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

Research output: Contribution to journalJournal articleResearchpeer-review

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.
Udgivelsesdato: 2007-May
Original languageEnglish
JournalMolecular and Cellular Biochemistry
Volume299
Issue number1-2
Pages (from-to)55-65
Number of pages10
ISSN0300-8177
DOIs
Publication statusPublished - 2007

Bibliographical note

Keywords: Animals; Diazepam Binding Inhibitor; Humans; Phylogeny; Structure-Activity Relationship

ID: 2890706