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Caenorhabditis elegans screen reveals role of PAR-5 in RAB-11-recycling endosome positioning and apicobasal cell polarity.

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Winter,  Julia Franziska
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Korn,  Kerstin
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Farnung,  Benjamin
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Bradshaw,  Charles R.
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Marsico,  Giovanni
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Volkmer,  Michael
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Habermann,  Bianca
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Zerial,  Marino
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Citation

Winter, J. F., Höpfner, S., Korn, K., Farnung, B., Bradshaw, C. R., Marsico, G., et al. (2012). Caenorhabditis elegans screen reveals role of PAR-5 in RAB-11-recycling endosome positioning and apicobasal cell polarity. Nature Cell Biology, 14(7), 666-676.


Cite as: https://hdl.handle.net/21.11116/0000-0001-07E4-6
Abstract
Apically enriched Rab11-positive recycling endosomes (Rab11-REs) are important for establishing and maintaining epithelial polarity. Yet, little is known about the molecules controlling trafficking of Rab11-REs in an epithelium in vivo. Here, we report a genome-wide, image-based RNA interference screen for regulators of Rab11-RE positioning and transport of an apical membrane protein (PEPT-1) in C. elegans intestine. Among the 356 screen hits was the 14-3-3 and partitioning defective protein PAR-5, which we found to be specifically required for Rab11-RE positioning and apicobasal polarity maintenance. Depletion of PAR-5 induced abnormal clustering of Rab11-REs to ectopic sites at the basolateral cortex containing F-actin and other apical domain components. This phenotype required key regulators of F-actin dynamics and polarity, such as Rho GTPases (RHO-1 and the Rac1 orthologue CED-10) and apical PAR proteins. Our data suggest that PAR-5 acts as a regulatory hub for a polarity-maintaining network required for apicobasal asymmetry of F-actin and proper Rab11-RE positioning.