Identification of a new fatty acid synthesis-transport machinery at the peroxisomal membrane

Standard

Identification of a new fatty acid synthesis-transport machinery at the peroxisomal membrane. / Hillebrand, Merle; Gersting, Søren W; Lotz-Havla, Amelie S; Schäfer, Annika; Rosewich, Hendrik; Valerius, Oliver; Muntau, Ania C; Gärtner, Jutta.

In: J BIOL CHEM, Vol. 287, No. 1, 02.01.2012, p. 210-21.

Research output: SCORING: Contribution to journalSCORING: Journal articleResearchpeer-review

Harvard

Hillebrand, M, Gersting, SW, Lotz-Havla, AS, Schäfer, A, Rosewich, H, Valerius, O, Muntau, AC & Gärtner, J 2012, 'Identification of a new fatty acid synthesis-transport machinery at the peroxisomal membrane', J BIOL CHEM, vol. 287, no. 1, pp. 210-21. https://doi.org/10.1074/jbc.M111.272732

APA

Hillebrand, M., Gersting, S. W., Lotz-Havla, A. S., Schäfer, A., Rosewich, H., Valerius, O., Muntau, A. C., & Gärtner, J. (2012). Identification of a new fatty acid synthesis-transport machinery at the peroxisomal membrane. J BIOL CHEM, 287(1), 210-21. https://doi.org/10.1074/jbc.M111.272732

Vancouver

Hillebrand M, Gersting SW, Lotz-Havla AS, Schäfer A, Rosewich H, Valerius O et al. Identification of a new fatty acid synthesis-transport machinery at the peroxisomal membrane. J BIOL CHEM. 2012 Jan 2;287(1):210-21. https://doi.org/10.1074/jbc.M111.272732

Bibtex

@article{a1ccf583fd864d319aaa9882ecc5221a,
title = "Identification of a new fatty acid synthesis-transport machinery at the peroxisomal membrane",
abstract = "The neurodegenerative disease X-linked adrenoleukodystrophy (X-ALD) is characterized by the abnormal accumulation of very long chain fatty acids. Mutations in the gene encoding the peroxisomal ATP-binding cassette half-transporter, adrenoleukodystrophy protein (ALDP), are the primary cause of X-ALD. To gain a better understanding of ALDP dysfunction, we searched for interaction partners of ALDP and identified binary interactions to proteins with functions in fatty acid synthesis (ACLY, FASN, and ACC) and activation (FATP4), constituting a thus far unknown fatty acid synthesis-transport machinery at the cytoplasmic side of the peroxisomal membrane. This machinery adds to the knowledge of the complex mechanisms of peroxisomal fatty acid metabolism at a molecular level and elucidates potential epigenetic mechanisms as regulatory processes in the pathogenesis and thus the clinical course of X-ALD.",
keywords = "ATP-Binding Cassette Transporters, Acetyl-CoA Carboxylase, Adrenoleukodystrophy, Biological Transport, Fatty Acid Synthases, Fatty Acid Transport Proteins, Fatty Acids, Fluorescence Resonance Energy Transfer, HeLa Cells, Humans, Immunoprecipitation, Intracellular Membranes, Peroxisomes, Spectrum Analysis",
author = "Merle Hillebrand and Gersting, {S{\o}ren W} and Lotz-Havla, {Amelie S} and Annika Sch{\"a}fer and Hendrik Rosewich and Oliver Valerius and Muntau, {Ania C} and Jutta G{\"a}rtner",
year = "2012",
month = jan,
day = "2",
doi = "10.1074/jbc.M111.272732",
language = "English",
volume = "287",
pages = "210--21",
journal = "J BIOL CHEM",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "1",

}

RIS

TY - JOUR

T1 - Identification of a new fatty acid synthesis-transport machinery at the peroxisomal membrane

AU - Hillebrand, Merle

AU - Gersting, Søren W

AU - Lotz-Havla, Amelie S

AU - Schäfer, Annika

AU - Rosewich, Hendrik

AU - Valerius, Oliver

AU - Muntau, Ania C

AU - Gärtner, Jutta

PY - 2012/1/2

Y1 - 2012/1/2

N2 - The neurodegenerative disease X-linked adrenoleukodystrophy (X-ALD) is characterized by the abnormal accumulation of very long chain fatty acids. Mutations in the gene encoding the peroxisomal ATP-binding cassette half-transporter, adrenoleukodystrophy protein (ALDP), are the primary cause of X-ALD. To gain a better understanding of ALDP dysfunction, we searched for interaction partners of ALDP and identified binary interactions to proteins with functions in fatty acid synthesis (ACLY, FASN, and ACC) and activation (FATP4), constituting a thus far unknown fatty acid synthesis-transport machinery at the cytoplasmic side of the peroxisomal membrane. This machinery adds to the knowledge of the complex mechanisms of peroxisomal fatty acid metabolism at a molecular level and elucidates potential epigenetic mechanisms as regulatory processes in the pathogenesis and thus the clinical course of X-ALD.

AB - The neurodegenerative disease X-linked adrenoleukodystrophy (X-ALD) is characterized by the abnormal accumulation of very long chain fatty acids. Mutations in the gene encoding the peroxisomal ATP-binding cassette half-transporter, adrenoleukodystrophy protein (ALDP), are the primary cause of X-ALD. To gain a better understanding of ALDP dysfunction, we searched for interaction partners of ALDP and identified binary interactions to proteins with functions in fatty acid synthesis (ACLY, FASN, and ACC) and activation (FATP4), constituting a thus far unknown fatty acid synthesis-transport machinery at the cytoplasmic side of the peroxisomal membrane. This machinery adds to the knowledge of the complex mechanisms of peroxisomal fatty acid metabolism at a molecular level and elucidates potential epigenetic mechanisms as regulatory processes in the pathogenesis and thus the clinical course of X-ALD.

KW - ATP-Binding Cassette Transporters

KW - Acetyl-CoA Carboxylase

KW - Adrenoleukodystrophy

KW - Biological Transport

KW - Fatty Acid Synthases

KW - Fatty Acid Transport Proteins

KW - Fatty Acids

KW - Fluorescence Resonance Energy Transfer

KW - HeLa Cells

KW - Humans

KW - Immunoprecipitation

KW - Intracellular Membranes

KW - Peroxisomes

KW - Spectrum Analysis

U2 - 10.1074/jbc.M111.272732

DO - 10.1074/jbc.M111.272732

M3 - SCORING: Journal article

C2 - 22045812

VL - 287

SP - 210

EP - 221

JO - J BIOL CHEM

JF - J BIOL CHEM

SN - 0021-9258

IS - 1

ER -