ArticleThe Journal of cell biology2002
Acyl-CoA oxidase is imported as a heteropentameric, cofactor-containing complex into peroxisomes of Yarrowia lipolytica.
Article in The Journal of cell biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 124 citations in OpenAlex.
- Peroxisome Carrier SLC25A17: Potential Biomarker for Peroxisome Dysfunction and Human Disease.International journal of molecular sciences · 2026Review
- Identifying and characterizing a missing peroxin-PEX8-in Arabidopsis thaliana.The Plant cell · 2025Article
- Acyl CoA oxidase: from its expression, structure, folding, and import to its role in human health and disease.Molecular genetics and genomics : MGG · 2023Review
- Non-lysine ubiquitylation: Doing things differently.Frontiers in molecular biosciences · 2022Review
- Translating theFrontiers in cell and developmental biology · 2022Review
- Engineering Escherichia coli biofilm to increase contact surface for shikimate and L-malate production.Bioresources and bioprocessing · 2021Article
- Dimerization Drives Proper Folding of Human Alanine:Glyoxylate Aminotransferase But Is Dispensable for Peroxisomal Targeting.Journal of personalized medicine · 2021Article
- Nitric Oxide (NO) Scaffolds the Peroxisomal Protein-Protein Interaction Network in Higher Plants.International journal of molecular sciences · 2021Review
- Nucleotide sugar biosynthesis occurs in the glycosomes of procyclic and bloodstream form Trypanosoma brucei.PLoS neglected tropical diseases · 2021Article
- Peroxisomal Cofactor Transport.Biomolecules · 2020Review
- The Peroxisomal Targeting Signal 3 (PTS3) of the Budding Yeast Acyl-CoA Oxidase Is a Signal Patch.Frontiers in cell and developmental biology · 2020Article
- Peroxisomal Metabolite and Cofactor Transport in Humans.Frontiers in cell and developmental biology · 2020Review
- Harnessing yeast organelles for metabolic engineering.Nature chemical biology · 2017Review
- Signaling dynamics and peroxisomes.Current opinion in cell biology · 2015Review
- The peroxisomal protein import machinery displays a preference for monomeric substrates.Open biology · 2015Article
- Dynein light chain interaction with the peroxisomal import docking complex modulates peroxisome biogenesis in yeast.Journal of cell science · 2013Article
- A cargo-centered perspective on the PEX5 receptor-mediated peroxisomal protein import pathway.The Journal of biological chemistry · 2013Article
- Import of proteins into the peroxisomal matrix.Frontiers in physiology · 2013Review
- Phosphoglucomutase is absent in Trypanosoma brucei and redundantly substituted by phosphomannomutase and phospho-N-acetylglucosamine mutase.Molecular microbiology · 2012Article
- Transport proteins regulate the flux of metabolites and cofactors across the membrane of plant peroxisomes.Frontiers in plant science · 2012Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Five isoforms of acyl-CoA oxidase (Aox), designated Aox1p to Aox5p, constitute a 443-kD heteropentameric complex containing one polypeptide chain of each isoform within the peroxisomal matrix of the yeast Yarrowia lipolytica. Assembly of the Aox complex occurs in the cytosol and precedes its import into peroxisomes. Peroxisomal targeting of the Aox complex is abolished in a mutant lacking the peroxin Pex5p, a component of the matrix protein targeting machinery. Import of the Aox complex into peroxisomes does not involve the cytosolic chaperone Pex20p, which mediates the oligomerization and import of peroxisomal thiolase. Aox2p and Aox3p play a pivotal role in the formation of the Aox complex in the cytosol and can substitute for one another in promoting assembly of the complex. In vitro, these subunits retard disassembly of the Aox complex and increase the efficiency of its reassembly. Neither Aox2p nor Aox3p is required for acquisition of the cofactor FAD by other components of the complex. We provide evidence that the Aox2p- and Aox3p-assisted assembly of the Aox complex in the cytosol is mandatory for its import into peroxisomes and that no component of the complex can penetrate the peroxisomal matrix as a monomer.
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