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Two Forms of Opa1 Cooperate to Complete Fusion of the Mitochondrial Inner-Membrane

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Two Forms of Opa1 Cooperate to Complete Fusion of the Mitochondrial Inner-Membrane

Yifan Ge et al. Elife.

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.

Keywords: fusion; in vitro reconstitution; membranes; mitochondria; molecular biophysics; none; structural biology.

Conflict of interest statement

YG, XS, SB, JM, AS, LC No competing interests declared

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