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Acyl-CoA binding proteins; structural and functional conservation over 2000 MYA

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Abstract

Besides serving as essential substrates for β-oxidation and synthesis of triacylglycerols and more complex lipids like sphingolipids and sterol esters, long-chain fatty acyl-CoA esters are increasingly being recognized as important regulators of enzyme activities and gene transcription. Acyl-CoA binding protein, ACBP, has been proposed to play a pivotal role in the intracellular trafficking and utilization of long-chain fatty acyl-CoA esters. Depletion of acyl-CoA binding protein in yeast results in aberrant organelle morphology incl. fragmented vacuoles, multi-layered plasma membranes and accumulation of vesicles of variable sizes. In contrast to synthesis and turn-over of glycerolipids, the levels of very-long-chain fatty acids, long-chain bases and ceramide are severely affected by Acb1p depletion, suggesting that Acb1p, rather than playing a general role, serves specific roles in cellular lipid metabolism.

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  1. Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK-5230, Odense M, Denmark

    Nils J. Færgeman, Majken Wadum, Søren Feddersen, Mark Burton & Jens Knudsen

  2. Department of Protein Chemistry, Institute of Molecular Biology, University of Copenhagen, Øster Farimagsgade 2A, DK-1353, Copenhagen K, Denmark

    Birthe B. Kragelund

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Færgeman, N.J., Wadum, M., Feddersen, S. et al. Acyl-CoA binding proteins; structural and functional conservation over 2000 MYA. Mol Cell Biochem 299, 55–65 (2007). https://doi.org/10.1007/s11010-005-9040-3

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  • DOI: https://doi.org/10.1007/s11010-005-9040-3

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