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New way to control protein activity could lead to cancer therapies
Date:9/28/2008

ion is knocked out, it can't be turned back on or difficult to execute.

The new technique, instead, influences the level of speed with which the protein is broken downa much faster process than its production. Moreover, it is reversible and works like a dimmer switch for an overhead light. The rate of a protein's degradation and, thus, the level of its biological activity can be increased or decreased by supplying more or less of Shield-1, permitting scientists to study the biological effects of slightly increasing or diminishing a protein's activity inside a cell over short time frames: for example, during a particular period in an organism's development.

The Stanford team succeeded in controlling levels of proteins by a relatively simple method pioneered by Wandless and his then-graduate student, Laura Banaszynski, PhD. They created special, bioengineered versions of several different proteins, in each case altering the protein by adding a small extra piece that didn't interfere with its biological function, but flagged it for rapid degradation. This degradation can be halted in its tracks, however, by Shield-1, which binds to the bioengineered protein, shielding it from destruction by the cell's breakdown machinery. The drug thus can enhance the bioengineered protein's intracellular concentration and activity; withdrawing the drug has the opposite effect.

"The process is tunable, and fast. As soon as you remove the drug, you affect the degradation time of the protein," said Mark Sellmyer, a graduate student at the School of Medicine, who shares lead authorship of the study with Banaszynski.

The degradation-vulnerable bioengineered proteins were each produced by attaching the gene coding for a protein to another DNA sequence coding for the small extra piece that flags the protein for rapid degradation. The scientists then inserted the altered gene into a virus capable of inf
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Contact: Bruce Goldman
goldmanb@stanford.edu
650-725-2106
Stanford University Medical Center
Source:Eurekalert

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