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Intracellular polarity protein PAR‐1 regulates extracellular laminin assembly by regulating the dystroglycan complex
Author(s) -
MasudaHirata Maki,
Suzuki Atsushi,
Amano Yoshiko,
Yamashita Kazunari,
Ide Mariko,
Yamanaka Tomoyuki,
Sakai Michihiro,
Imamura Michihiro,
Ohno Shigeo
Publication year - 2009
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1111/j.1365-2443.2009.01315.x
Subject(s) - microbiology and biotechnology , biology , laminin , cell polarity , dystroglycan , epithelial polarity , extracellular matrix , polarity (international relations) , extracellular , morphogenesis , intracellular , basement membrane , cell , biochemistry , gene
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.