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2018 - Romo1 is a mitochondrial nonselective cation channel with viroporin-like characteristics

icon pap   Port-a-Patch and   icon vpp   Vesicle Prep Pro publication in Journal of Cell Biology (2018)

Authors:
Lee G.Y., You D.G., Lee H.R., Hwang S.W., Lee C.J., Do Yoo Y.

Journal:
Journal of Cell Biology (2018) doi: 10.1083/jcb.201709001 


Abstract:

Reactive oxygen species (ROS) modulator 1 (Romo1) is a nuclear-encoded mitochondrial inner membrane protein known to regulate mitochondrial ROS production and to act as an essential redox sensor in mitochondrial dynamics. Although its physiological roles have been studied for a decade, the biophysical mechanisms that explain these activities of Romo1 are unclear. In this study, we report that Romo1 is a unique mitochondrial ion channel that differs from currently identified eukaryotic ion channels. Romo1 is a highly conserved protein with structural features of class II viroporins, which are virus-encoded nonselective cation channels. Indeed, Romo1 forms a nonselective cation channel with its amphipathic helical transmembrane domain necessary for pore-forming activity. Notably, channel activity was specifically inhibited by Fe2+ ions, an essential transition metal ion in ROS metabolism. Using structural bioinformatics, we designed an experimental data-guided structural model of Romo1 with a rational hexameric structure. We propose that Romo1 establishes a new category of viroporin-like nonselective cation channel in eukaryotes.


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