Intracellular polarity protein PAR-1 regulates extracellular laminin assembly by regulating the dystroglycan complex
Autor: | Yoshiko Amano, Tomoyuki Yamanaka, Michihiro Sakai, Kazunari Yamashita, Michihiro Imamura, Atsushi Suzuki, Maki Masuda-Hirata, Shigeo Ohno, Mariko Ide |
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Rok vydání: | 2009 |
Předmět: |
Protein Serine-Threonine Kinases
Transfection Receptors Laminin Extracellular matrix Cell membrane Dogs Laminin Cell polarity Genetics medicine Extracellular Dystroglycan Animals Dystroglycans Cells Cultured Epithelial polarity biology Cell Membrane Cell Polarity Cell Biology Extracellular Matrix Dystroglycan complex Cell biology medicine.anatomical_structure Microscopy Fluorescence biology.protein |
Zdroj: | Genes to Cells. 14:835-850 |
ISSN: | 1365-2443 1356-9597 |
DOI: | 10.1111/j.1365-2443.2009.01315.x |
Popis: | 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. |
Databáze: | OpenAIRE |
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