Letter abstract
Nature Cell Biology 6, 427 - 435 (2004)
Published online: 11 April 2004 | doi:10.1038/ncb1122
Egalitarian binds dynein light chain to establish oocyte polarity and maintain oocyte fate
Caryn Navarro1,3, Hamsa Puthalakath2,3, Jerry M. Adams2, Andreas Strasser2 & Ruth Lehmann1
In many cell types polarized transport directs the movement of mRNAs and proteins from their site of synthesis to their site of action, thus conferring cell polarity1. The cytoplasmic dynein microtubule motor complex is involved in this process. In Drosophila melanogaster, the Egalitarian (Egl) and Bicaudal-D (BicD) proteins are also essential for the transport of macromolecules to the oocyte and to the apical surface of the blastoderm embryo2, 3, 4, 5. Hence, Egl and BicD, which have been shown to associate4, may be part of a conserved core localization machinery in Drosophila, although a direct association between these molecules and the dynein motor complex has not been shown. Here we report that Egl interacts directly with Drosophila dynein light chain (Dlc), a microtubule motor component, through an Egl domain distinct from that which binds BicD4. We propose that the Egl–BicD complex is loaded through Dlc onto the dynein motor complex thereby facilitating transport of cargo. Consistent with this model, point mutations that specifically disrupt Egl–Dlc association also disrupt microtubule-dependant trafficking both to and within the oocyte, resulting in a loss of oocyte fate maintenance and polarity. Our data provide a direct link between a molecule necessary for oocyte specification and the microtubule motor complex, and supports the hypothesis that microtubule-mediated transport is important for preserving oocyte fate.
- Developmental Genetics Program and The Department of Cell Biology, The Skirball Institute and Howard Hughes Medical Institute, NYU School of Medicine, 540 First Avenue, New York, NY 10016, USA.
- The Walter and Eliza Hall Institute of Medical Research, 1G, Royal Parade, Victoria 3050, Australia.
- These authors contributed equally to this work.
Correspondence to: Ruth Lehmann1 e-mail: lehmann@saturn.med.nyu.edu
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