Abstract

Publisher Summary The physiological role of long-chain fatty acyl-CoA (LCACoA) is an intermediate in lipid metabolism. However, LCACoA esters are increasingly recognized as modulators of a wide range of cellular functions. This requires a tight regulation of the intracellular LCACoA concentration in a way that simultaneously allows large variation in the rate of lipogenesis and β-oxidation and sufficient supply of LCACoA for special purposes like protein acylation. The major players in the control of the cellular LCACoA concentration are fatty acid supply, the delicate balance between the activity of acyl-CoA synthetases (ACS) and acyl-CoA thioesterase (TE), and finally the concentration of cellular LCACoA binding proteins. A number of proteins are reported to bind LCACoA including liver fatty acid binding protein (L-FABP), sterol carrier protein 2 (SCP-2), and acyl-coenzyme A binding protein (ACBP). In contrast to FABPs and SCP-2, ACBP binds only LCACoA. ACBP is a ∼10 kDa cytosolic protein, which binds LCACoA esters with high specificity and affinity.

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