Abstract
The structure, biochemistry and effect of mutagenesis suggest a more complex regulation of GSK-3 than previously imagined. This protein kinase is able to process at least two different stimuli and deliver distinct outcomes. This in part may be due to compartmentalization of GSK-3 action within the cell, but what these recent results suggest is that specificity could also be achieved by intrinsic properties of GSK-3. These could allow a common pool of GSK-3 to participate in multiple pathways, but limit inappropriate cross-talk. These results may also lead to the design of function-specific drugs that disrupt some actions of GSK-3, but leave others intact. To date much of our knowledge of GSK-3 activity is based on in vitro studies. With the GSK-3 structure, we are now in the position to design mutant proteins that lack some but not all of the kinase properties and test our knowledge gained in vitro in the context of the cell.
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