Two forms of Opa1 cooperate to complete fusion of the mitochondrial inner-membrane
- Massachusetts General Hospital, United States
- University of Akron, United States
Abstract
Mitochondrial membrane dynamics is a cellular rheostat that relates metabolic function and organelle morphology. Using an in vitro reconstitution system, we describe a mechanism for how mitochondrial inner-membrane fusion is regulated by the ratio of two forms of Opa1. We found that the long-form of Opa1 (l-Opa1) is sufficient for membrane docking, hemifusion and low levels of content release. However, stoichiometric levels of the processed, short form of Opa1 (s-Opa1) work together with l-Opa1 to mediate efficient and fast membrane pore opening. Additionally, we found that excess levels of s-Opa1 inhibit fusion activity, as seen under conditions of altered proteostasis. These observations describe a mechanism for gating membrane fusion.
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All data generated or analyses during this study are include in the manuscript and supporting files.
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Funding
Charles H Hood Foundation (Child Health Research Award)
- Luke H Chao
Charles H Hood Foundation (Child Health Research Award)
- Yifan Ge
National Science Foundation (CHE-1753060)
- Xiaojun Shi
- Adam W Smith
The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.
Copyright
© 2020, Ge et al.
This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
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Two forms of Opa1 cooperate to complete fusion of the mitochondrial inner-membrane
eLife 9:e50973.
https://doi.org/10.7554/eLife.50973
