Interaction of purified protein kinase C with key proteins of energy metabolism and cellular motility

Nachum Reiss, Jacob Hermon, Avraham Oplatka, Zvi Naor

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Pages (from-to)711-719
Number of pages9
JournalBiochemistry and Molecular Biology International
Volume38
Issue number4
StatePublished - 1996

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