Ontology highlight
ABSTRACT:
SUBMITTER: Ehses S
PROVIDER: S-EPMC2806285 | biostudies-literature | 2009 Dec
REPOSITORIES: biostudies-literature
Ehses Sarah S Raschke Ines I Mancuso Giuseppe G Bernacchia Andrea A Geimer Stefan S Tondera Daniel D Martinou Jean-Claude JC Westermann Benedikt B Rugarli Elena I EI Langer Thomas T
The Journal of cell biology 20091201 7
Mitochondrial fusion depends on the dynamin-like guanosine triphosphatase OPA1, whose activity is controlled by proteolytic cleavage. Dysfunction of mitochondria induces OPA1 processing and results in mitochondrial fragmentation, allowing the selective removal of damaged mitochondria. In this study, we demonstrate that two classes of metallopeptidases regulate OPA1 cleavage in the mitochondrial inner membrane: isoenzymes of the adenosine triphosphate (ATP)-dependent matrix AAA (ATPase associated ...[more]