scholarly journals Mitochondrial permeability transition involves dissociation of F 1 F O ATP synthase dimers and C‐ring conformation

EMBO Reports ◽  
2017 ◽  
Vol 18 (7) ◽  
pp. 1077-1089 ◽  
Author(s):  
Massimo Bonora ◽  
Claudia Morganti ◽  
Giampaolo Morciano ◽  
Gaia Pedriali ◽  
Magdalena Lebiedzinska‐Arciszewska ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Mitochondrial Permeability Transition ◽  
Permeability Transition ◽  
Ring Conformation ◽  
Mitochondrial Permeability

scholarly journals Arginine 107 of yeast ATP synthase subunit g mediates sensitivity of the mitochondrial permeability transition to phenylglyoxal

2018 ◽  
Vol 293 (38) ◽  
pp. 14632-14645 ◽  
Author(s):  
Lishu Guo ◽  
Michela Carraro ◽  
Geppo Sartori ◽  
Giovanni Minervini ◽  
Ove Eriksson ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Mitochondrial Permeability Transition ◽  
Permeability Transition ◽  
Mitochondrial Permeability

scholarly journals FOF1-ATP Synthase Dimers and The Mitochondrial Permeability Transition Pore from Yeast to Mammals

2014 ◽  
Vol 106 (2) ◽  
pp. 3a
Author(s):  
Paolo Bernardi ◽  
Valentina Giorgio ◽  
Michela Carraro ◽  
Sophia von Stockum ◽  
Victoria Burchell ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Mitochondrial Permeability Transition Pore ◽  
Mitochondrial Permeability Transition ◽  
Permeability Transition Pore ◽  
Permeability Transition ◽  
Mitochondrial Permeability ◽  
Fof1 Atp Synthase

scholarly journals Molecular mechanisms of cell death: central implication of ATP synthase in mitochondrial permeability transition

Oncogene ◽  
2014 ◽  
Vol 34 (12) ◽  
pp. 1475-1486 ◽  
Author(s):  
M Bonora ◽  
M R Wieckowski ◽  
C Chinopoulos ◽  
O Kepp ◽  
G Kroemer ◽  
...  
Keyword(s):  
Cell Death ◽  
Atp Synthase ◽  
Molecular Mechanisms ◽  
Mitochondrial Permeability Transition ◽  
Permeability Transition ◽  
Mitochondrial Permeability

scholarly journals The mitochondrial permeability transition pore activates the mitochondrial unfolded protein response and promotes aging

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Suzanne Angeli ◽  
Anna Foulger ◽  
Manish Chamoli ◽  
Tanuja Harshani Peiris ◽  
Akos Gerencser ◽  
...  
Keyword(s):  
Unfolded Protein Response ◽  
Atp Synthase ◽  
Mitochondrial Permeability Transition Pore ◽  
Mitochondrial Permeability Transition ◽  
Permeability Transition Pore ◽  
Permeability Transition ◽  
Mitochondrial Permeability ◽  
Unfolded Protein ◽  
Protein Response ◽  
Mitochondrial Unfolded Protein Response

Mitochondrial activity determines aging rate and the onset of chronic diseases. The mitochondrial permeability transition pore (mPTP) is a pathological pore in the inner mitochondrial membrane thought to be composed of the F-ATP synthase (complex V). OSCP, a subunit of F-ATP synthase, helps protect against mPTP formation. How the destabilization of OSCP may contribute to aging, however, is unclear. We have found that loss OSCP in the nematode Caenorhabditis elegans initiates the mPTP and shortens lifespan specifically during adulthood, in part via initiation of the mitochondrial unfolded protein response (UPRmt). Pharmacological or genetic inhibition of the mPTP inhibits the UPRmt and restores normal lifespan. Loss of the putative pore-forming component of F-ATP synthase extends adult lifespan, suggesting that the mPTP normally promotes aging. Our findings reveal how an mPTP/UPRmt nexus may contribute to aging and age-related diseases and how inhibition of the UPRmt may be protective under certain conditions.

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