Article
Cross-talk phosphorylations by protein kinase C and Pho85p-Pho80p protein kinase regulate Pah1p phosphatidate phosphatase abundance in Saccharomyces cerevisiae.
The Journal of biological chemistry - 4 Jul 2014
Su Wen-Min, Han Gil-Soo, Carman George M
Abstract excerpt
Yeast Pah1p is the phosphatidate phosphatase that catalyzes the penultimate step in triacylglycerol synthesis and plays a role in the transcriptional regulation of phospholipid synthesis genes. The enzyme is multiply phosphorylated, some of which is mediated by Pho85p-Pho80p, Cdc28p-cyclin B, and...
Topics
- Binding Sites
- Cyclin-Dependent Kinases
- Cyclins
- Mutation
- Phosphatidate Phosphatase
- Phosphorylation
- Protein Kinase C
- Proteolysis
- Saccharomyces cerevisiae
- Saccharomyces cerevisiae Proteins
- Serine