PMID: 22371556 RLIMS-P 2 eFIP 0 miRTex 0 eGARD 0 Issue Report
Title
| 1. | aPKC phosphorylates JAM-A at Ser285 to promote cell contact maturation and tight junction formation. |
Abstract
| 2. | The PAR-3-atypical protein kinase C (aPKC)-PAR-6 complex has been implicated in the development of apicobasal polarity and the formation of tight junctions (TJs) in vertebrate epithelial cells. |
| 3. | It is recruited by junctional adhesion molecule A (JAM-A) to primordial junctions where aPKC is activated by Rho family small guanosine triphosphatases. |
| 4. | In this paper, we show that aPKC can interact directly with JAM-A in a PAR-3-independent manner. |
| 5. | Upon recruitment to primordial junctions, aPKC phosphorylates JAM-A at S285 to promote the maturation of immature cell-cell contacts. |
| 6. | In fully polarized cells, S285-phosphorylated JAM-A is localized exclusively at the TJs, and S285 phosphorylation of JAM-A is required for the development of a functional epithelial barrier. |
| 7. | Protein phosphatase 2A dephosphorylates JAM-A at S285, suggesting that it antagonizes the activity of aPKC. |
| 8. | Expression of nonphosphorylatable JAM-A/S285A interferes with single lumen specification during cyst development in three-dimensional culture. |
| 9. | Our data suggest that aPKC phosphorylates JAM-A at S285 to regulate cell-cell contact maturation, TJ formation, and single lumen specification. |
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