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Volume 272, Number 32, Issue of August 8, 1997 pp. 20088-20095
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

A Dual Involvement of the Amino-terminal Domain of Ezrin in F- and G-actin Binding

(Received for publication, March 14, 1997, and in revised form, May 9, 1997)

From the Laboratoire de Dynamique Moléculaire des Interactions Membranaires, CNRS UMR 5539, Université Montpellier II, Bât. 24, CC107, place Eugène Bataillon, 34095 Montpellier Cedex 5, France

Human recombinant ezrin, or truncated forms, were coated in microtiter plate and their capacity to bind actin determined. F-actin bound ezrin with a K_d of 504 ± 230 nM and a molecular stoichiometry of 10.6 actin per ezrin. Ezrin bound both - and /-actin essentially as F-form. F-actin binding was totally prevented or drastically reduced when residues 534-586 or 13-30 were deleted, respectively. An actin binding activity was detected in amino-terminal constructs (ezrin 1-310 and 1-333) provided the glutathione S-transferase moiety of the fusion protein was removed. Series of carboxyl-terminal truncations confirmed the presence of this actin-binding site which bound both F- and G-actin. The F- and G-actin-binding sites were differently sensitive to various chemical effectors and distinct specific ezrin antibodies. The internal actin-binding site was mapped between residues 281 and 333. The association of ezrin amino-terminal fragment to full-length ezrin blocked F-actin binding to ezrin. It is proposed that, in full-length ezrin, the F-actin-binding site required the juxtaposition of the distal-most amino- and carboxyl-terminal residues of the ezrin molecule.

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