Article
Phosphorylation of phosphatidate phosphatase regulates its membrane association and physiological functions in Saccharomyces cerevisiae: identification of SER(602), THR(723), AND SER(744) as the sites phosphorylated by CDC28 (CDK1)-encoded cyclin-dependent kinase.
The Journal of biological chemistry - 14 Jan 2011
Choi Hyeon-Son, Su Wen-Min, Morgan Jeanelle M, Han Gil-Soo, Xu Zhi, Karanasios Eleftherios, Siniossoglou Symeon, Carman George M
Abstract excerpt
The Saccharomyces cerevisiae PAH1-encoded phosphatidate phosphatase (PAP) catalyzes the penultimate step in the synthesis of triacylglycerol and plays a role in the transcriptional regulation of phospholipid synthesis genes. PAP is phosphorylated at multiple Ser and Thr residues and is dephosphorylated for in vivo function by the Nem1p-Spo7p protein phosphatase complex localized in the nuclear/endoplasmic...
Topics
- CDC28 Protein Kinase, S cerevisiae
- Endoplasmic Reticulum
- Inositol
- Lipid Metabolism
- Mutagenesis, Site-Directed
- Nuclear Envelope
- Phenotype
- Phosphatidate Phosphatase
- Phosphatidic Acids