OPA1-dependent cristae modulation is essential for cellular adaptation to metabolic demand

Cristae, the organized invaginations of the mitochondrial inner membrane, respond structurally to the energetic demands of the cell. The mechanism by which these dynamic changes are regulated and the consequences thereof are largely unknown. Optic atrophy 1 (OPA1) is the mitochondrial GTPase respons...

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Published inThe EMBO journal Vol. 33; no. 22; pp. 2676 - 2691
Main Authors Patten, David A, Wong, Jacob, Khacho, Mireille, Soubannier, Vincent, Mailloux, Ryan J, Pilon-Larose, Karine, MacLaurin, Jason G, Park, David S, McBride, Heidi M, Trinkle-Mulcahy, Laura, Harper, Mary-Ellen, Germain, Marc, Slack, Ruth S
Format Journal Article
LanguageEnglish
Published London Blackwell Publishing Ltd 18.11.2014
Nature Publishing Group UK
BlackWell Publishing Ltd
Subjects
Adaptation
Animals
Anion Transport Proteins - genetics
Anion Transport Proteins - metabolism
ATP synthase
Cellular biology
cristae
EMBO20
EMBO21
GTP Phosphohydrolases - genetics
GTP Phosphohydrolases - metabolism
HeLa Cells
Humans
Metabolism
Mice
mitochondria
Mitochondria - enzymology
Mitochondria - ultrastructure
Mitochondrial DNA
Mitochondrial Dynamics - physiology
Mitochondrial Membranes - enzymology
Mitochondrial Membranes - ultrastructure
Mitochondrial Proteins - genetics
Mitochondrial Proteins - metabolism
OPA1
Oxygen Consumption - physiology
Protein Multimerization - physiology
SLC25A
cristae
ATP synthase
OPA1
SLC25A
mitochondria
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Abstract Cristae, the organized invaginations of the mitochondrial inner membrane, respond structurally to the energetic demands of the cell. The mechanism by which these dynamic changes are regulated and the consequences thereof are largely unknown. Optic atrophy 1 (OPA1) is the mitochondrial GTPase responsible for inner membrane fusion and maintenance of cristae structure. Here, we report that OPA1 responds dynamically to changes in energetic conditions to regulate cristae structure. This cristae regulation is independent of OPA1's role in mitochondrial fusion, since an OPA1 mutant that can still oligomerize but has no fusion activity was able to maintain cristae structure. Importantly, OPA1 was required for resistance to starvation‐induced cell death, for mitochondrial respiration, for growth in galactose media and for maintenance of ATP synthase assembly, independently of its fusion activity. We identified mitochondrial solute carriers (SLC25A) as OPA1 interactors and show that their pharmacological and genetic blockade inhibited OPA1 oligomerization and function. Thus, we propose a novel way in which OPA1 senses energy substrate availability, which modulates its function in the regulation of mitochondrial architecture in a SLC25A protein‐dependent manner. Synopsis Metabolic stress causes inner mitochondrial membrane fusion protein OPA1 to interact with solute carriers and to oligomerize to regulate cristae shape, thereby maintaining mitochondrial activity under low energy availability. OPA1 dynamically responds to energy substrate availability, mediating changes in cristae ultrastructure. OPA1‐mediated cristae changes are required for cell adaptation to metabolic demand, independently of OPA1 fusion activity. SLC25A proteins interact with OPA1 and modulate its function. OGC (SLC25A11) affects how OPA1 oligomerizes in response to starvation, mediating changes in mitochondrial function. Graphical Abstract Metabolic stress causes inner mitochondrial membrane fusion protein OPA1 to interact with solute carriers and to oligomerize to regulate cristae shape, thereby maintaining mitochondrial activity under low energy availability.
