Abstract
The identity of the mitochondrial permeability transition (mPT) pore, a megachannel embedded in the inner membrane opened by Ca2+, is fiercely debated. Unraveling the components structuring this pore is critical for combating diseases as diverse as neurodegeneration, cancer, autoimmunity, and myopathies in which this phenomenon is implicated. Current consensus is that the pore is formed within, or in-between F0F1 ATP synthase dimers, but not through their c-subunit ring. Two recent studies in this issue of EMBO Reports throw more light on these aspects, one by Giorgio et al showing that the β subunit of the ATP synthase harbors a Ca2+-binding site responsible for triggering mPT, and the other by Bonora et al demonstrating that permeability transition requires dissociation of F0F1 ATP synthase dimers, albeit in a manner involving the c-subunit ring.
| Original language | English |
|---|---|
| Journal | EMBO Reports |
| DOIs | |
| Publication status | Accepted/In press - jan. 1 2017 |
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ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Genetics
Cite this
ATP synthase complex and the mitochondrial permeability transition pore : Poles of attraction. / Chinopoulos, C.
In: EMBO Reports, 01.01.2017.Research output: Article
}
TY - JOUR
T1 - ATP synthase complex and the mitochondrial permeability transition pore
T2 - Poles of attraction
AU - Chinopoulos, C.
PY - 2017/1/1
Y1 - 2017/1/1
N2 - The identity of the mitochondrial permeability transition (mPT) pore, a megachannel embedded in the inner membrane opened by Ca2+, is fiercely debated. Unraveling the components structuring this pore is critical for combating diseases as diverse as neurodegeneration, cancer, autoimmunity, and myopathies in which this phenomenon is implicated. Current consensus is that the pore is formed within, or in-between F0F1 ATP synthase dimers, but not through their c-subunit ring. Two recent studies in this issue of EMBO Reports throw more light on these aspects, one by Giorgio et al showing that the β subunit of the ATP synthase harbors a Ca2+-binding site responsible for triggering mPT, and the other by Bonora et al demonstrating that permeability transition requires dissociation of F0F1 ATP synthase dimers, albeit in a manner involving the c-subunit ring.
AB - The identity of the mitochondrial permeability transition (mPT) pore, a megachannel embedded in the inner membrane opened by Ca2+, is fiercely debated. Unraveling the components structuring this pore is critical for combating diseases as diverse as neurodegeneration, cancer, autoimmunity, and myopathies in which this phenomenon is implicated. Current consensus is that the pore is formed within, or in-between F0F1 ATP synthase dimers, but not through their c-subunit ring. Two recent studies in this issue of EMBO Reports throw more light on these aspects, one by Giorgio et al showing that the β subunit of the ATP synthase harbors a Ca2+-binding site responsible for triggering mPT, and the other by Bonora et al demonstrating that permeability transition requires dissociation of F0F1 ATP synthase dimers, albeit in a manner involving the c-subunit ring.
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UR - http://www.scopus.com/inward/citedby.url?scp=85021304190&partnerID=8YFLogxK
U2 - 10.15252/embr.201744412
DO - 10.15252/embr.201744412
M3 - Article
C2 - 28630136
AN - SCOPUS:85021304190
JO - EMBO Reports
JF - EMBO Reports
SN - 1469-221X
ER -