Substrate-specific stimulation of protein kinase C by polyvalent anions

Mohammad D. Bazzi, Gary L Nelsestuen

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

The activity of protein kinase C (PKC) toward arginine-rich substrates was greatly stimulated by sulfate and phosphate, but not by monovalent anions. This stimulation did not require phospholipid, calcium, or diacylglycerol, and appeared to mimic the stimulation by phospholipid. Anionic proteins such as bovine serum albumin also promoted PKC activity toward certain substrates that were characterized by either high arginine or high lysine content. The mechanism of both of these stimulations appeared to be related to formation of a substrate-PKC complex which is essential to phosphorylation by PKC. Polyvalent anions bind the cationic substrate and, together with PKC, form an aggregate which allows phosphorylation. Potential physiological relevance of this stimulation is discussed.

Original languageEnglish (US)
Pages (from-to)248-253
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume147
Issue number1
DOIs
StatePublished - Aug 31 1987

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