Phosphorylation of MARCKS, neuromodulin, and neurogranin by protein kinase C exhibits differential responses to diacylglycerols
| Autor: | Koichi Seki, Charles W. Mahoney, Kuo-Ping Huang |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Nerve Tissue Proteins
Diglycerides chemistry.chemical_compound GAP-43 Protein Phosphatidylcholine Pi Animals Phosphatidylinositol Neurogranin Phosphorylation Gap-43 protein MARCKS Myristoylated Alanine-Rich C Kinase Substrate Protein Kinase C Protein kinase C Membrane Glycoproteins biology Chemistry Intracellular Signaling Peptides and Proteins Brain Membrane Proteins Proteins Cell Biology Phosphoproteins Molecular biology Rats Enzyme Activation Biochemistry biology.protein Calmodulin-Binding Proteins |
| Zdroj: | Cellular Signalling. 7:679-685 |
| ISSN: | 0898-6568 |
| DOI: | 10.1016/0898-6568(95)00043-o |
| Popis: | Diacylglycerols (DG) derived from brain phosphatidylinositol (PI) and phosphatidylcholine (PC) and synthetic 1,2-dioleoylglycerol (diC18:1) and 1,2-dioctanoylglycerol (diC8) were tested for their efficacy in stimulating PKC-catalyzed phosphorylation of three physiological substrates in the brain, namely, MARCKS, neuromodulin (Nm), and neurogranin (Ng). The A0.5 of these DGs for PKC were variable dependent on the protein substrates; the values were lowest with MARCKS and highest with Ng. With Ng as a substrate the A0.5 of these DGs for PKC γ were PI- and PC-DGs < diC18:1 < diC8. Both PI- and PC-DGs, in spite of their differences in unsaturated fatty acids content, were similarly effective in stimulating PKC. Since the phosphorylation of MARCKS, as compared to those of Nm and Ng, has the lowest A0.5 with the various DGs, it seems that among these three PKC substrates MARCKS is most readily phosphorylated by PKCs following DG formation in vivo. |
| Databáze: | OpenAIRE |
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