ATP synthase membrane subunit k, mitochondrial (ATP5MK)

ATP synthase membrane subunit k (ATP5MK) is a small, highly conserved protein within the F₀ subunit of the mitochondrial ATP synthase complex that is embedded in the inner mitochondrial membrane. ATP synthase is a large multimeric enzyme responsible for synthesizing ATP from ADP and inorganic phosphate during oxidative phosphorylation. Subunit k (also known as DAPIT) is involved in the assembly, stability, and structural integrity of the ATP synthase complex, including the formation of ATP synthase dimers that are essential for proper cristae morphology in mitochondria. Dysregulation or mutation of ATP5MK/DAPIT has been associated with altered energy metabolism and implicated in certain pathologies, including diabetes and muscular disorders. Although subunit k itself is not currently a direct therapeutic target, its role in disease mechanisms and as a potential biomarker is of growing research interest[2][3][4].

Other names

ATP5MKATP synthase F(0) complex subunit k, mitochondrialDAPITATP5MDHCVFTP2USMG5Up-regulated during skeletal muscle growth protein 5Diabetes-associated protein in insulin-sensitive tissuesHCV F-transactivated protein 2AGPbA792D24.4

Not established for subunit k alone For the entire ATP synthase complex: inhibitors bind F₀ sector and block proton translocation, inhibiting ATP synthesis