ArticleNature cell biology2025
Import mechanism of peroxisomal proteins with an N-terminal signal sequence.
Article in Nature cell biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Building peroxisomes: perspectives on plant peroxins.Biochemical Society transactions · 2026Review
- Peroxin Pex8 couples stress responses, antifungal tolerance, and virulence regulation inAntimicrobial agents and chemotherapy · 2026Article
- Structural basis of receptor retro-translocation in peroxisomal protein import.bioRxiv : the preprint server for biology · 2026Article
- Evolutionary remodeling of a remnant GET pathway factor into PEX38, an essential peroxin.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The yeast peroxisomal proteome at absolute quantitative scale.Histochemistry and cell biology · 2026Article
- PEX39 facilitates the peroxisomal import of PTS2-containing proteins.Nature cell biology · 2025Article
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Authors and funding
2 authors.
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Abstract
Most proteins imported into peroxisomes use a carboxy-terminal PTS1 signal, which is recognized by soluble receptors that transport the cargo through a nuclear pore-like conduit in the peroxisomal membrane formed by the tyrosine and glycine-rich YG domain of PEX13. The receptors then return to the cytosol through a separate retrotranslocon. Some peroxisomal proteins instead use an amino-terminal PTS2 signal that is recognized by an adaptor called PEX7, but how they are imported is poorly understood. Here we show that PTS2 cargo is moved through the YG phase by PEX7 bound to a receptor. After cargo release inside peroxisomes, PEX7 returns to the cytosol by moving back on its own through the YG phase. The chaperone PEX39 then extracts PEX7 from the phase on the cytosolic side and helps to reload PEX7 with a new receptor and cargo to start another import cycle. Our results provide a comprehensive model of PTS2 protein import.
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