Journal
JOURNAL OF CELL SCIENCE
Volume 131, Issue 7, Pages -Publisher
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.213546
Keywords
OMA1; OPA1; m-AAA complex; Mitochondrial dynamics
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Funding
- Italian Telethon Foundation [GGP12235]
- Fondazione Cariplo [2012_0646]
- Ministero Italiano dell'Universita e della Ricerca (MIUR) [20108WT59Y_001]
- Associazione Italiana Sindromi Atassiche (AISA)
- National Ataxia Foundation (NAF)
- Ministero Italiano della Salute (Giovani Ricercatori) [GR-2011-02351638]
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The proteolytic processing of dynamin-like GTPase OPA1, mediated by the activity of both YME1L1 [intermembrane (i)-AAA protease complex] and OMA1, is a crucial step in the regulation of mitochondrial dynamics. OMA1 is a zinc metallopeptidase of the inner mitochondrial membrane that undergoes pre-activating proteolytic and auto-proteolytic cleavage after mitochondrial import. Here, we identify AFG3L2 [matrix (m)-AAA complex] as the major protease mediating this event, which acts by maturing the 60 kDa pre-pro-OMA1 to the 40 kDa pro-OMA1 form by severing the N-terminal portion without recognizing a specific consensus sequence. Therefore, m-AAA and i-AAA complexes coordinately regulate OMA1 processing and turnover, and consequently control which OPA1 isoforms are present, thus adding new information on the molecular mechanisms of mitochondrial dynamics and neurodegenerative diseases affected by these phenomena.
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