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Updated: Jul 9, 2026

Detection of Phospholipase C Activity in the Brain Homogenate from the Honeybee
Published on: September 14, 2018
An upstream regulator and downstream target of phospholipase D1 activity during pheromone response in Saccharomyces
April L Harkins1, Steven D London, Joseph W Dolan
1Department of Microbiology and Immunology, Medical University of South Carolina, Charleston, SC, USA. april.harkins@marquette.edu
Abstract:
Phospholipase D1 (PLD1), which is the product of the SPO14 gene, has been shown to play a role in the process of polarized cell growth (PCG) during the pheromone response in Saccharomyces cerevisiae. PLD1 hydrolyzes phosphatidylcholine to produce phosphatidic acid (PA) and a free choline headgroup. This study investigated the interactions of PLD1 and PA with two proteins known to be involved in the cellular signaling leading to PCG in yeast, the small GTPase Cdc42p and the PAK family kinase Ste20p. Constitutively activated Cdc42p stimulates PLD1 activity. Protein-lipid binding blots confirmed the specific binding of Ste20p to the PLD1 product, PA. Finally, kinase activity assays provided evidence for the stimulation of Ste20p by PA. These findings highlight the important interactions among PLD1, Cdc42p and Ste20p during PCG in S. cerevisiae.
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