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J. Biol. Chem., Vol. 276, Issue 36, 33328-33335, September 7, 2001

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Analysis of the -Actinin/Zyxin Interaction^*

Bo Li and Beat Trueb

From the M. E. Müller Institute, University of Bern, P. O. Box 30, CH-3010 Bern, Switzerland

The yeast two-hybrid system was used to search for interaction partners of human zyxin. Screening of two different cDNA libraries, one prepared from human placenta, the other from human heart, yielded several positive clones that occurred in both searches, including clones coding for cyclophilin, nebulette, and -actinin. The zyxin/-actinin interaction was analyzed in detail. By site-directed mutagenesis, a linear motif of 6 amino acids (Phe-Gly-Pro-Val-Val-Ala) present at the N terminus of zyxin was found to play a critical role. Replacement of a single amino acid within this motif abolished binding to -actinin in blot overlays as well as in living cells. On the other hand, the interaction site in -actinin was mapped to a conformational determinant present in the center of the protein as demonstrated by a fragment deletion analysis. This binding site involved a tandem array of two complete spectrin-like domains. Only fragments that were able to dimerize in yeast also bound to zyxin, suggesting that dimerization of -actinin is essential for zyxin binding.

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