Assembly of the catalytic module and the rotor of human ATP synthase.
Level 5 - mechanism / opinion, no new human data
Mechanism-based in vitro bench research in human cell lines.
PubMed 42362697 · doi:10.1038/s44318-026-00842-9
What was done
Researchers knocked out specific subunits and known assembly factors in human cell lines to accumulate assembly intermediate complexes of human ATP synthase. These complexes were purified and analyzed using gel electrophoresis and mass spectrometry to define the assembly pathways of the rotor and the catalytic F1-module of the stator.
What was found
The abstract reports no numerical metrics or statistical values. Biochemically, the authors identified distinct subunit compositions of intermediate complexes, proposed pathways for the assembly of the rotor and catalytic stator module, and observed compositional patterns supporting the independent evolutionary origin of the F1-module, peripheral stalk, and membrane-associated Fo-module.
Why it matters
Mapping the stepwise biogenesis of human ATP synthase clarifies how this multi-subunit mitochondrial machine is constructed, providing a framework for studying mitochondrial disorders caused by assembly defects.
Limits
The abstract provides qualitative assembly models without quantitative yields, kinetics, or statistical data. Findings are derived from in vitro cellular knockout models and steady-state intermediate accumulation rather than real-time structural assembly dynamics.
Cited by
- supports The human body produces approximately its own body weight in ATP every day.