| Literature DB >> 28636943 |
Valentina Del Dotto1, Prashant Mishra2, Sara Vidoni3, Mario Fogazza4, Alessandra Maresca5, Leonardo Caporali5, J Michael McCaffery6, Martina Cappelletti4, Enrico Baruffini7, Guy Lenaers8, David Chan2, Michela Rugolo9, Valerio Carelli10, Claudia Zanna11.
Abstract
OPA1 is a GTPase that controls mitochondrial fusion, cristae integrity, and mtDNA maintenance. In humans, eight isoforms are expressed as combinations of long and short forms, but it is unclear whether OPA1 functions are associated with specific isoforms and/or domains. To address this, we expressed each of the eight isoforms or different constructs of isoform 1 in Opa1-/- MEFs. We observed that any isoform could restore cristae structure, mtDNA abundance, and energetic efficiency independently of mitochondrial network morphology. Long forms supported mitochondrial fusion; short forms were better able to restore energetic efficiency. The complete rescue of mitochondrial network morphology required a balance of long and short forms of at least two isoforms, as shown by combinatorial isoform silencing and co-expression experiments. Thus, multiple OPA1 isoforms are required for mitochondrial dynamics, while any single isoform can support all other functions. These findings will be useful in designing gene therapies for patients with OPA1 haploinsufficiency.Entities:
Keywords: OPA1 isoforms; OPA1 long-short form balance; dominant optic atrophy; mitochondrial network dynamics; mtDNA
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Year: 2017 PMID: 28636943 DOI: 10.1016/j.celrep.2017.05.073
Source DB: PubMed Journal: Cell Rep Impact factor: 9.423