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Publication : Regulation of very-long acyl chain ceramide synthesis by acyl-CoA-binding protein.

First Author  Ferreira NS Year  2017
Journal  J Biol Chem Volume  292
Issue  18 Pages  7588-7597
PubMed ID  28320857 Mgi Jnum  J:242498
Mgi Id  MGI:5905500 Doi  10.1074/jbc.M117.785345
Citation  Ferreira NS, et al. (2017) Regulation of very-long acyl chain ceramide synthesis by acyl-CoA-binding protein. J Biol Chem 292(18):7588-7597
abstractText  Ceramide and more complex sphingolipids constitute a diverse group of lipids that serve important roles as structural entities of biological membranes and as regulators of cellular growth, differentiation, and development. Thus, ceramides are vital players in numerous diseases including metabolic and cardiovascular diseases, as well as neurological disorders. Here we show that acyl-coenzyme A-binding protein (ACBP) potently facilitates very-long acyl chain ceramide synthesis. ACBP increases the activity of ceramide synthase 2 (CerS2) by more than 2-fold and CerS3 activity by 7-fold. ACBP binds very-long-chain acyl-CoA esters, which is required for its ability to stimulate CerS activity. We also show that high-speed liver cytosol from wild-type mice activates CerS3 activity, whereas cytosol from ACBP knock-out mice does not. Consistently, CerS2 and CerS3 activities are significantly reduced in the testes of ACBP-/- mice, concomitant with a significant reduction in long- and very-long-chain ceramide levels. Importantly, we show that ACBP interacts with CerS2 and CerS3. Our data uncover a novel mode of regulation of very-long acyl chain ceramide synthesis by ACBP, which we anticipate is of crucial importance in understanding the regulation of ceramide metabolism in pathogenesis.
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