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in called Ena--was known from other systems to bind profilin and affect actin.

The second paper exposes the other half of the pathway from the membrane downwards. It begins with Dlar, a gene causing the bypass phenotype. Dlar is a member of the receptor tyrosine phosphatase family-- membrane-spanning proteins that slice phosphate groups off other proteins inside the cell. Three years ago, Van Vactor and Haruo Saito, HMS professor of biological chemistry and molecular pharmacology, first implicated Dlar in axon guidance.

Trying to understand how Dlar signals, Van Vactor, working with graduate student Zachary Wills and others, discovered that a triumvirate of proteins--Dlar, Abl, and Ena--is bound together in intimate, antagonistic relationships. The trio makes key decisions about what information is transmitted to the cytoskeleton, Van Vactor says.

Evidence supporting that idea also comes from experiments testing the sensitivity of one protein to the dose of another. The scientists found that Dlar is as sensitive to the amount of Abl as is profilin. Halving the amount of Abl protein suppresses the damage wrought by the Dlar mutation--that is, fewer ISNb nerves bypass their targets. Conversely, increasing the amount of Abl protein beyond normal levels overwhelmed Dlar and produced the bypass phenotype in normal fly embryos, just as if they had a Dlar mutation.

This key experiment shows that the kinase Abl and the phosphatase Dlar are opposing enzymes locked in a balance of power, and each one can tip the scale. Bringing the research full circle, the scientists show that an object of this competition was the phosphate recipient Ena, the protein known to interact with profilin.

One reason this work appears complicated is that even though the researchers have established a sequence of players, they still do not fully understand the precise relationships among them.

It is not as if a valve opened at
'"/>

Contact: Peta Gillyatt
gillyatt@hms.harvard.edu
617-432-0443
Harvard Medical School
26-Feb-1999


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