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

mes. Says Yang, this enables p53, which at most is present at 10 percent the abundance of G6PD, to regulate its binding partner.

"By converting G6PD from active to inactive form, p53 also has an enzymatic function," says Yang. That kind of mechanism, he says, is "totally new" for p53, and a new paradigm for signal transduction in general.

"This non-stoichiometric effect of p53 on G6PDH is intriguing as it proposes a catalytic role for p53, something that even in the p53 world, which is accustomed to occasional twists, is surprising," wrote Eyal Gottlieb of Cancer Research UK in an accompanying editorial.

Now, says Yang, the question is whether this new role for p53 can be exploited to yield novel anticancer therapies. "Previously," he says, "people were hesitant to target the inefficient pathway because they thought it was stimulatory. Our data suggests the pathway is a good target."


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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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