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From the Ca 2+ -activated F 1 F O -ATPase to the mitochondrial permeability transition pore: an overview
- Source :
- Biochimie. 152:85-93
- Publication Year :
- 2018
- Publisher :
- Elsevier BV, 2018.
-
Abstract
- Based on recent advances on the Ca2+-activated F1FO-ATPase features, a novel multistep mechanism involving the mitochondrial F1FO complex in the formation and opening of the still enigmatic mitochondrial permeability transition pore (MPTP), is proposed. MPTP opening makes the inner mitochondrial membrane (IMM) permeable to ions and solutes and, through cascade events, addresses cell fate to death. Since MPTP forms when matrix Ca2+ concentration rises and ATP is hydrolyzed by the F1FO-ATPase, conformational changes, triggered by Ca2+ insertion in F1, may be transmitted to FO and locally modify the IMM curvature. These events would cause F1FO-ATPase dimer dissociation and MPTP opening.
- Subjects :
- 0301 basic medicine
Mitochondrial permeability transition pore
F1Fo-ATPase
MPTP
Dimer
chemistry.chemical_element
General Medicine
Calcium
Cell fate determination
Biochemistry
03 medical and health sciences
chemistry.chemical_compound
030104 developmental biology
0302 clinical medicine
chemistry
Conformational mechanism
Calcium ion
Biophysics
F(1)F(O)-ATPase
Inner mitochondrial membrane
030217 neurology & neurosurgery
Subjects
Details
- ISSN :
- 03009084
- Volume :
- 152
- Database :
- OpenAIRE
- Journal :
- Biochimie
- Accession number :
- edsair.doi.dedup.....d6b879b668905e687abae43855ac946c