Correlation between Membrane Binding and Phosphorylation by Protein Kinase C of Acylated Protein(Biological Chemistry)

概要

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The relationship between membrane binding and phosphorylation by protein kinase C(PKC) of acylated protein was examined using chemically acylated lysozyme and phosphatidylserine(PS)-containing dipalmitoylphosphatidylcholine(DPPC) vesicles. Lysozyme monoacylated with a short chain fatty acid such as caproic acid (C_6) was neither bound nor phosphorylated similarly to native lysozyme. With monoacylated lysozyme with the longer chain fatty acids from caprylic acid (C_8) to myristic acid (C_<14>), on the contrary, both membrane binding and phosphorylation increased linearly as the fatty acid chain length increased and reached the maximum value with monomyristoylated lysozyme. The similarity of the profiles in increase in membrane binding and phosphorylation indicated that these two phenomena might be concomitant events. It was also found that the phosphorylated monomyristoylated lysozyme was detected exclusively in the vesicle fraction and the phosphorylation of unbound monomyristoylated lysozme was negligible. These data suggest that the membrane binding mediated by protein acylation directs the protein phosphorylation by PKC.
社団法人日本農芸化学会の論文
1990-01-23