Structure-Function Analysis of Peroxisomal ATP-binding Cassette Transporters Using Chimeric Dimers
Open accessAbstract
ABCD1 and ABCD2 are two closely related ATP-binding cassette half-transporters predicted to homodimerize and form peroxisomal importers for fatty acyl-CoAs. Available evidence has shown that ABCD1 and ABCD2 display a distinct but overlapping substrate specificity, although much remains to be learned in this respect as well as in their capability to form functional heterodimers. Using a cell model expressing an ABCD2-EGFP fusion protein, we first demonstrated by proximity ligation assay and co-immunoprecipitation assay that ABCD1 interacts with ABCD2. Next, we tested in the pxa1/pxa2Δ yeast mutant the functionality of ABCD1/ABCD2 dimers by expressing chimeric proteins mimicking homo- or heterodimers. For further structure-function analysis of ABCD1/ABCD2 dimers, we expressed chimeric dimers fused to enhanced GFP in human skin fibroblasts of X-linked adrenoleukodystrophy patients. These cells are devoid of ABCD1 and accumulate very long-chain fatty acids (C26:0 and C26:1). We checked that the chimeric proteins were correctly expressed and targeted to the peroxisomes. Very long-chain fatty acid levels were partially restored in transfected X-linked adrenoleukodystrophy fibroblasts regardless of the chimeric construct used, thus demonstrating functionality of both homo- and heterodimers. Interestingly, the level of C24:6 n-3, the immediate precursor of docosahexaenoic acid, was decreased in cells expressing chimeric proteins containing at least one ABCD2 moiety. Our data demonstrate for the first time that both homo- and heterodimers of ABCD1 and ABCD2 are functionally active. Interestingly, the role of ABCD2 (in homo- and heterodimeric forms) in the metabolism of polyunsaturated fatty acids is clearly evidenced, and the chimeric dimers provide a novel tool to study substrate specificity of peroxisomal ATP-binding cassette transporters.
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Chimeric heterodimers of ABCD1 and ABCD2 were shown in vitro to be functional.
“As chimeric heterodimers of ABCD1 and ABCD2 were shown in vitro to be functional, this would raise the possibility of different substrate preferences for such putative heterodimers.126”
From The genetic landscape of X-linked adrenoleukodystrophy: inheritance, mutations, modifier genes, and diagnosis (2015) · cites this paper as [126]
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- Authors
- Geillon, F., Gondcaille, C., Charbonnier, S., Van Roermund, C. W., Lopez, T. E., Dias, A. M. M., Pais de Barros, J.-P., Arnould, C., Wanders, R. J., Trompier, D., & Savary, S.
- Affiliations
- Université de Bourgogne (FR)
- Centre National de la Recherche Scientifique (FR)
- Amsterdam UMC Location University of Amsterdam (NL)
- Corresponding author
- Savary, Stéphane
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2014-08
- Volume
- 289
- Issue
- 35
- Pages
- 24511-24520
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC4148876
- OpenAlex
- W1991673143
- Cited by
- 24
- References
- 51
- Citations by year
- 2025: 1 · 2023: 1 · 2022: 2 · 2021: 1 · 2020: 1 · 2019: 5 · 2018: 4 · 2017: 2 · 2016: 5 · 2015: 2
- FWCI
- 2.08
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- HAL (submittedVersion, cc-by)
- Pure Amsterdam UMC (submittedVersion)
- Funders
- Conseil régional de Bourgogne-Franche-Comté
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Peroxisome Proliferator-Activated Receptors
- Keywords
- ABCD1, ABCD2, heterodimerization, homo- and heterodimers, X-linked adrenoleukodystrophy, very long chain fatty acids, polyunsaturated fatty acid metabolism, substrate specificity, peroxisomes
- MeSH terms
- Animals, Base Sequence, Cell Line, Humans, Plasmids, Structure-Activity Relationship, Polymerase Chain Reaction, DNA Primers, ATP-Binding Cassette Transporters, Dimerization, Peroxisomes, Mice, Rats
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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