TY  - JOUR
A1  - Rampello, Nadia Giusi
A1  - Stenger, Maria
A1  - Westermann, Benedikt
A1  - Osiewacz, Heinz D.
T1  - Impact of F1Fo-ATP-synthase dimer assembly factors on mitochondrial function and organismic aging
T2  - Microbial cell
N2  - In aerobic organisms, mitochondrial F1Fo-ATP-synthase is the major site of ATP production. Beside this fundamental role, the protein complex is involved in shaping and maintenance of cristae. Previous electron microscopic studies identified the dissociation of F1Fo-ATP-synthase dimers and oligomers during organismic aging correlating with a massive remodeling of the mitochondrial inner membrane. Here we report results aimed to experimentally proof this impact and to obtain further insights into the control of these processes. We focused on the role of the two dimer assembly factors PaATPE and PaATPG of the aging model Podospora anserina. Ablation of either protein strongly affects mitochondrial function and leads to an accumulation of senescence markers demonstrating that the inhibition of dimer formation negatively influences vital functions and accelerates organismic aging. Our data validate a model that links mitochondrial membrane remodeling to aging and identify specific molecular components triggering this process.
KW  - aging
KW  - F1Fo-ATP-synthase
KW  - membranes
KW  - mitochondria
KW  - remodeling
Y1  - 2018
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/52554
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-525542
N1  - © 2018 Rampello et al. This is an open-access article released under the terms of the Creative Commons Attribution (CC BY) license, which allows the unrestricted use, distribution, and reproduction in any medium, provided the original author and source are acknowledged
VL  - 5
IS  - 4
SP  - 198
EP  - 207
ER  -