ArticleNature communications2023
Structure of the peroxisomal Pex1/Pex6 ATPase complex bound to a substrate.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 17 citations in OpenAlex.
- Clinically isolated hearing loss as a mild phenotype of PEX26-associated peroxisomal biogenesis disorder: A case report, literature review, and in silico analysis.Molecular biology reports · 2026Review
- Review
- Visualisation of peroxisomes: a journey through seven decades.Histochemistry and cell biology · 2026Review
- In vivo base editing rescues liver pathophysiology and peroxisome dysfunction in a mouse model of Zellweger spectrum disorder.Nature biomedical engineering · 2026Article
- Structural basis of receptor retro-translocation in peroxisomal protein import.bioRxiv : the preprint server for biology · 2026Article
- Maternal obesity disrupts epigenetic reprogramming via peroxisomal-dependent phospholipid-methyl uncoupling during zygotic genome activation.Nature communications · 2026Article
- Pex6 and ubiquitination regulate topological remodeling of the peroxisomal membrane protein Pex14.The Journal of biological chemistry · 2026Article
- The yeast peroxisomal proteome at absolute quantitative scale.Histochemistry and cell biology · 2026Article
- Integrative transcriptomic and genomic insights into diabetic kidney disease: evidence from multi-omics analysis and experimental validation.Renal failure · 2025Article
- A large-scale curated and filterable dataset for cryo-EM foundation model pre-training.Scientific data · 2025Article
- PEX1The Journal of biological chemistry · 2025Article
- Seventy years of peroxisome research: current advances and future perspectives.Histochemistry and cell biology · 2025Article
- The peroxisome: an update on mysteries 3.0.Histochemistry and cell biology · 2024Review
- Identification of Potential Feature Genes in CRSwNP Using Bioinformatics Analysis and Machine Learning Strategies.Journal of inflammation research · 2024Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The double-ring AAA+ ATPase Pex1/Pex6 is required for peroxisomal receptor recycling and is essential for peroxisome formation. Pex1/Pex6 mutations cause severe peroxisome associated developmental disorders. Despite its pathophysiological importance, mechanistic details of the heterohexamer are not yet available. Here, we report cryoEM structures of Pex1/Pex6 from Saccharomyces cerevisiae, with an endogenous protein substrate trapped in the central pore of the catalytically active second ring (D2). Pairs of Pex1/Pex6(D2) subdomains engage the substrate via a staircase of pore-1 loops with distinct properties. The first ring (D1) is catalytically inactive but undergoes significant conformational changes resulting in alternate widening and narrowing of its pore. These events are fueled by ATP hydrolysis in the D2 ring and disengagement of a "twin-seam" Pex1/Pex6(D2) heterodimer from the staircase. Mechanical forces are propagated in a unique manner along Pex1/Pex6 interfaces that are not available in homo-oligomeric AAA-ATPases. Our structural analysis reveals the mechanisms of how Pex1 and Pex6 coordinate to achieve substrate translocation.
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