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cristae mitochondria briefs
2 importance briefs tagged cristae, including the current week and the archive.
- biorxiv2026-10-28score 92
NDUFA13 lysine-7 acetylation is the switch from OXPHOS failure to cristae collapse in heart failure
Nan, Yang, Liu, He and colleagues identify acetylation of the Complex I accessory subunit NDUFA13 at lysine 7 as the sensor that turns OXPHOS inhibition into cristae disintegration. Hyperacetylated NDUFA13 compacts, moves toward the intermembrane space, binds PHB2, displaces PHB1, and takes apart prohibitin scaffolds. The acetylation mimic K7Q fragments cristae in cells. Cardiomyocyte-specific K7Q knock-in mice die faster under pressure overload, lose cristae, slow the TCA cycle and fatty acid oxidation, and selectively deplete polyunsaturated cardiolipins. NDUFA13 is not an Fe-S subunit. Complex I's N-module carries Fe-S clusters; this abstract does not name them or a couple at K7. The chemistry on the residue is lysine acetylation, reversed in principle by deacetylation. The membrane chemistry that fails downstream is polyunsaturated cardiolipin.
- biorxiv2026-08-04score 91
Cholesterol in APOE4 astrocytes truncates cristae, drops Complexes I and IV, and leaves cells dependent on a reversing ATP synthase
Lee, Holt and colleagues find that APOE4 mouse astrocytes with high intracellular cholesterol build sparse, truncated cristae and extra crista-junction complexes, lose respiratory Complexes I and IV, and respire less. Membrane potential still rises, because proton leak is low and ATP synthase runs in reverse, hydrolyzing ATP to support the gradient. Oligomycin becomes selectively toxic, and sequestering cholesterol with methyl-β-cyclodextrin removes that toxicity. The lost complexes imply iron-sulfur, heme, and copper sites. The abstract reports the complexes, not the metals. The enzyme they actually catch misbehaving is ATP synthase.
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