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New study defines the long-sought structure of a protein necessary for cell-cell interaction
Date:1/6/2013

#945;-catenin forms links to the cytoskeleton by binding to a protein called F-actin (the "F" stands for filament), which is found in species ranging from yeast to humans. The paradox for scientists has been that, despite being able to bind to F-actin on its own, when bound to α-catenin α-catenin cannot bind to F-actin. That is, the binding of α-catenin to F-actin and to β-catenin are, in the test tube, mutually exclusive. So how does α-catenin bind to F-actin versus β-catenin and how is the final link in the chain stabilized in cells?

To resolve this paradox, the scientists crystallized and determined the structure of a nearly full-length human α-catenin. This structure showed why α-catenin cannot simultaneously bind to F-actin and β-catenin. Specifically, in its unbound state, α-catenin was shown to be an asymmetric dimer, where the two subunits have remarkable differences in their architecture that appear to together create the binding site for F-actin. Binding of β-catenin to α-catenin disrupts the interaction of its two subunits, changing its architecture and displacing F-actin.

The second part of the puzzlehow cadherin-β-catenin and α-catenin-F-actin complexes are linked together in cellswas resolved when the scientists realized that another cytoskeleton protein called vinculin, which can also bind to F-actin, plays a critical role in this process. The scientists established the structures of dimeric α-catenin alone and when in complex with pre-activated vinculin. The results showed that vinculin binding did not disrupt the α-catenin dimer and that both partners of the vinculin-α-catenin complex were in fact capable of binding to F-actin, a scenario that stabilizes adhesion complexes.


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Contact: Eric Sauter
esauter@scripps.edu
267-337-3859
Scripps Research Institute
Source:Eurekalert  

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