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MBC in Press, published online ahead of print February 2, 2005
Mol. Biol. Cell 10.1091/mbc.E04-07-0564

A more recent version of this article appeared on April 1, 2005
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Submitted on July 7, 2004
Accepted on January 25, 2005

The PH Domain Proteins Slm1 and Slm2 Are Required for Actin Cytoskeleton Organization in Yeast and Bind PtdIns(4,5)P2 and TORC2

Maria Fadri,* Alexes Daquinag,* Shimei Wang, Tao Xue, and Jeannette Kunz

Department of Molecular Physiology and Biophysics, Baylor College of Medicine, Houston, TX 77030

Monitoring Editor: Sandra Schmid

Phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2) is a key second messenger that regulates actin and membrane dynamics, as well as other cellular processes. Many of the effects of PtdIns(4,5)P2 are mediated by binding to effector proteins that contain a pleckstrin homology (PH) domain. Here we identify two novel effectors of PtdIns(4,5)P2 in the budding yeast S. cerevisiae: the PH domain containing protein Slm1 and its homolog Slm2. Slm1 and Slm2 serve redundant roles essential for cell growth and actin cytoskeleton polarization. Slm1 and Slm2 bind PtdIns(4,5)P2 through their PH domains. In addition Slm1 and Slm2 physically interact with Avo2 and Bit61, two components of the TORC2 signaling complex, which mediates Tor2 signaling to the actin cytoskeleton. Together, these interactions coordinately regulate Slm1 targeting to the plasma membrane. Our results thus identify two novel effectors of PtdIns(4,5)P2 regulating cell growth and actin organization and suggest that Slm1 and Slm2 integrate inputs from the PtdIns(4,5)P2 and TORC2 to modulate polarized actin assembly and growth.

*These authors contributed equally to this work.

Address correspondence to: Jeannette Kunz (jkunz{at}bcm.tmc.edu)




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