Analysis of novel regulatory mechanism of apoptosis mediated by the posttranslational N-myristoylation of protein

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Protein N-myristoylation has been recognized as a cotranslational protein modification. Recently, it was demonstrated that protein N-myristoylation could also occur posttranslationally during apoptosis as in the case of BID, actin, gelsolin and PAK2. The posttranslational N-myristoylation has been shown to play a crucial role in the biological activity of BID, gelsolin, and PAK2. However, it was not fully accepted that the reaction is a universal posttranslational modification frequently observed during the apoptosis pathway.In this study, we established the strategy for genome-wide screening of posttranslationally N-myristoylated proteins. Using this strategy, we could successfully demonstrate that the posttranslational myristoylation of caspase cleavage product represents a universal mechanism widely used to regulate cellular apoptosis.