Regulation of OPA1 processing and mitochondrial fusion by m-AAA protease isoenzymes and OMA1
Open Access
- 28 December 2009
- journal article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 187 (7), 1023-1036
- https://doi.org/10.1083/jcb.200906084
Abstract
M-AAA proteases cleave OPA1 to ensure a balance of long and short OPA1 isoforms, whereas cleavage by OMA1 causes an accumulation of the short OPA1 variants. (See also companion paper from Head et al. in this issue.)Keywords
This publication has 39 references indexed in Scilit:
- Autocatalytic Processing of m-AAA Protease Subunits in MitochondriaMolecular Biology of the Cell, 2009
- An Intersubunit Signaling Network Coordinates ATP Hydrolysis by m-AAA ProteasesMolecular Cell, 2009
- SLP-2 is required for stress-induced mitochondrial hyperfusionThe EMBO Journal, 2009
- The genetic interactome of prohibitins: coordinated control of cardiolipin and phosphatidylethanolamine by conserved regulators in mitochondriaThe Journal of cell biology, 2009
- OPA1 Processing Reconstituted in Yeast Depends on the Subunit Composition of them-AAA Protease in MitochondriaMolecular Biology of the Cell, 2007
- Regulation of the mitochondrial dynamin-like protein Opa1 by proteolytic cleavageThe Journal of cell biology, 2007
- OPA1 processing controls mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and Yme1LThe Journal of cell biology, 2007
- m-AAA protease-driven membrane dislocation allows intramembrane cleavage by rhomboid in mitochondriaThe EMBO Journal, 2007
- Regulation of mitochondrial morphology through proteolytic cleavage of OPA1The EMBO Journal, 2006
- Distinct Roles for the AAA ATPases NSF and p97 in the Secretory PathwayMolecular Biology of the Cell, 2004