High‐throughput screening identifies suppressors of mitochondrial fragmentation in OPA1 fibroblasts

Abstract Mutations in OPA1 cause autosomal dominant optic atrophy (DOA) as well as DOA+, a phenotype characterized by more severe neurological deficits. OPA1 deficiency causes mitochondrial fragmentation and also disrupts cristae, respiration, mitochondrial DNA (mtDNA) maintenance, and cell viabilit...

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Main Authors: Emma Cretin, Priscilla Lopes, Elodie Vimont, Takashi Tatsuta, Thomas Langer, Anastasia Gazi, Martin Sachse, Patrick Yu‐Wai‐Man, Pascal Reynier, Timothy Wai
Format: Article
Language:English
Published: Springer Nature 2021-05-01
Series:EMBO Molecular Medicine
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Online Access:https://doi.org/10.15252/emmm.202013579
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author Emma Cretin
Priscilla Lopes
Elodie Vimont
Takashi Tatsuta
Thomas Langer
Anastasia Gazi
Martin Sachse
Patrick Yu‐Wai‐Man
Pascal Reynier
Timothy Wai
author_facet Emma Cretin
Priscilla Lopes
Elodie Vimont
Takashi Tatsuta
Thomas Langer
Anastasia Gazi
Martin Sachse
Patrick Yu‐Wai‐Man
Pascal Reynier
Timothy Wai
author_sort Emma Cretin
collection DOAJ
description Abstract Mutations in OPA1 cause autosomal dominant optic atrophy (DOA) as well as DOA+, a phenotype characterized by more severe neurological deficits. OPA1 deficiency causes mitochondrial fragmentation and also disrupts cristae, respiration, mitochondrial DNA (mtDNA) maintenance, and cell viability. It has not yet been established whether phenotypic severity can be modulated by genetic modifiers of OPA1. We screened the entire known mitochondrial proteome (1,531 genes) to identify genes that control mitochondrial morphology using a first‐in‐kind imaging pipeline. We identified 145 known and novel candidate genes whose depletion promoted elongation or fragmentation of the mitochondrial network in control fibroblasts and 91 in DOA+ patient fibroblasts that prevented mitochondrial fragmentation, including phosphatidyl glycerophosphate synthase (PGS1). PGS1 depletion reduces CL content in mitochondria and rebalances mitochondrial dynamics in OPA1‐deficient fibroblasts by inhibiting mitochondrial fission, which improves defective respiration, but does not rescue mtDNA depletion, cristae dysmorphology, or apoptotic sensitivity. Our data reveal that the multifaceted roles of OPA1 in mitochondria can be functionally uncoupled by modulating mitochondrial lipid metabolism, providing novel insights into the cellular relevance of mitochondrial fragmentation.
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spelling doaj-art-0f7ab26593fd4ea9a7b36b1989bf8ee62025-08-20T04:03:06ZengSpringer NatureEMBO Molecular Medicine1757-46761757-46842021-05-0113612910.15252/emmm.202013579High‐throughput screening identifies suppressors of mitochondrial fragmentation in OPA1 fibroblastsEmma Cretin0Priscilla Lopes1Elodie Vimont2Takashi Tatsuta3Thomas Langer4Anastasia Gazi5Martin Sachse6Patrick Yu‐Wai‐Man7Pascal Reynier8Timothy Wai9Mitochondrial Biology Group, Institut Pasteur, CNRS UMR 3691Mitochondrial Biology Group, Institut Pasteur, CNRS UMR 3691Mitochondrial Biology Group, Institut Pasteur, CNRS UMR 3691Max‐Planck‐Institute for Biology of AgeingMax‐Planck‐Institute for Biology of AgeingUTechS Ultrastructural Bio Imaging, Institut PasteurUTechS Ultrastructural Bio Imaging, Institut PasteurCambridge Centre for Brain Repair and MRC Mitochondrial Biology Unit, Department of Clinical Neurosciences, University of CambridgeLaboratoire de Biochimie et biologie moléculaire, Centre Hospitalier UniversitaireMitochondrial Biology Group, Institut Pasteur, CNRS UMR 3691Abstract Mutations in OPA1 cause autosomal dominant optic atrophy (DOA) as well as DOA+, a phenotype characterized by more severe neurological deficits. OPA1 deficiency causes mitochondrial fragmentation and also disrupts cristae, respiration, mitochondrial DNA (mtDNA) maintenance, and cell viability. It has not yet been established whether phenotypic severity can be modulated by genetic modifiers of OPA1. We screened the entire known mitochondrial proteome (1,531 genes) to identify genes that control mitochondrial morphology using a first‐in‐kind imaging pipeline. We identified 145 known and novel candidate genes whose depletion promoted elongation or fragmentation of the mitochondrial network in control fibroblasts and 91 in DOA+ patient fibroblasts that prevented mitochondrial fragmentation, including phosphatidyl glycerophosphate synthase (PGS1). PGS1 depletion reduces CL content in mitochondria and rebalances mitochondrial dynamics in OPA1‐deficient fibroblasts by inhibiting mitochondrial fission, which improves defective respiration, but does not rescue mtDNA depletion, cristae dysmorphology, or apoptotic sensitivity. Our data reveal that the multifaceted roles of OPA1 in mitochondria can be functionally uncoupled by modulating mitochondrial lipid metabolism, providing novel insights into the cellular relevance of mitochondrial fragmentation.https://doi.org/10.15252/emmm.202013579genetic modifiershigh‐throughput screeningmitochondrial dynamicsOPA1phospholipid metabolism
spellingShingle Emma Cretin
Priscilla Lopes
Elodie Vimont
Takashi Tatsuta
Thomas Langer
Anastasia Gazi
Martin Sachse
Patrick Yu‐Wai‐Man
Pascal Reynier
Timothy Wai
High‐throughput screening identifies suppressors of mitochondrial fragmentation in OPA1 fibroblasts
EMBO Molecular Medicine
genetic modifiers
high‐throughput screening
mitochondrial dynamics
OPA1
phospholipid metabolism
title High‐throughput screening identifies suppressors of mitochondrial fragmentation in OPA1 fibroblasts
title_full High‐throughput screening identifies suppressors of mitochondrial fragmentation in OPA1 fibroblasts
title_fullStr High‐throughput screening identifies suppressors of mitochondrial fragmentation in OPA1 fibroblasts
title_full_unstemmed High‐throughput screening identifies suppressors of mitochondrial fragmentation in OPA1 fibroblasts
title_short High‐throughput screening identifies suppressors of mitochondrial fragmentation in OPA1 fibroblasts
title_sort high throughput screening identifies suppressors of mitochondrial fragmentation in opa1 fibroblasts
topic genetic modifiers
high‐throughput screening
mitochondrial dynamics
OPA1
phospholipid metabolism
url https://doi.org/10.15252/emmm.202013579
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