Acyl-coenzyme A organizes laterally in membranes and is recognized specifically by acyl-coenzyme A binding protein
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Acyl-coenzyme A organizes laterally in membranes and is recognized specifically by acyl-coenzyme A binding protein. / Cohen Simonsen, A.; Bernchou Jensen, U.; Færgeman, N. J.; Knudsen, J.; Mouritsen, O. G.
I: FEBS Letters, Bind 552, Nr. 2-3, 25.09.2003, s. 253-258.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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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
VL - 552
SP - 253
EP - 258
JO - F E B S Letters
JF - F E B S Letters
SN - 0014-5793
IS - 2-3
ER -
ID: 230986143