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Cancer researchers find key protein link
Date:3/27/2014

HOUSTON (March 27, 2014) A new understanding of proteins at the nexus of a cell's decision to survive or die has implications for researchers who study cancer and age-related diseases, according to biophysicists at the Rice University-based Center for Theoretical Biological Physics (CTBP).

Experiments and computer analysis of two key proteins revealed a previously unknown binding interface that could be addressed by medication. Results of the research appear this week in an open-source paper in the Proceedings of the National Academy of Sciences.

The proteins are Bcl-2, well-known for its role in programmed cell death, and NAF-1, a member of the NEET family that binds toxic clusters of iron and sulfur. How the two interact is now known as a major determinant in the cell processes of autophagy and apoptosis -- literally, life and death. An ability to uncover binding sites on the proteins that send the cell one way or the other opens a path toward the regulation of those processes, according to Jos Onuchic, Rice's the Harry C. and Olga K. Wiess Chair of Physics and professor of physics and astronomy.

Pockets and folds in proteins exist to bind to other molecules and catalyze actions in a cell in signaling pathways. The ability to block a specific binding site or to enhance a desired interaction is critical to drug design, Onuchic said.

"In our early work we have shown the link between NEET proteins and cancer. Now we can understand the molecular details of how these interactions are governed," Onuchic said. "Others have shown that NAF-1 is up-regulated in cancer cells, which leads us to believe that cancer may hijack control over the expression of this protein. This affects the cell's system of checks and balances. Understanding NAF-1 gives us a better idea of how to approach treatment."

The researchers found that NAF-1 binds to two specific regions of the protein Bcl-2 and that Bcl-2 binds to the NAF-
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Contact: David Ruth
david@rice.edu
713-348-6327
Rice University
Source:Eurekalert  

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