Proteolytic fragment of protein kinase C (kinase M) phosphorylates in vitro phosphatidylinositol-4-phosphate.
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.
Tusupov
O K
OK
M.V. Lomonosov Institute of Fine Chemical Technology, Moscow, USSR.
Severin
S E
SE
Shvets
V I
VI
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001921:Brain / Q000201:enzymology; D007700:Kinetics; D008954:Models, Biological; D008970:Molecular Weight; D010446:Peptide Fragments / Q000378:metabolism*; D018129:Phosphatidylinositol Phosphates; D010716:Phosphatidylinositols / Q000302:isolation & purification / Q000378:metabolism*; D010761:Phosphorus Radioisotopes; D010766:Phosphorylation; D011493:Protein Kinase C / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D014357:Trypsin / Q000378:metabolism
D010446:Peptide Fragments; D018129:Phosphatidylinositol Phosphates; D010716:Phosphatidylinositols; D010761:Phosphorus Radioisotopes; C037178:phosphatidylinositol 4-phosphate; D000255:Adenosine Triphosphate; D011493:Protein Kinase C; D014357:Trypsin