AbstractList Abstract Cristae, the organized invaginations of the mitochondrial inner membrane, respond structurally to the energetic demands of the cell. The mechanism by which these dynamic changes are regulated and the consequences thereof are largely unknown. Optic atrophy 1 ( OPA 1) is the mitochondrial GTP ase responsible for inner membrane fusion and maintenance of cristae structure. Here, we report that OPA 1 responds dynamically to changes in energetic conditions to regulate cristae structure. This cristae regulation is independent of OPA 1's role in mitochondrial fusion, since an OPA 1 mutant that can still oligomerize but has no fusion activity was able to maintain cristae structure. Importantly, OPA 1 was required for resistance to starvation‐induced cell death, for mitochondrial respiration, for growth in galactose media and for maintenance of ATP synthase assembly, independently of its fusion activity. We identified mitochondrial solute carriers ( SLC 25A) as OPA 1 interactors and show that their pharmacological and genetic blockade inhibited OPA 1 oligomerization and function. Thus, we propose a novel way in which OPA 1 senses energy substrate availability, which modulates its function in the regulation of mitochondrial architecture in a SLC 25A protein‐dependent manner. Synopsis image Metabolic stress causes inner mitochondrial membrane fusion protein OPA 1 to interact with solute carriers and to oligomerize to regulate cristae shape, thereby maintaining mitochondrial activity under low energy availability. OPA 1 dynamically responds to energy substrate availability, mediating changes in cristae ultrastructure. OPA 1‐mediated cristae changes are required for cell adaptation to metabolic demand, independently of OPA 1 fusion activity. SLC 25A proteins interact with OPA 1 and modulate its function. OGC ( SLC 25A11) affects how OPA 1 oligomerizes in response to starvation, mediating changes in mitochondrial function.
Cristae, the organized invaginations of the mitochondrial inner membrane, respond structurally to the energetic demands of the cell. The mechanism by which these dynamic changes are regulated and the consequences thereof are largely unknown. Optic atrophy 1 (OPA1) is the mitochondrial GTPase responsible for inner membrane fusion and maintenance of cristae structure. Here, we report that OPA1 responds dynamically to changes in energetic conditions to regulate cristae structure. This cristae regulation is independent of OPA1's role in mitochondrial fusion, since an OPA1 mutant that can still oligomerize but has no fusion activity was able to maintain cristae structure. Importantly, OPA1 was required for resistance to starvation‐induced cell death, for mitochondrial respiration, for growth in galactose media and for maintenance of ATP synthase assembly, independently of its fusion activity. We identified mitochondrial solute carriers (SLC25A) as OPA1 interactors and show that their pharmacological and genetic blockade inhibited OPA1 oligomerization and function. Thus, we propose a novel way in which OPA1 senses energy substrate availability, which modulates its function in the regulation of mitochondrial architecture in a SLC25A protein‐dependent manner. Synopsis Metabolic stress causes inner mitochondrial membrane fusion protein OPA1 to interact with solute carriers and to oligomerize to regulate cristae shape, thereby maintaining mitochondrial activity under low energy availability. OPA1 dynamically responds to energy substrate availability, mediating changes in cristae ultrastructure. OPA1‐mediated cristae changes are required for cell adaptation to metabolic demand, independently of OPA1 fusion activity. SLC25A proteins interact with OPA1 and modulate its function. OGC (SLC25A11) affects how OPA1 oligomerizes in response to starvation, mediating changes in mitochondrial function. Metabolic stress causes inner mitochondrial membrane fusion protein OPA1 to interact with solute carriers and to oligomerize to regulate cristae shape, thereby maintaining mitochondrial activity under low energy availability.
Cristae, the organized invaginations of the mitochondrial inner membrane, respond structurally to the energetic demands of the cell. The mechanism by which these dynamic changes are regulated and the consequences thereof are largely unknown. Optic atrophy 1 (OPA1) is the mitochondrial GTPase responsible for inner membrane fusion and maintenance of cristae structure. Here, we report that OPA1 responds dynamically to changes in energetic conditions to regulate cristae structure. This cristae regulation is independent of OPA1's role in mitochondrial fusion, since an OPA1 mutant that can still oligomerize but has no fusion activity was able to maintain cristae structure. Importantly, OPA1 was required for resistance to starvation-induced cell death, for mitochondrial respiration, for growth in galactose media and for maintenance of ATP synthase assembly, independently of its fusion activity. We identified mitochondrial solute carriers (SLC25A) as OPA1 interactors and show that their pharmacological and genetic blockade inhibited OPA1 oligomerization and function. Thus, we propose a novel way in which OPA1 senses energy substrate availability, which modulates its function in the regulation of mitochondrial architecture in a SLC25A protein-dependent manner.
