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Penn researchers find new role for cancer protein p53
Date:3/2/2011

When it takes up glucose, a cell has three choices: It can store the sugar, turn it into energy, or use it to make nucleic acids and lipids. As Yang explains, researchers have recognized for years that tumor cells consume glucose far faster than non-cancerous cells, but also that they don't seem to use the most energy efficient pathway to burn the fuel. What, then, were they doing with it?

Yang and his team found in both human colon cancer cells and fibroblast cells from mouse embryos that loss of p53 leads to increased glucose consumption though the energy inefficient pathway. This increase was associated with greater lipid synthesis and increased activity of G6PD, the enzyme that p53 is supposed to latch onto to shunt glucose into storage, not wild synthesis.

The team found that p53 binds directly to G6PD to inhibit its activity, apparently by interfering with the ability of G6PD to form a molecular complex. In contrast, p53 mutants lack this binding activity. In effect, demonstrating the binding role of p53 is distinct from its function as a regulator of protein transcription.

Intriguingly, Yang and his team estimate that the level of p53 is only about 3 percent that of G6PD. So in the cell, the p53/G6PD ratio is very low. But p53 has a dramatic effect on the overall activity of G6PD. This suggests that one p53 molecule can inactivate many G6PD molecules. This qualifies p53 as a catalyst. It appears to act almost as an enzyme to convert its much more abundant binding partner into an inactive form via transient rather than stable interactions.

Normally, when one protein binds to and inhibits another, that inhibition lasts only as long as the two proteins are bound together; dissolution of the complex almost invariably activates the released proteins. But in the case of p53 and G6PD, transient interaction with p53 is sufficient to convert G6PD into an inactive form - a property that is most often associated with enzy
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Contact: Karen Kreeger
karen.kreeger@uphs.upenn.edu
215-349-5658
University of Pennsylvania School of Medicine
Source:Eurekalert  

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