2009年7月
Intracellular polarity protein PAR-1 regulates extracellular laminin assembly by regulating the dystroglycan complex
GENES TO CELLS
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- 巻
- 14
- 号
- 7
- 開始ページ
- 835
- 終了ページ
- 850
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1111/j.1365-2443.2009.01315.x
- 出版者・発行元
- WILEY-BLACKWELL PUBLISHING, INC
Cell polarity depends on extrinsic spatial cues and intrinsic polarity proteins including PAR-aPKC proteins. In mammalian epithelial cells, cell-cell contacts provide spatial cues that activate the aPKC-PAR-3-PAR-6 complex to establish the landmark of the initial cellular asymmetry. PAR-1, a downstream target of the aPKC-PAR-3-PAR-6 complex, mediates further development of the apical and basolateral membrane domains. However, the relationships between the PAR-aPKC proteins and other extrinsic spatial cues provided by the extracellular matrix (ECM) remain unclear. Here, we show that PAR-1 colocalizes with laminin receptors and is required for the assembly of extracellular laminin on the basal surface of epithelial cells. Furthermore, PAR-1 regulates the basolateral localization of the dystroglycan (DG) complex, one of the laminin receptors essential for basement membrane formation. We also show that PAR-1 interacts with the DG complex and is required for the formation of a functional DG complex. These results reveal the presence of a novel inside-out pathway in which an intracellular polarity protein regulates the ECM organization required for epithelial cell polarity and tissue morphogenesis.
- リンク情報
- ID情報
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- DOI : 10.1111/j.1365-2443.2009.01315.x
- ISSN : 1356-9597
- PubMed ID : 19549170
- Web of Science ID : WOS:000267369000005