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EMBO Rep. 2014 May;15(5):576-85. doi: 10.1002/embr.201338240. Epub 2014 Apr 9.

Membrane depolarization activates the mitochondrial protease OMA1 by stimulating self-cleavage.

Author information

1
College of Life Sciences, Wuhan University, Wuhan, China.

Abstract

Mitochondrial inner membrane fusion depends on the dynamin-related GTPase OPA1 and the function of OPA1 is regulated by proteolytic cleavage. The mitochondrial proteases Yme1L and OMA1 cleave OPA1 at S2 and S1 sites, respectively. Here, we show that OMA1 is cleaved to a short form (S-OMA1) by itself upon mitochondrial membrane depolarization; S-OMA1 is degraded quickly but could be stabilized by CCCP treatment or Prohibitin knockdown in cells. In addition, OMA1 processing is positively correlated with OPA1 cleavage at the S1 site and the regulation of mitochondrial morphology. Thus, our results reveal the molecular mechanism for OMA1 activation toward OPA1 processing.

PMID:
24719224
PMCID:
PMC4210089
DOI:
10.1002/embr.201338240
[Indexed for MEDLINE]
Free PMC Article

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