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Published online January 14, 2008
doi:10.1083/jcb.200704128
The Journal of Cell Biology, Vol. 180, No. 1, 145-158
The Rockefeller University Press, 0021-9525 $30.00
© 2008 Zhang et al.
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Membrane association and functional regulation of Sec3 by phospholipids and Cdc42



Xiaoyu Zhang, Kelly Orlando, Bing He, Fengong Xi, Jian Zhang, Allison Zajac, and Wei Guo

Department of Biology, University of Pennsylvania, Philadelphia, PA 19104

Correspondence to Wei Guo: guowei{at}sas.upenn.edu

The exocyst is an octameric protein complex implicated in tethering post-Golgi secretory vesicles at the plasma membrane in preparation for fusion. However, it is not clear how the exocyst is targeted to and physically associates with specific domains of the plasma membrane and how its functions are regulated at those regions. We demonstrate that the N terminus of the exocyst component Sec3 directly interacts with phosphatidylinositol 4,5-bisphosphate. In addition, we have identified key residues in Sec3 that are critical for its binding to the guanosine triphosphate–bound form of Cdc42. Genetic analyses indicate that the dual interactions of Sec3 with phospholipids and Cdc42 control its function in yeast cells. Disrupting these interactions not only blocks exocytosis and affects exocyst polarization but also leads to defects in cell morphogenesis. We propose that the interactions of Sec3 with phospholipids and Cdc42 play important roles in exocytosis and polarized cell growth.

Abbreviations used in this paper: 5-FOA, 5–fluoroorotic acid; CRIB, Cdc42/Rac interactive binding; FRAP, fluorescence recovery after photobleaching; Lat B, latrunculin B; LUV, large unilamellar vesicle; N-WASP, neural Wiskott-Aldrich syndrome protein; PC, phosphatidylcholine; PIP2, phosphatidylinositol 4,5-bisphosphate; PS, phosphatidylserine; SC, synthetic complete.


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