Mitochondrial Membrane Dynamics-Functional Positioning of OPA1

The maintenance of mitochondrial energetics requires the proper regulation of mitochondrial morphology, and vice versa. Mitochondrial dynamins control mitochondrial morphology by mediating fission and fusion. One of them, optic atrophy 1 (OPA1), is the mitochondrial inner membrane remodeling protein...

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Bibliographic Details
Published in:Antioxidants 2018-12, Vol.7 (12), p.186
Main Authors: Lee, Hakjoo, Yoon, Yisang
Format: Article
Language:English
Subjects:
Adenosine triphosphate
Alternative splicing
Atrophy
cardiolipin
Cristae
fission
fusion
Lipids
Membrane fusion
Membrane proteins
Membranes
Metabolites
Mitochondria
mitochondrial dynamics
Morphology
OPA1
Optic atrophy
Overlapping activity with m-AAA protease 1 (OMA1)
Oxidative phosphorylation (OXPHOS)
Phosphorylation
Post-translation
Proteins
Proteolysis
Roles
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Summary:The maintenance of mitochondrial energetics requires the proper regulation of mitochondrial morphology, and vice versa. Mitochondrial dynamins control mitochondrial morphology by mediating fission and fusion. One of them, optic atrophy 1 (OPA1), is the mitochondrial inner membrane remodeling protein. OPA1 has a dual role in maintaining mitochondrial morphology and energetics through mediating inner membrane fusion and maintaining the cristae structure. OPA1 is expressed in multiple variant forms through alternative splicing and post-translational proteolytic cleavage, but the functional differences between these variants have not been completely understood. Recent studies generated new information regarding the role of OPA1 cleavage. In this review, we will first provide a brief overview of mitochondrial membrane dynamics by describing fission and fusion that are mediated by mitochondrial dynamins. The second part describes OPA1-mediated fusion and energetic maintenance, the role of OPA1 cleavage, and a new development in OPA1 function, in which we will provide new insight for what OPA1 does and what proteolytic cleavage of OPA1 is for.
ISSN:2076-3921
2076-3921
DOI:10.3390/antiox7120186