ABC lipid transporter
Wagner, E. M. National Heart, Lung and Blood Institutes, National Institutes of Health, Bethesda, Maryland.
Basso, F. National Heart, Lung and Blood Institutes, National Institutes of Health, Bethesda, Maryland.
Kim, C. S. National Heart, Lung and Blood Institutes, National Institutes of Health, Bethesda, Maryland.
Amar, M. J. A. National Heart, Lung and Blood Institutes, National Institutes of Health, Bethesda, Maryland.
Last reviewed:August 2020
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Any of the adenosine triphosphate–binding cassette (ABC) transmembrane proteins that use energy to transport various molecules across extracellular and intracellular membranes (cytoplasmic membranes, endoplasmic reticulum, mitochondria, or peroxisomes). ABC lipid transporters consist of two hydrophobic transmembrane domains and two hydrophilic nucleotide-binding folds. These binding folds contain highly conserved sequence motifs (Walker A and B) and are separated by a linker sequence, also known as the signature (C) motif. ABC transporters are organized as full transporters or half transporters depending on the number of transmembrane domains and nucleotide-binding folds. Half transporters must form homodimers or heterodimers to be functional. See also: Adenosine triphosphate (ATP); Lipid; Lipid metabolism; Protein
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