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

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

DOI:
10.1074/jbc.m201641200
复制
发表时间:
2002-06-14
影响因子:
4.8
通讯作者:
McNiven, MA
McNiven, MA
中科院分区:
生物学2区
文献类型:
--
作者:
Accola, MA;Huang, B;McNiven, MA

文献摘要

被引文献

相似文献

MX蛋白由I型干扰素诱导,并通过未知的机制抑制广泛的病毒。它们属于大型GTP酶的Dynamin家族,参与囊泡运输,并具有共同的生物物理特征。这些特性包括自组装的倾向,对脂质的亲和力,以及管状膜的能力。在这份报告中,我们确定了人类MXA,尽管与传统的Dynamin只有30%的同源性,但拥有许多这些特性。我们首次证明了MXA在体外自组装成管状脂类的环,并与细胞中特定的膜室--平滑内质网联系在一起。
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.