Identification of new OPA1 cleavage site reveals that short isoforms regulate mitochondrial fusion
نویسندگان
چکیده
OPA1 is a dynamin-family GTPase that the central mediator of mitochondrial inner membrane fusion. The Opa1 gene generates both long and short isoforms (l-OPA1 s-OPA1) through proteolytic processing. We identify new s-OPA1 show it functions with l-OPA1 to tune level
منابع مشابه
Proteolytic cleavage of Opa1 stimulates mitochondrial inner membrane fusion and couples fusion to oxidative phosphorylation.
Mitochondrial fusion is essential for maintenance of mitochondrial function. The mitofusin GTPases control mitochondrial outer membrane fusion, whereas the dynamin-related GTPase Opa1 mediates inner membrane fusion. We show that mitochondrial inner membrane fusion is tuned by the level of oxidative phosphorylation (OXPHOS), whereas outer membrane fusion is insensitive. Consequently, cells from ...
متن کاملOPA1 processing controls mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and Yme1L
OPA1, a dynamin-related guanosine triphosphatase mutated in dominant optic atrophy, is required for the fusion of mitochondria. Proteolytic cleavage by the mitochondrial processing peptidase generates long isoforms from eight messenger RNA (mRNA) splice forms, whereas further cleavages at protease sites S1 and S2 generate short forms. Using OPA1-null cells, we developed a cellular system to stu...
متن کاملRegulation of mitochondrial morphology through proteolytic cleavage of OPA1.
The dynamin-like GTPase OPA1, a causal gene product of human dominant optic atrophy, functions in mitochondrial fusion and inner membrane remodeling. It has several splice variants and even a single variant is found as several processed forms, although their functional significance is unknown. In yeast, mitochondrial rhomboid protease regulates mitochondrial function and morphology through prot...
متن کاملRegulation of OPA1 processing and mitochondrial fusion by m-AAA protease isoenzymes and OMA1
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...
متن کاملMitofusins and OPA1 mediate sequential steps in mitochondrial membrane fusion.
Mitochondrial fusion requires the coordinated fusion of the outer and inner membranes. Three large GTPases--OPA1 and the mitofusins Mfn1 and Mfn2--are essential for the fusion of mammalian mitochondria. OPA1 is mutated in dominant optic atrophy, a neurodegenerative disease of the optic nerve. In yeast, the OPA1 ortholog Mgm1 is required for inner membrane fusion in vitro; nevertheless, yeast la...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Molecular Biology of the Cell
سال: 2021
ISSN: ['1059-1524', '1939-4586']
DOI: https://doi.org/10.1091/mbc.e20-09-0605