Loss of the F-ATP synthase c-subunit inhibits a pathological mitochondrial permeability transition pore that is coupled to a maladaptive mitochondrial unfolded protein response while also extending lifespan.

Mitochondria can trigger massive endocytosis by releasing coenzyme A into the cytoplasm and thereby promoting the addition of fatty acids to surface membrane proteins.

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.

The proteins Bax and Bak, which increase the permeability of the mitochondrial membrane during apoptosis, are also crucial for generating a mitochondrial membrane pore that is specifically involved in necrosis.

Promoter studies identified BMP/Smad signaling as a transcriptional regulator of Ppif gene encoding cyclophilin D, a component of the mitochondrial permeability transition pore, and gain- and loss-of-function experiments determined how such regulation affects osteogenic differentiation.

Polymorphic residues of a vacuolar Ca²⁺ sensor site in TPC1 channels differ between species of Brassicacea and Fabaceae and lead to distinct TPC1 gating behavior.

Contrary to a generally accepted principle, the pore properties of KCNQ1 channels depend on the states of voltage-sensing domains activation; KCNE1 alters the voltage-sensing domains-pore coupling to modulate KCNQ1 channel properties.

Cryo-EM structures of the gating cycle of bestrophin reveal the molecular underpinnings of activation and inactivation gating in this calcium-activated chloride channel and reveal a surprisingly wide pore.

Reoxygenation of anoxic cardiac tissue promotes massive endocytosis that is triggered by release of coenzymeA from mitochondria, followed by palmitoylation of membrane proteins, sarcolemma vesiculation, and transfer of sarolemma vesicles to large endosomes and vacuoles.