ATP synthase subunit beta, mitochondrial (ATP5F1B) (ATP5F1B)

The HDL catabolism receptor, primarily identified as the beta-chain of mitochondrial ATP synthase (ATP5F1B) when expressed on the hepatocyte cell surface, is a key regulator of high-density lipoprotein (HDL) metabolism (UniProt P06576). Unlike the scavenger receptor class B member 1 (SR-B1), which facilitates the selective uptake of cholesterol esters, the HDL catabolism receptor mediates the endocytosis and degradation of the entire HDL-apoA-I holoparticle (Kamanna & Kashyap, 2008). This process significantly influences the plasma residence time and concentration of HDL, which is vital for reverse cholesterol transport and cardiovascular health (PubMed: 18375237). Niacin (nicotinic acid) is the primary pharmacological agent known to interact with this pathway, specifically by inhibiting the surface expression of the receptor on hepatocytes (ResearchGate: 265524351). By reducing the catabolism of HDL particles, niacin effectively increases circulating HDL-C and apolipoprotein A-I levels. This mechanism contributes to the therapeutic efficacy of niacin in treating dyslipidemia and reducing the risk of atherosclerosis. However, targeting this pathway is also associated with metabolic challenges, such as potential impacts on glucose homeostasis and hepatic function (StatPearls: NBK526125).

Other names

HDL catabolism receptorBeta-chain adenosine triphosphate synthaseEcto-F1-ATPaseATP5BATP synthase subunit betaHDL holoparticle receptor

Niacin inhibits the cell surface expression of the beta-chain ATP synthase on hepatocytes, which reduces the endocytosis and catabolism of HDL-apoA-I holoparticles, leading to increased plasma HDL levels (Kamanna & Kashyap, 2008).