TY - JOUR
T1 - The antiviral dynamin family member, MxA, tubulates lipids and localizes to the smooth endoplasmic reticulum
AU - Accola, Molly A.
AU - Huang, Bing
AU - Masri, Azzah Al
AU - McNiven, Mark A.
PY - 2002/6/14
Y1 - 2002/6/14
N2 - 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.
AB - 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.
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U2 - 10.1074/jbc.M201641200
DO - 10.1074/jbc.M201641200
M3 - Article
C2 - 11916975
AN - SCOPUS:0037077224
SN - 0021-9258
VL - 277
SP - 21829
EP - 21835
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 24
ER -