Acyl-CoA binding proteins; structural and functional conservation over 2000 MYA.
Besides serving as essential substrates for beta-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.
Faergeman
Nils J
NJ
Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK-5230, Odense M, Denmark. nils.f@bmb.sdu.dk
Wadum
Majken
M
Feddersen
Søren
S
Burton
Mark
M
Kragelund
Birthe B
BB
Knudsen
Jens
J
D000818:Animals; D026261:Diazepam Binding Inhibitor / Q000737:chemistry* / Q000145:classification / Q000378:metabolism*; D006801:Humans; D010802:Phylogeny; D013329:Structure-Activity Relationship
D026261:Diazepam Binding Inhibitor