly, loss-of-function mutation of Rbsn-5 recapitulated the aberrant localization phenotypes of beta-integrin and Fas III, but not those of DE-cadherin and Flamingo. These results suggest that PI3K (III) differentially regulates localization of proteins at distinct membrane domains and that Rbsn-5 mediates only a part of the PI3K (III)-dependent processes.
- リンク情報
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- DOI
- https://doi.org/10.1371/journal.pone.0007306
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/19798413
- PubMed Central
- https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2749332
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000270593300011&DestApp=WOS_CPL
- ID情報
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- DOI : 10.1371/journal.pone.0007306
- ISSN : 1932-6203
- PubMed ID : 19798413
- PubMed Central 記事ID : PMC2749332
- Web of Science ID : WOS:000270593300011