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   <subfield code="a">IF1 distribution in HepG2 cells in relation to ecto-F0F1ATPsynthase and calmodulin</subfield>
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   <subfield code="c">[Stefania Contessi, Marina Comelli, Sara Cmet, Giovanna Lippe, Irene Mavelli]</subfield>
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   <subfield code="a">F0F1ATPsynthase is now known to be expressed as a plasma membrane receptor for several extracellular ligands. On hepatocytes, ecto-F0F1ATPsynthase binds apoA-I and triggers HDL endocytosis concomitant with ATP hydrolysis. Considering that inhibitor protein IF1 was shown to regulate the hydrolytic activity of ecto-F0F1ATPsynthase and to interact with calmodulin (CaM) in vitro, we investigated the subcellular distributions of IF1, calmodulin (CaM), OSCP and β subunits of F0F1ATPsynthase in HepG2 cells. Using immunofluorescence and Western blotting, we found that around 50% of total cellular IF1 is localized outside mitochondria, a relevant amount of which is associated to the plasma membrane where we also found Ca2+-CaM, OSCP and β. Confocal microscopy showed that IF1 colocalized with Ca2+-CaM on plasma membrane but not in mitochondria, suggesting that Ca2+-CaM may modulate the cell surface availability of IF1 and thus its ability to inhibit ATP hydrolysis by ecto-F0F1ATPsynthase. These observations support a hypothesis that the IF1-Ca2+-CaM complex, forming on plasma membrane, functions in the cellular regulation of HDL endocytosis by hepatocytes.</subfield>
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