Transient contraction of mitochondria induces depolarization through the inner membrane dynamin OPA1 protein.

ABSTRACT: Dynamin-related membrane remodeling proteins regulate mitochondrial morphology by mediating fission and fusion. Although mitochondrial morphology is considered an important factor in maintaining mitochondrial function, a direct mechanistic link between mitochondrial morphology and function has not been defined. We report here a previously unrecognized cellular process of transient contraction of the mitochondrial matrix. Importantly, we found that this transient morphological contraction of mitochondria is accompanied by a reversible loss or decrease of inner membrane potential. Fission deficiency greatly amplified this phenomenon, which functionally exhibited an increase of inner membrane proton leak. We found that electron transport activity is necessary for the morphological contraction

SUBMITTER: Lee H 

PROVIDER: S-EPMC4002095 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature