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Updated: Nov 6, 2025

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
Published on: September 14, 2014
The f subunit of human ATP synthase is essential for normal mitochondrial morphology and permeability transition
Chiara Galber1, Giovanni Minervini2, Giuseppe Cannino2
1Department of Biomedical Sciences, University of Padova, Padova 35121, Italy; Consiglio Nazionale delle Ricerche Institute of Neuroscience, Padova 35121, Italy.
Abstract:
The f subunit is localized at the base of the ATP synthase peripheral stalk. Its function in the human enzyme is poorly characterized. Because full disruption of its ATP5J2 gene with the CRISPR-Cas9 strategy in the HAP1 human model has been shown to cause alterations in the amounts of other ATP synthase subunits, here we investigated the role of the f subunit in HeLa cells by regulating its levels through RNA interference. We confirm the role of the f subunit in ATP synthase dimer stability and observe that its downregulation per se does not alter the amounts of the other enzyme subunits or ATP synthase synthetic/hydrolytic activity. We show that downregulation of the f subunit causes abnormal crista organization and decreases permeability transition pore (PTP) size, whereas its re-expression in f subunit knockdown cells rescues mitochondrial morphology and PTP-dependent swelling.
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