Cristae, the organized invaginations of the mitochondrial inner membrane, respond structurally to the energetic demands of the cell. The mechanism by which these dynamic changes are regulated and the consequences thereof are largely unknown. Optic atrophy 1 (OPA1) is the mitochondrial GTPase responsible for inner membrane fusion and maintenance of cristae structure. Here, we report that OPA1 responds dynamically to changes in energetic conditions to regulate cristae structure. This cristae regulation is independent of OPA1's role in mitochondrial fusion, since an OPA1 mutant that can still oligomerize but has no fusion activity was able to maintain cristae structure. Importantly, OPA1 was required for resistance to starvation-induced cell death, for mitochondrial respiration, for growth in galactose media and for maintenance of ATP synthase assembly, independently of its fusion activity. We identified mitochondrial solute carriers (SLC25A) as OPA1 interactors and show that their pharmacological and genetic blockade inhibited OPA1 oligomerization and function. Thus, we propose a novel way in which OPA1 senses energy substrate availability, which modulates its function in the regulation of mitochondrial architecture in a SLC25A protein-dependent manner. Synopsis Metabolic stress causes inner mitochondrial membrane fusion protein OPA1 to interact with solute carriers and to oligomerize to regulate cristae shape, thereby maintaining mitochondrial activity under low energy availability. OPA1 dynamically responds to energy substrate availability, mediating changes in cristae ultrastructure. OPA1-mediated cristae changes are required for cell adaptation to metabolic demand, independently of OPA1 fusion activity. SLC25A proteins interact with OPA1 and modulate its function. OGC (SLC25A11) affects how OPA1 oligomerizes in response to starvation, mediating changes in mitochondrial function.
Cristae, the organized invaginations of the mitochondrial inner membrane, respond structurally to the energetic demands of the cell. The mechanism by which these dynamic changes are regulated and the consequences thereof are largely unknown. Optic atrophy 1 (OPA1) is the mitochondrial GTPase responsible for inner membrane fusion and maintenance of cristae structure. Here, we report that OPA1 responds dynamically to changes in energetic conditions to regulate cristae structure. This cristae regulation is independent of OPA1's role in mitochondrial fusion, since an OPA1 mutant that can still oligomerize but has no fusion activity was able to maintain cristae structure. Importantly, OPA1 was required for resistance to starvation‐induced cell death, for mitochondrial respiration, for growth in galactose media and for maintenance of ATP synthase assembly, independently of its fusion activity. We identified mitochondrial solute carriers (SLC25A) as OPA1 interactors and show that their pharmacological and genetic blockade inhibited OPA1 oligomerization and function. Thus, we propose a novel way in which OPA1 senses energy substrate availability, which modulates its function in the regulation of mitochondrial architecture in a SLC25A protein‐dependent manner. Synopsis Metabolic stress causes inner mitochondrial membrane fusion protein OPA1 to interact with solute carriers and to oligomerize to regulate cristae shape, thereby maintaining mitochondrial activity under low energy availability. OPA1 dynamically responds to energy substrate availability, mediating changes in cristae ultrastructure. OPA1‐mediated cristae changes are required for cell adaptation to metabolic demand, independently of OPA1 fusion activity. SLC25A proteins interact with OPA1 and modulate its function. OGC (SLC25A11) affects how OPA1 oligomerizes in response to starvation, mediating changes in mitochondrial function. Graphical Abstract Metabolic stress causes inner mitochondrial membrane fusion protein OPA1 to interact with solute carriers and to oligomerize to regulate cristae shape, thereby maintaining mitochondrial activity under low energy availability.
