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First published online 21 February 2007
doi: 10.1242/dev.02833
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Skirball Institute of Biomolecular Medicine and NYU School of Medicine, 540 First Avenue, New York, NY 10016, USA.
Author for correspondence (e-mail:
nance{at}saturn.med.nyu.edu)
Accepted 12 January 2007
Epithelial cells perform important roles in the formation and function of organs and the genesis of many solid tumors. A distinguishing feature of epithelial cells is their apicobasal polarity and the presence of apical junctions that link cells together. The interacting proteins Par-6 (a PDZ and CRIB domain protein) and aPKC (an atypical protein kinase C) localize apically in fly and mammalian epithelial cells and are important for apicobasal polarity and junction formation. Caenorhabditis elegans PAR-6 and PKC-3/aPKC also localize apically in epithelial cells, but a role for these proteins in polarizing epithelial cells or forming junctions has not been described. Here, we use a targeted protein degradation strategy to remove both maternal and zygotic PAR-6 from C. elegans embryos before epithelial cells are born. We find that PKC-3 does not localize asymmetrically in epithelial cells lacking PAR-6, apical junctions are fragmented, and epithelial cells lose adhesion with one another. Surprisingly, junction proteins still localize apically, indicating that PAR-6 and asymmetric PKC-3 are not needed for epithelial cells to polarize. Thus, whereas the role of PAR-6 in junction formation appears to be widely conserved, PAR-6-independent mechanisms can be used to polarize epithelial cells.
Key words: Polarity, Organogenesis, Epithelium, Cell junctions, PAR-6, C. elegans
This article has been cited by other articles:
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D. C. Anderson, J. S. Gill, R. M. Cinalli, and J. Nance Polarization of the C. elegans Embryo by RhoGAP-Mediated Exclusion of PAR-6 from Cell Contacts Science, June 27, 2008; 320(5884): 1771 - 1774. [Abstract] [Full Text] [PDF] |
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