Intracellular polarity protein PAR-1 regulates extracellular laminin assembly by regulating the dystroglycan complex

Maki Masuda-Hirata, Atsushi Suzuki, Yoshiko Amano, Kazunari Yamashita, Mariko Ide, Tomoyuki Yamanaka, Michihiro Sakai, Michihiro Imamura, Shigeo Ohno

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)835-850
Number of pages16
JournalGenes to Cells
Volume14
Issue number7
DOIs
Publication statusPublished - 2009 Jul 6
Externally publishedYes

ASJC Scopus subject areas

  • Genetics
  • Cell Biology

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