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Cited by 157Metabolism and Genetic DisordersDrug Transport and Resistance MechanismsPeroxisome Proliferator-Activated Receptors

The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.

A Saccharomyces cerevisiae homolog of the human adrenoleukodystrophy transporter is a heterodimer of two half ATP-binding cassette transporters.

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Shani, N, Valle, D·1996·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.93.21.11901PMC PMC38156
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Abstract

The adrenoleukodystrophy protein (ALDP) and the 70-kDa peroxisomal membrane protein (PMP70) are half ATP-binding cassette (ABC) transporters in the human peroxisome membrane. ALDP and PMP70 share sequence homology and both are implicated in genetic diseases. PXA1 and YKL741 are Saccharomyces cerevisiae genes that encode homologs of ALDP and PMP70. Pxa1p, a putative ortholog of ALDP, is involved in peroxisomal beta-oxidation of fatty acids while YKL741 is an open reading frame found by the yeast genome sequencing project. Here we designate YKL741 as PXA2 and show that its protein product, Pxa2p, like Pxa1p, is associated with peroxisomes but not required for their assembly. Yeast strains carrying gene disruption of PXA1, PXA2, or both have similar and, in the case of the latter, nonadditive phenotypes. We also find that the stability of Pxa1p, but not Pxa2p, is markedly reduced in the absence of the other. Finally, we find that Pxa1p and Pxa2p coimmuno-precipitate. These genetic and physical data suggest that Pxa1p and Pxa2p heterodimerize to form a complete peroxisomal ABC transporter involved in fatty acid beta-oxidation. This result predicts the presence of similar heterodimeric ABC transporters in the mammalian peroxisome membrane.

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Research works printed but not linked: 4

  1. [8]Lombard-Platet, G., Savary, S., Sarde, C.-O. & Mandel, J.-L. (1996) Proc. Natl. Acad. Sci. USA 93, 1265–1269.
  2. [9]Moser, H., Smith, K. & Moser, A. (1995) in The Metabolic and Molecular Bases of Inherited Disease, eds. Scriver, C., Beaudet, A., Sly, W. & Valle, D. (McGraw–Hill, New York), pp. 2325–2349.
  3. [16]Shani, N., Watkins, P. A. & Valle, D. (1995) Proc. Natl. Acad. Sci. USA 92, 6012–6016.
  4. [18]Èrdmann, R., Veenhuis, D., Mertens, D. & Kunau, W. H. (1989) Proc. Natl. Acad. Sci. USA 86, 5419–5423.

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Metadata

Authors
Shani, N., & Valle, D.
Affiliations
Kennedy Krieger Institute (US)
ORCID
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
1996-10-15
Volume
93
Issue
21
Pages
11901-11906
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.93.21.11901
PMC
PMC38156
OpenAlex
W2055737079
Cited by
157
References
42
Citations by year
2026: 2 · 2025: 1 · 2024: 1 · 2023: 2 · 2022: 3 · 2021: 1 · 2020: 5 · 2019: 3 · 2018: 2 · 2017: 1 · 2016: 3 · 2015: 6 · 2014: 2 · 2013: 6 · 2012: 3
FWCI
8.35
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Howard Hughes Medical Institute
  • National Institutes of Health (HD10981)
  • Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD-10981, P01HD010981)
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
PMP70, peroxisomal membrane proteins, peroxisomal beta-oxidation, fatty acid beta-oxidation, protein stability, protein-protein interaction, Saccharomyces cerevisiae, peroxisome biogenesis
MeSH terms
ATP Binding Cassette Transporter, Subfamily D, Member 1, Adenosine Triphosphate, Fungal Proteins, Genes, Fungal, Humans, Membrane Proteins, Microbodies, Protein Binding, Saccharomyces cerevisiae, Transcription, Genetic, Open Reading Frames, ATP-Binding Cassette Transporters, Saccharomyces cerevisiae Proteins

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