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MBC in Press, published online ahead of print October 3, 2007
Mol. Biol. Cell 10.1091/mbc.E07-07-0676

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Submitted on July 18, 2007
Revised on September 10, 2007
Accepted on September 25, 2007

Identification of Novel Membrane-binding Domains in Multiple Yeast Cdc42 Effectors

Satoe Takahashi and Peter M. Pryciak

Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, MA 01605

Monitoring Editor: Martin A. Schwartz

The Rho-type GTPase Cdc42 is a central regulator of eukaryotic cell polarity and signal transduction. In budding yeast, Cdc42 regulates polarity and MAP kinase signaling in part through the PAK-family kinase Ste20. Activation of Ste20 requires a Cdc42/Rac interactive binding (CRIB) domain, which mediates its recruitment to membrane-associated Cdc42. Here, we identify a separate domain in Ste20 that interacts directly with membrane phospholipids and is critical for its function. This short region, termed the basic-rich (BR) domain, can target GFP to the plasma membrane in vivo and binds PIP2-containing liposomes in vitro. Mutation of basic or hydrophobic residues in the BR domain abolishes polarized localization of Ste20 and its function in both MAP kinase-dependent and independent pathways. Thus, Cdc42 binding is required but is insufficient; instead, direct membrane binding by Ste20 is also required. Nevertheless, phospholipid specificity is not essential in vivo, as the BR domain can be replaced with several heterologous lipid-binding domains of varying lipid preferences. We also identify functionally important BR domains in two other yeast Cdc42 effectors, Gic1 and Gic2, suggesting that cooperation between protein-protein and protein-membrane interactions is a prevalent mechanism during Cdc42-regulated signaling, and perhaps for other dynamic localization events at the cell cortex.

Address correspondence to: Peter M. Pryciak (peter.pryciak{at}umassmed.edu)




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K. Orlando, J. Zhang, X. Zhang, P. Yue, T. Chiang, E. Bi, and W. Guo
Regulation of Gic2 Localization and Function by Phosphatidylinositol 4,5-Bisphosphate during the Establishment of Cell Polarity in Budding Yeast
J. Biol. Chem., May 23, 2008; 283(21): 14205 - 14212.
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