Author McBride, Heidi M
Trinkle‐Mulcahy, Laura
Khacho, Mireille
Wong, Jacob
Slack, Ruth S
Pilon‐Larose, Karine
Patten, David A
Mailloux, Ryan J
MacLaurin, Jason G
Soubannier, Vincent
Park, David S
Germain, Marc
Harper, Mary‐Ellen
Author_xml – sequence: 1
  givenname: David A
  surname: Patten
  fullname: Patten, David A
  organization: Department of Cellular & Molecular Medicine, University of Ottawa, ON, Ottawa, Canada
– sequence: 2
  givenname: Jacob
  surname: Wong
  fullname: Wong, Jacob
  organization: Department of Cellular & Molecular Medicine, University of Ottawa, ON, Ottawa, Canada
– sequence: 3
  givenname: Mireille
  surname: Khacho
  fullname: Khacho, Mireille
  organization: Department of Cellular & Molecular Medicine, University of Ottawa, ON, Ottawa, Canada
– sequence: 4
  givenname: Vincent
  surname: Soubannier
  fullname: Soubannier, Vincent
  organization: Montreal Neurological Institute, McGill University, QC, Montreal, Canada
– sequence: 5
  givenname: Ryan J
  surname: Mailloux
  fullname: Mailloux, Ryan J
  organization: Department of Biochemistry, Microbiology & Immunology, University of Ottawa, ON, Ottawa, Canada
– sequence: 6
  givenname: Karine
  surname: Pilon-Larose
  fullname: Pilon-Larose, Karine
  organization: Department of Cellular & Molecular Medicine, University of Ottawa, ON, Ottawa, Canada
– sequence: 7
  givenname: Jason G
  surname: MacLaurin
  fullname: MacLaurin, Jason G
  organization: Department of Cellular & Molecular Medicine, University of Ottawa, ON, Ottawa, Canada
– sequence: 8
  givenname: David S
  surname: Park
  fullname: Park, David S
  organization: Department of Cellular & Molecular Medicine, University of Ottawa, ON, Ottawa, Canada
– sequence: 9
  givenname: Heidi M
  surname: McBride
  fullname: McBride, Heidi M
  organization: Montreal Neurological Institute, McGill University, QC, Montreal, Canada
– sequence: 10
  givenname: Laura
  surname: Trinkle-Mulcahy
  fullname: Trinkle-Mulcahy, Laura
  organization: Department of Cellular & Molecular Medicine, University of Ottawa, ON, Ottawa, Canada
– sequence: 11
  givenname: Mary-Ellen
  surname: Harper
  fullname: Harper, Mary-Ellen
  organization: Department of Biochemistry, Microbiology & Immunology, University of Ottawa, ON, Ottawa, Canada
– sequence: 12
  givenname: Marc
  surname: Germain
  fullname: Germain, Marc
  email: Corresponding author. Tel: +1 613 562 5800; , rslack@uottawa.ca, Corresponding author. Tel: +1 819 376 5011 x3330; , marc.germain1@uqtr.ca
  organization: Département de Biologie Médicale, Université du Québec à Trois-Rivières, QC, Trois-Rivières, Canada
– sequence: 13
  givenname: Ruth S
  surname: Slack
  fullname: Slack, Ruth S
  email: Corresponding author. Tel: +1 613 562 5800; , rslack@uottawa.ca, Corresponding author. Tel: +1 819 376 5011 x3330; , marc.germain1@uqtr.ca
  organization: Department of Cellular & Molecular Medicine, University of Ottawa, ON, Ottawa, Canada
BackLink https://www.ncbi.nlm.nih.gov/pubmed/25298396$$D View this record in MEDLINE/PubMed
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Keywords cristae
ATP synthase
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mitochondria
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Snippet Cristae, the organized invaginations of the mitochondrial inner membrane, respond structurally to the energetic demands of the cell. The mechanism by which...
Abstract Cristae, the organized invaginations of the mitochondrial inner membrane, respond structurally to the energetic demands of the cell. The mechanism by...
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StartPage 2676
SubjectTerms Adaptation
Animals
Anion Transport Proteins - genetics
Anion Transport Proteins - metabolism
ATP synthase
Cellular biology
cristae
EMBO20
EMBO21
GTP Phosphohydrolases - genetics
GTP Phosphohydrolases - metabolism
HeLa Cells
Humans
Metabolism
Mice
mitochondria
Mitochondria - enzymology
Mitochondria - ultrastructure
Mitochondrial DNA
Mitochondrial Dynamics - physiology
Mitochondrial Membranes - enzymology
Mitochondrial Membranes - ultrastructure
Mitochondrial Proteins - genetics
Mitochondrial Proteins - metabolism
OPA1
Oxygen Consumption - physiology
Protein Multimerization - physiology
SLC25A
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Title OPA1-dependent cristae modulation is essential for cellular adaptation to metabolic demand
URI https://api.istex.fr/ark:/67375/WNG-DXH929C2-6/fulltext.pdf
https://link.springer.com/article/10.15252/embj.201488349
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Volume 33
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