The phospholipid dependent protein kinase C is involved in regulation of cellular motility and energy metabolism. To study a possible direct interaction of protein kinase C with cellular motility and energy metabolism, we used purified rat brain protein kinase C to phosphorylate key proteins of these systems. Protein kinase C phosphorylates with comparable stoichiometry the G- but not the F-form of muscle and brain actin, the key protein of cellular motility. Glyceraldehyde-3-phosphate dehydrogenase, creatine kinase and glutamine synthase, key enzymes of energy metabolism, are also phosphorylated at comparable stoichiometry. The data suggest that protein kinase C might be directly involved in the regulation of cellular motility and energy metabolism.
|Number of pages||9|
|Journal||Biochemistry and Molecular Biology International|
|State||Published - 1996|