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Scientists discover a mechanism that can send cells on the road to cancer
Date:4/22/2008

ey hypothesized that the answer could be found in the activity of yet another protein, called Myc, which Dr. Tansey has spent much of his career studying. Myc is an oncoprotein: one that is important in a great many regulatory processes in the cell, and which, when overexpressed, can cause dysregulation that leads to cancer.

Prior work had shown that when E1A was present in a cell, the potentially dangerous Myc protein was stable -- it did not degrade naturally. In new experiments, Tansey and colleagues found that E1As stabilization of the Myc protein was accomplished not, as was suspected by some, by directly inhibiting its degradation in a cellular component called the proteosome, which destroys proteins. Rather, E1A stabilized Myc by promoting its binding with p400.

To recap the complex sequence of events: E1A, when present in a cell, binds to p400. That protein, in turn, forms a complex with Myc which accounts for Mycs stability in cells in which E1A is present. Close study showed that the piece of the E1A protein that was important for stabilizing Myc was the same piece that bound to p400, Dr. Tansey said. And just as E1A can pull the Rb protein away from E2F, initiating a cascade of pathologies potentially leading to oncogenesis, so does the ability of E1A to bind p400 -- and via that connection to engage Myc -- stabilize that oncoprotein and open the door to tumorigenesis.

We know now that the interaction of E1A and p400 is very important in terms of regulating cell growth in normal and cancer cells, Dr. Tansey said. So were taking a cue from the history of work on adenoviruses and were leaving E1A behind to concentrate on Myc and p400. For us, now, the next step is to learn more about the p400-Myc connection.


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Contact: Jim Bono
bono@cshl.edu
516-367-8455
Cold Spring Harbor Laboratory
Source:Eurekalert

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