Contribution of phosphatidylserine to Rho1- and Pkc1-related repolarization of the actin cytoskeleton under stressed conditions in Saccharomyces cerevisiae.

The budding yeast Saccharomyces cerevisiae undergoes polarized cell growth, which is established in association with actin polarization. Rho1, one of the Rho-type GTPases in S. cerevisiae, is crucial for maintaining polarized cell growth and actin polarization and controlling the downstream signaling pathway, the Pkc1-Mpk1 MAP kinase cascade, through a physical interaction with Pkc1, the sole protein kinase C in this yeast. The Pkc1-Mpk1 MAP kinase cascade is important for the repolarization of actin under heat shock-stressed conditions. We recently reported that phosphatidylserine (PS), a membrane phospholipid component, played a pivotal role in the physical interaction between Rho1 and Pkc1 as well as the activation of the Pkc1-Mpk1 MAP kinase cascade. However, it currently remains unclear whether PS is involved in actin polarization by regulating the physical interaction between Rho1 and Pkc1. We herein demonstrated that the C1 domain of Pkc1, which is responsible for the interaction with Rho1, was crucial for Rho1-regulated actin polarization. We also found that actin repolarization under heat shock-stressed conditions was impaired in a mutant defective in CHO1 encoding PS synthase. These results suggest that PS contributes to actin polarization in which Rho1 and Pkc1 play a crucial role.

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