Romo1 is a mitochondrial nonselective cation channel with viroporin-like characteristics
- Authors
- Lee, Gi Young; You, Deok-gyun; Lee, Hye-Ra; Hwang, Sun Wook; Lee, C. Justin; Do Yoo, Young
- Issue Date
- 6월-2018
- Publisher
- ROCKEFELLER UNIV PRESS
- Citation
- JOURNAL OF CELL BIOLOGY, v.217, no.6, pp.2059 - 2071
- Indexed
- SCIE
SCOPUS
- Journal Title
- JOURNAL OF CELL BIOLOGY
- Volume
- 217
- Number
- 6
- Start Page
- 2059
- End Page
- 2071
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/75063
- DOI
- 10.1083/jcb.201709001
- ISSN
- 0021-9525
- 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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Collections - Graduate School > Department of Biomedical Sciences > 1. Journal Articles
- Graduate School > Department of Medicine > 1. Journal Articles
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