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M201641200v1
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Papers In Press, published online ahead of print March 26, 2002
J. Biol. Chem, 10.1074/jbc.M201641200
Submitted on February 18, 2002
Revised on March 26, 2002
Accepted on March 26, 2002

The antiviral dynamin family member, MxA, tubulates lipids and localizes to the smooth endoplasmic reticulum

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

Center for Basic Research in Digestive Diseases & Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, MN 55905

Corresponding Author: mcniven.mark{at}mayo.edu

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, can tubulate lipids in vitro, and associates with a specific membrane compartment in cells, the smooth ER.


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