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ATP synthase membrane subunit c locus 2 (ATP5MC2) is one of three human genes encoding the precursor for subunit c of mitochondrial ATP synthase's F₀ sector. This 75-residue peptide is imported into mitochondria, processed to its mature form, and incorporated into the c-ring complex, which oligomerizes to form the membrane-embedded proton channel. The c subunit's rotation, driven by proton transit, is critical for ATP generation from ADP and inorganic phosphate. Distinct isoforms (P1, P2, P3) differ mainly in their mitochondrial targeting sequences, and each is necessary for optimal ATP synthase function and assembly. Malfunction or aggregation of this subunit impairs mitochondrial energy metabolism and has been implicated in neurodegeneration and stress-induced mitochondrial permeability transitions.
Inhibitors such as oligomycin and DCCD bind to the c subunit, blocking proton translocation and thus halting ATP synthesis, leading to cellular energy failure.
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