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 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.
Reiss
N
N
Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Israel.
Hermon
J
J
Oplatka
A
A
Naor
Z
Z
D000199:Actins / Q000378:metabolism*; D000818:Animals; D001921:Brain / Q000201:enzymology; D002465:Cell Movement / Q000502:physiology; D003402:Creatine Kinase / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D004734:Energy Metabolism; D005974:Glutamate-Ammonia Ligase / Q000378:metabolism*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism*; D009132:Muscles / Q000737:chemistry / Q000378:metabolism; D010766:Phosphorylation; D011493:Protein Kinase C / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats; D012967:Sodium Dodecyl Sulfate
D000199:Actins; D012967:Sodium Dodecyl Sulfate; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D011493:Protein Kinase C; D003402:Creatine Kinase; D005974:Glutamate-Ammonia Ligase