Acyl-coenzyme A organizes laterally in membranes and is recognized specifically by acyl-coenzyme A binding protein

FEBS Lett. 2003 Sep 25;552(2-3):253-8. doi: 10.1016/s0014-5793(03)00970-0.

Abstract

Long chain acyl-coenzyme A (acyl-CoA) is a biochemically important amphiphilic molecule that is known to partition strongly into membranes by insertion of the acyl chain. At present, microscopically resolved evidence is lacking on how acyl-CoA influences and organizes laterally in membranes. By atomic force microscopy (AFM) imaging of membranes exposed to acyl-CoA in microM concentrations, it is shown that aggregate formation takes place within the membrane upon long-time exposure. It is known that acyl-CoA is bound by acyl-CoA binding protein (ACBP) with high affinity and specificity and that ACBP may bind and desorb membrane-bound acyl-CoA via a partly unknown mechanism. Following incubation with acyl-CoA, it is shown that ACBP is able to reverse the formation of acyl-CoA aggregates and to associate peripherally with acyl-CoA on the membrane surface. Our microscopic results point to the role of ACBP as an intermembrane transporter of acyl-CoA and demonstrate the ability of AFM to reveal the remodelling of membranes by surfactants and proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyl Coenzyme A / metabolism*
  • Animals
  • Cattle
  • Diazepam Binding Inhibitor / chemistry
  • Diazepam Binding Inhibitor / metabolism*
  • In Vitro Techniques
  • Lipid Bilayers / metabolism
  • Membranes / metabolism
  • Microscopy, Atomic Force
  • Models, Molecular
  • Phosphatidylcholines / metabolism
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism

Substances

  • Acyl Coenzyme A
  • Diazepam Binding Inhibitor
  • Lipid Bilayers
  • Phosphatidylcholines
  • Recombinant Proteins
  • 1,2-oleoylphosphatidylcholine