The anti-viral dynamin family member MxB participates in mitochondrial integrity

被引:11
作者
Cao, Hong [1 ,2 ]
Krueger, E. W. [2 ]
Chen, Jing [2 ]
Drizyte-Miller, Kristina [3 ]
Schulz, Mary E. [2 ]
McNiven, Mark A. [1 ,2 ]
机构
[1] Mayo Clin, Dept Biochem & Mol Biol, 200 1st St SW, Rochester, MN 55905 USA
[2] Mayo Clin, Div Gastroenterol & Hepatol, Ctr Basic Res Digest Dis, 200 1st St SW, Rochester, MN 55905 USA
[3] Mayo Clin, Grad Sch Biomed Sci, Biochem & Mol Biol Program, 200 1st St SW, Rochester, MN 55905 USA
关键词
CAPSID-BINDING; PROTEIN; GTPASE; REQUIRES; FISSION; DNA; FUSION; OLIGOMERIZATION; CRISTAE; MAINTENANCE;
D O I
10.1038/s41467-020-14727-w
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The membrane deforming dynamin family members MxA and MxB are large GTPases that convey resistance to a variety of infectious viruses. During viral infection, Mx proteins are known to show markedly increased expression via an interferon-responsive promoter to associate with nuclear pores. In this study we report that MxB is an inner mitochondrial membrane GTPase that plays an important role in the morphology and function of this organelle. Expression of mutant MxB or siRNA knockdown of MxB leads to fragmented mitochondria with disrupted inner membranes that are unable to maintain a proton gradient, while expelling their nucleoid-based genome into the cytoplasm. These findings implicate a dynamin family member in mitochondrial-based changes frequently observed during an interferon-based, anti-viral response.
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页数:13
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