Structural mechanism of mitochondrial membrane remodelling by human OPA1.

ABSTRACT: Distinct morphologies of the mitochondrial network support divergent metabolic and regulatory processes that determine cell function and fate^1-3. The mechanochemical GTPase optic atrophy 1 (OPA1) influences the architecture of cristae and catalyses the fusion of the mitochondrial inner membrane^4,5. Despite its fundamental importance, the molecular mechanisms by which OPA1 modulates mitochondrial morphology are unclear. Here, using a combination of cellular and structural analyses, we illuminate the molecular mechanisms that are key to OPA1-dependent membrane remodelling and fusion. Human OPA1 embeds itself into cardiolipin-containing membranes through a lipid-binding paddle domain. A conserved loop within the paddle domain inserts deeply into the bilayer, further stab

SUBMITTER: von der Malsburg A 

PROVIDER: S-EPMC10875962 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature