Proteolytic fragment of protein kinase C (kinase M) phosphorylates in vitro phosphatidylinositol-4-phosphate. |
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Authors: | O K Tusupov S E Severin V I Shvets |
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Institution: | M.V. Lomonosov Institute of Fine Chemical Technology, Moscow, USSR. |
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Abstract: | Limited tryptic proteolysis of homogeneous protein kinase C induces the formation of a catalytically active fragment of 50 kDa (kinase M) which, unlike native PK C acquires the ability to phosphorylate PIP. Both ATP and GTP were found to be capable of serving as phosphate donors in this process. Incubation of purified kinase M with a preparation of rat brain membrane fraction enhanced the level of phosphorylation of PIP in the presence and in the absence of exogenous PIP. A scheme of the interrelationship of phosphoinositide metabolism and the proteolytic processing of protein kinase C is proposed. |
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