INTERACTION OF PURIFIED PROTEIN-KINASE-C WITH KEY PROTEINS OF ENERGY-METABOLISM AND CELLULAR MOTILITY

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 met abolism, we used purified rat brain protein kinase C to phosphorylate key proteins of these systems. Protein kinase C phosphorylates with co mparable stoichiometry the G- but not the F- form of muscle and brain actin, the key protein of cellular motility. Glyceraldehyde-3-phosphat e dehydrogenase, creatine kinase and glutamine synthase, key enzymes o f energy metabolism, are also phosphorylated at comparable stoichiomet ry. The data suggest that protein kinase C might be directly involved in the regulation of cellular motility and energy metabolism.