An upstream regulator and downstream target of phospholipase D1 activity during pheromone response in Saccharomyces cerevisiae. FEMS Yeast Res 2008 Mar;8(2):237-44
Date
11/27/2007Pubmed ID
18036176DOI
10.1111/j.1567-1364.2007.00336.xScopus ID
2-s2.0-38849100432 (requires institutional sign-in at Scopus site) 7 CitationsAbstract
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.
Author List
Harkins AL, London SD, Dolan JWAuthor
April Harkins PhD Assistant Professor in the Clinical Laboratory Science department at Marquette UniversityMESH terms used to index this publication - Major topics in bold
Gene DeletionIntracellular Signaling Peptides and Proteins
MAP Kinase Kinase Kinases
Models, Biological
Pheromones
Phosphatidic Acids
Phospholipase D
Protein Binding
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
cdc42 GTP-Binding Protein, Saccharomyces cerevisiae
