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

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

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.

In: FEBS Letters, Vol. 552, No. 2-3, 25.09.2003, p. 253-258.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Cohen Simonsen, A, Bernchou Jensen, U, Færgeman, NJ, Knudsen, J & Mouritsen, OG 2003, 'Acyl-coenzyme A organizes laterally in membranes and is recognized specifically by acyl-coenzyme A binding protein', FEBS Letters, vol. 552, no. 2-3, pp. 253-258. https://doi.org/10.1016/S0014-5793(03)00970-0

APA

Cohen Simonsen, A., Bernchou Jensen, U., Færgeman, N. J., Knudsen, J., & Mouritsen, O. G. (2003). Acyl-coenzyme A organizes laterally in membranes and is recognized specifically by acyl-coenzyme A binding protein. FEBS Letters, 552(2-3), 253-258. https://doi.org/10.1016/S0014-5793(03)00970-0

Vancouver

Cohen Simonsen A, Bernchou Jensen U, Færgeman NJ, Knudsen J, Mouritsen OG. Acyl-coenzyme A organizes laterally in membranes and is recognized specifically by acyl-coenzyme A binding protein. FEBS Letters. 2003 Sep 25;552(2-3):253-258. https://doi.org/10.1016/S0014-5793(03)00970-0

Author

Cohen Simonsen, A. ; Bernchou Jensen, U. ; Færgeman, N. J. ; Knudsen, J. ; Mouritsen, O. G. / Acyl-coenzyme A organizes laterally in membranes and is recognized specifically by acyl-coenzyme A binding protein. In: FEBS Letters. 2003 ; Vol. 552, No. 2-3. pp. 253-258.

Bibtex

@article{1f4bac807ce84772b4d16ed97c7c3c26,
title = "Acyl-coenzyme A organizes laterally in membranes and is recognized specifically by acyl-coenzyme A binding protein",
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 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.",
keywords = "Acyl-coenzyme A binding protein, Atomic force microscopy, Lipid bilayer membrane, Long chain fatty acyl-coenzyme A, Phosphatidylcholine",
author = "{Cohen Simonsen}, A. and {Bernchou Jensen}, U. and F{\ae}rgeman, {N. J.} and J. Knudsen and Mouritsen, {O. G.}",
year = "2003",
month = sep,
day = "25",
doi = "10.1016/S0014-5793(03)00970-0",
language = "English",
volume = "552",
pages = "253--258",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "2-3",

}

RIS

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

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