REFERENCES
- Adamo, J. E., J. J. Moskow, A. S. Gladfelter, D. Viterbo, D. J. Lew, and P. J. Brennwald. 2001. Yeast Cdc42 functions at a late step in exocytosis, specifically during polarized growth of the emerging bud. J. Cell Biol. 155:581–592.
- Adamo, J. E., G. Rossi, and P. Brennwald. 1999. The Rho GTPase Rho3 has a direct role in exocytosis that is distinct from its role in actin polarity. Mol. Biol. Cell 10:4121–4133.
- Bartels, D. J., D. A. Mitchell, X. Dong, and R. J. Deschenes. 1999. Erf2, a novel gene product that affects the localization and palmitoylation of Ras2 in Saccharomyces cerevisiae. Mol. Cell. Biol. 19:6775–6787.
- Boyd, C., T. Hughes, M. Pypaert, and P. Novick. 2004. Vesicles carry most exocyst subunits to exocytic sites marked by the remaining two subunits, Sec3p and Exo70p. J. Cell Biol. 167:889–901.
- Brennwald, P., and P. Novick. 1993. Interactions of three domains distinguishing the Ras-related GTP-binding proteins Ypt1 and Sec4. Nature 362:560–563.
- Ghomashchi, F., X. Zhang, L. Liu, and M. H. Gelb. 1995. Binding of prenylated and polybasic peptides to membranes: affinities and intervesicle exchange. Biochemistry 34:11910–11918.
- Goud, B., A. Salminen, N. C. Walworth, and P. J. Novick. 1988. A GTP-binding protein required for secretion rapidly associates with secretory vesicles and the plasma membrane in yeast. Cell 53:753–768.
- Guo, W., F. Tamanoi, and P. Novick. 2001. Spatial regulation of the exocyst complex by Rho1 GTPase. Nat. Cell Biol. 3:353–360.
- Guthrie, C., and G. Fink (ed.). 1991. Guide to yeast genetics and molecular biology. Academic Press, San Diego, CA.
- Hancock, J. F., H. Paterson, and C. J. Marshall. 1990. A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane. Cell 63:133–139.
- He, B., F. Xi, J. Zhang, D. TerBush, X. Zhang, and W. Guo. 2007. Exo70p mediates the secretion of specific exocytic vesicles at early stages of the cell cycle for polarized cell growth. J. Cell Biol. 176:771–777.
- Heo, W. D., T. Inoue, W. S. Park, M. L. Kim, B. O. Park, T. J. Wandless, and T. Meyer. 2006. PI(3,4,5)P3 and PI(4,5)P2 lipids target proteins with polybasic clusters to the plasma membrane. Science 314:1458–1461.
- Horton, R. M., H. D. Hunt, S. N. Ho, J. K. Pullen, and L. R. Pease. 1989. Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene 77:61–68.
- Hougland, J. L., C. L. Lamphear, S. A. Scott, R. A. Gibbs, and C. A. Fierke. 2009. Context-dependent substrate recognition by protein farnesyltransferase. Biochemistry 48:1691–1701.
- Irazoqui, J. E., A. S. Gladfelter, and D. J. Lew. 2003. Scaffold-mediated symmetry breaking by Cdc42p. Nat. Cell Biol. 5:1062–1070.
- Linder, M. E., and R. J. Deschenes. 2007. Palmitoylation: policing protein stability and traffic. Nat. Rev. Mol. Cell Biol. 8:74–84.
- Maurer-Stroh, S., and F. Eisenhaber. 2005. Refinement and prediction of protein prenylation motifs. Genome Biol. 6:R55.
- Mitchell, D. A., A. Vasudevan, M. E. Linder, and R. J. Deschenes. 2006. Protein palmitoylation by a family of DHHC protein S-acyltransferases. J. Lipid Res. 47:1118–1127.
- Moores, S. L., M. D. Schaber, S. D. Mosser, E. Rands, M. B. O'Hara, V. M. Garsky, M. S. Marshall, D. L. Pompliano, and J. B. Gibbs. 1991. Sequence dependence of protein isoprenylation. J. Biol. Chem. 266:14603–14610.
- Nassar, N., G. R. Hoffman, D. Manor, J. C. Clardy, and R. A. Cerione. 1998. Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP. Nat. Struct. Biol. 5:1047–1052.
- Nelson, W. J. 2009. Remodeling epithelial cell organization: transitions between front-rear and apical-basal polarity. Cold Spring Harb. Perspect. Biol. 1:a000513.
- Robinson, N. G., L. Guo, J. Imai, E. A. Toh, Y. Matsui, and F. Tamanoi. 1999. Rho3 of Saccharomyces cerevisiae, which regulates the actin cytoskeleton and exocytosis, is a GTPase which interacts with Myo2 and Exo70. Mol. Cell. Biol. 19:3580–3587.
- Roth, A. F., Y. Feng, L. Chen, and N. G. Davis. 2002. The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyl transferase. J. Cell Biol. 159:23–28.
- Roth, A. F., J. Wan, A. O. Bailey, B. Sun, J. A. Kuchar, W. N. Green, B. S. Phinney, J. R. Yates III, and N. G. Davis. 2006. Global analysis of protein palmitoylation in yeast. Cell 125:1003–1013.
- Roumanie, O., H. Wu, J. N. Molk, G. Rossi, K. Bloom, and P. Brennwald. 2005. Rho GTPase regulation of exocytosis in yeast is independent of GTP hydrolysis and polarization of the exocyst complex. J. Cell Biol. 170:583–594.
- Seabra, M. C. 1998. Membrane association and targeting of prenylated Ras-like GTPases. Cell Signal. 10:167–172.
- Wedlich-Soldner, R., S. Altschuler, L. Wu, and R. Li. 2003. Spontaneous cell polarization through actomyosin-based delivery of the Cdc42 GTPase. Science 299:1231–1235.
- Wu, H., G. Rossi, and P. Brennwald. 2008. The ghost in the machine: small GTPases as spatial regulators of exocytosis. Trends Cell Biol. 18:397–404.
- Wu, H., C. Turner, J. Gardner, B. Temple, and P. Brennwald. 2010. The exo70 subunit of the exocyst is an effector for both cdc42 and rho3 function in polarized exocytosis. Mol. Biol. Cell 21:430–442.
- Yakir-Tamang, L., and J. E. Gerst. 2009. Phosphoinositides, exocytosis and polarity in yeast: all about actin? Trends Cell Biol. 19:677–684.
- Yon, J., and M. Fried. 1989. Precise gene fusion by PCR. Nucleic Acids Res. 17:4895.
- Zhang, X., E. Bi, P. Novick, L. Du, K. G. Kozminski, J. H. Lipschutz, and W. Guo. 2001. Cdc42 interacts with the exocyst and regulates polarized secretion. J. Biol. Chem. 276:46745–46750.