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

TY - JOUR

T1 - Acyl-coenzyme A organizes laterally in membranes and is recognized specifically by acyl-coenzyme A binding protein

AU - Cohen Simonsen, A.

AU - Bernchou Jensen, U.

AU - Færgeman, N. J.

AU - Knudsen, J.

AU - Mouritsen, O. G.

PY - 2003/9/25

Y1 - 2003/9/25

N2 - 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 μM 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.

AB - 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 μM 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.

KW - Acyl-coenzyme A binding protein

KW - Atomic force microscopy

KW - Lipid bilayer membrane

KW - Long chain fatty acyl-coenzyme A

KW - Phosphatidylcholine

UR - http://www.scopus.com/inward/record.url?scp=0141425728&partnerID=8YFLogxK

U2 - 10.1016/S0014-5793(03)00970-0

DO - 10.1016/S0014-5793(03)00970-0

M3 - Journal article

C2 - 14527695

AN - SCOPUS:0141425728

SN - 0014-5793

VL - 552

SP - 253

EP - 258

JO - F E B S Letters

JF - F E B S Letters

IS - 2-3

ER -