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A protein kinase C‐related enzyme activity in Dictyostelium discoideum
Author(s) -
Ludérus M.E.Eva,
Van der Most Robbert G.,
Otte Arie P.,
Van Driel Roel
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80932-9
Subject(s) - dictyostelium discoideum , staurosporine , protein kinase c , enzyme , biochemistry , phosphatidylserine , protein kinase a , phosphorylation , dictyostelium , microbiology and biotechnology , kinase , chemistry , biology , phospholipid , membrane , gene
In crude cell lysates of the cellular slime mould Dictyostelium discoideum we identified a protein kinase C (PKC)‐like enzyme activity. This activity, measured as phosphorylation of a synthetic EGF‐receptor‐derived peptide [(1987) J. Biol. Chem. 262, 772–777], was regulated by Ca 2+ , phosphatidylserine (PS), 1,2‐dioleoyl‐rac‐glycerol (DG) and the phorbol ester PMA. PS and DG stimulated the enzyme in a synergistic manner. The stimulation by these lipids was, in contrast to what has been found for ‘classical’ mammalian PKC, not dependent on Ca 2+ . The D. discoideum enzyme was strongly stimulated by nanomolar concentrations of PMA, and inhibited by PKC‐inhibitor staurosporine.