Published online January 14, 2008
doi:10.1083/jcb.200707007
The Journal of Cell Biology, Vol. 180, No. 1, 31-38
The Rockefeller University Press, 0021-9525 $30.00
© 2008 Li et al.
Dynein-mediated apical localization of crumbs transcripts is required for Crumbs activity in epithelial polarity
Zhouhua Li1,
Liwei Wang1,
Thomas S. Hays3, and
Yu Cai1,2
1 Temasek Lifesciences Laboratory and 2 Department of Biological Science, National University of Singapore, Singapore 117604
3 Department of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, MN 55455
Correspondence to Y. Cai: caiyu{at}tll.org.sg
Asymmetrical localization of transcripts coupled with localized translation constitutes an important mechanism widely deployed to regulate gene activity in a spatial manner. The conserved transmembrane protein Crumbs (Crb) is an important regulator of epithelial polarity. However, it remains unclear how Crb is targeted to the apical domain. Here, we show that the cytoplasmic dynein complex transports both Crb protein and transcripts to the apical domain of Drosophila melanogaster follicular cells (FCs). The crb 3' untranslated region (UTR) is necessary and sufficient for the apical localization of its transcript and this apical transcript localization is crucial for crb function. In crb mutant FCs, Crb protein derived from transgenes lacking the 3' UTR does not effectively localize to the apical domain and does not effectively restore normal epithelial polarity. We propose that dynein-mediated messenger RNA transport coupled with a localized translation mechanism is involved in localizing Crb to the apical domain to mediate epithelial apicobasal polarity and that this mechanism might be widely used to regulate cellular polarity.
Abbreviations used in this paper: A/B, apicobasal; Co-IP, coimmunoprecipitation; Crb, Crumbs; Dhc64C, Drosophila melanogaster dynein heavy chain 64C; EMS, ethyl methanesulfonate; FC, follicle cell; MT, microtubule; Sdt, Stardust; UTR, untranslated region; wt, wild type.

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