Acyl-CoA Binding Proteins; Structural and Functional Conservation over 2000 MYA

Overview

Journal Mol Cell Biochem

Publisher Springer

Specialty Biochemistry

Date 2006 Oct 3

PMID 17013545

Citations 37

Authors

Nils J Faergeman

Majken Wadum

Soren Feddersen

Mark Burton

Birthe B Kragelund

Jens Knudsen

Affiliations

Soon will be listed here.

Abstract

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.

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