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Published online 13 June 2005. doi:10.1083/jcb.200411053
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 169, Number 6, 953-963
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Article

The exocyst component Sec5 is present on endocytic vesicles in the oocyte of Drosophila melanogaster



Bernhard Sommer1, Adrian Oprins2,3, Catherine Rabouille2,3, and Sean Munro1

1 Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 2QH, England, UK
2 Department of Cell Biology, University Medical Centre Utrecht, 3584 CX Utrecht, Netherlands
3 Institute of Biomembranes, University Medical Centre Utrecht, 3584 CX Utrecht, Netherlands

Correspondence to S. Munro: sean{at}mrc-lmb.cam.ac.uk; or C. Rabouille: C.Rabouille{at}lab.azu.nl

The exocyst is an octameric complex required for polarized secretion. Some components of the exocyst are found on the plasma membrane, whereas others are recruited to Golgi membranes, suggesting that exocyst assembly tethers vesicles to their site of fusion. We have found that in Drosophila melanogaster oocytes the majority of the exocyst component Sec5 is unexpectedly present in clathrin-coated pits and vesicles at the plasma membrane. In oocytes, the major substrate for clathrin-dependent endocytosis is the vitellogenin receptor Yolkless. A truncation mutant of Sec5 (sec5E13) allows the formation of normally sized oocytes but with greatly reduced yolk uptake. We find that in sec5E13 oocytes Yolkless accumulates aberrantly in late endocytic compartments, indicating a defect in the endocytic cycling of the receptor. An analogous truncation of the yeast SEC5 gene results in normal secretion but a temperature-sensitive defect in endocytic recycling. Thus, the exocyst may act in both Golgi to plasma membrane traffic and endocytic cycling, and hence in oocytes is recruited to clathrin-coated pits to facilitate the rapid recycling of Yolkless.


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