In:
Journal of Cell Biology, Rockefeller University Press, Vol. 196, No. 5 ( 2012-03-05), p. 623-639
Abstract:
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. It is recruited by junctional adhesion molecule A (JAM-A) to primordial junctions where aPKC is activated by Rho family small guanosine triphosphatases. In this paper, we show that aPKC can interact directly with JAM-A in a PAR-3–independent manner. Upon recruitment to primordial junctions, aPKC phosphorylates JAM-A at S285 to promote the maturation of immature cell–cell contacts. 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. Protein phosphatase 2A dephosphorylates JAM-A at S285, suggesting that it antagonizes the activity of aPKC. Expression of nonphosphorylatable JAM-A/S285A interferes with single lumen specification during cyst development in three-dimensional culture. Our data suggest that aPKC phosphorylates JAM-A at S285 to regulate cell–cell contact maturation, TJ formation, and single lumen specification.
Type of Medium:
Online Resource
ISSN:
1540-8140
,
0021-9525
DOI:
10.1083/jcb.201104143
DOI:
10.1083/jcb.201104143.dv
Language:
English
Publisher:
Rockefeller University Press
Publication Date:
2012
detail.hit.zdb_id:
1421310-2
SSG:
12
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