Sumoylation and phosphorylation are post-translational modifications that have been
identified as important regulatory events that are implicated in several cellular processes.
The aim of this research was to study a cross-talk between sumoylation and phosphorylation
during the cell cycle, specifically by analyzing the activity of CDC2 upon inhibition of
sumoylation with a sumoylation inhibitor, ginkgolic acid (GA), and physiological/low levels
of H2O2. The activity of CDC2 was assessed using antibodies against an inactive and total
isoform of the protein. Our data suggest that inhibition of sumoylation activates CDC2 and,
therefore, its activity is inhibited by sumoylation. Further studies will address the mechanism
of the inhibition.
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