The heptad repeat domain 1 of Mitofusin has membrane destabilization function in mitochondrial fusion.

ABSTRACT: Mitochondria are double-membrane-bound organelles that constantly change shape through membrane fusion and fission. Outer mitochondrial membrane fusion is controlled by Mitofusin, whose molecular architecture consists of an N-terminal GTPase domain, a first heptad repeat domain (HR1), two transmembrane domains, and a second heptad repeat domain (HR2). The mode of action of Mitofusin and the specific roles played by each of these functional domains in mitochondrial fusion are not fully understood. Here, using a combination of in situ and in vitro fusion assays, we show that HR1 induces membrane fusion and possesses a conserved amphipathic helix that folds upon interaction with the lipid bilayer surface. Our results strongly suggest that HR1 facilitates membrane fusion by desta

SUBMITTER: Daste F 

PROVIDER: S-EPMC5989784 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature