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Published online December 10, 2007
doi:10.1083/jcb.200709111
The Journal of Cell Biology, Vol. 179, No. 6, 1133-1140
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Sfakianos et al.
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Report

 Par3 functions in the biogenesis of the primary cilium in polarized epithelial cells

Jeff Sfakianos1,3, Akashi Togawa2, Sandra Maday1, Mike Hull1, Marc Pypaert1, Lloyd Cantley2, Derek Toomre1, and Ira Mellman1,3

1 Department of Cell Biology, Ludwig Institute for Cancer Research, and 2 Section of Nephrology, Yale University School of Medicine, New Haven, CT 06520
3 Genentech, Inc., South San Francisco, CA 94080

Correspondence to Ira Mellman: mellman.ira{at}gene.com

Par3 is a PDZ protein important for the formation of junctional complexes in epithelial cells. We have identified an additional role for Par3 in membrane biogenesis. Although Par3 was not required for maintaining polarized apical or basolateral membrane domains, at the apical surface, Par3 was absolutely essential for the growth and elongation of the primary cilium. The activity reflected its ability to interact with kinesin-2, the microtubule motor responsible for anterograde transport of intraflagellar transport particles to the tip of the growing cilium. The Par3 binding partners Par6 and atypical protein kinase C interacted with the ciliary membrane component Crumbs3 and we show that the PDZ binding motif of Crumbs3 was necessary for its targeting to the ciliary membrane. Thus, the Par complex likely serves as an adaptor that couples the vectorial movement of at least a subset of membrane proteins to microtubule-dependent transport during ciliogenesis.

Abbreviations used in this paper: aPKC, atypical PKC; Crumbs3, Crb3a; IFT, intraflagellar transport; shRNA, short hairpin RNA.


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For long, lush cilia, try Par3
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J. Cell Biol. 2007 179: 1085. [Full Text] [PDF]



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