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Originally published In Press as doi:10.1074/jbc.M201641200 on March 26, 2002

J. Biol. Chem., Vol. 277, Issue 24, 21829-21835, June 14, 2002
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The Antiviral Dynamin Family Member, MxA, Tubulates Lipids and Localizes to the Smooth Endoplasmic Reticulum*

Molly A. AccolaDagger , Bing Huang, Azzah Al Masri, and Mark A. McNiven§

From the Center for Basic Research in Digestive Diseases and Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, Minnesota 55905

Mx proteins are induced by type I interferon and inhibit a broad range of viruses by undefined mechanisms. They are included within the dynamin family of large GTPases, which are involved in vesicle trafficking and share common biophysical features. These properties include the propensity to self-assemble, an affinity for lipids, and the ability to tubulate membranes. In this report we establish that human MxA, despite sharing only 30% homology with conventional dynamin, possesses many of these properties. We demonstrate for the first time that MxA self-assembles into rings that tubulate lipids in vitro, and associates with a specific membrane compartment in cells, the smooth endoplasmic reticulum.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Present address: Third Wave Technologies, Inc., Madison, WI 53719.

§ To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, Mayo Clinic, 200 First St., S. W., Rochester MN 55905. Tel.: 507-284-0683; Fax: 507-284-0762; E-mail: mcniven.mark@mayo.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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