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, Jahrgang 287, Nr. 1, 02.01.2012, S. 210-21.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
Harvard
APA
Vancouver
Bibtex
}
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 -