The MondoA transcription factor localizes to the outer mitochondrial membrane where it coordinates an adaptive transcriptional response to elevated cellular energy represented by high cytoplasmic glucose and high mitochondrial ATP.

Mitochondrial flashes counteract the imbalance of ATP supply-and-demand and constitute an auto-regulator of ATP homeostasis in the heart.

Structural analysis of the ATP synthase – in combination with evolutionary covariance analysis – reveals the fold of the a subunit and shows that the enzyme can adopt several different conformations, which support the Brownian ratchet model for generating rotation.

The atomic model of a mitochondrial ATP synthase dimer underlies functions of its specific protein constituents and boundary cardiolipins.

SIT4 deletion and phosphate starvation increase mitochondrial membrane potential via electron transport chain dependent and independent manners, and the increased membrane potential induced by phosphate depletion is conserved between yeast, flies, and humans.

Mitochondrial Cx43 hemichannels regulate ATP generation by mediating K+, H+, and ATP transfer across the mitochondrial inner membrane and the interaction with mitochondrial ATP synthase, contributing to maintenance of mitochondrial redox and cell protection under oxidative stress.

A flip of the dimer asymmetry following the first ATP hydrolysis provides a mechanistic model for client remodeling by the mitochondrial Hsp90, TRAP1.

The transmembrane shape of the F₁F_o ATP synthase monomer provides the molecular basis of high curvature at the ridges of mammalian mitochondrial cristae.

Three-dimensional electron microscopy (3DEM) demonstrates the dependence on presynaptic mitochondria for vesicle mobilization as dendritic spines are silently added at P15 or synapses are silently enlarged in adults after long-term potentiation.

The notion that the lumen of the ATP synthase membrane rotor is the long-sought megachannel that triggers the onset of the mitochondrial permeability transition is found to be inconsistent with its actual structural and functional properties.