ArticleThe EMBO journal1996
The import receptor for the peroxisomal targeting signal 2 (PTS2) in Saccharomyces cerevisiae is encoded by the PAS7 gene.
Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 179 citations in OpenAlex.
- Macrophage peroxisomes at the crossroads of inflammation.Immunometabolism (Cobham, Surrey) · 2026Review
- Visualisation of peroxisomes: a journey through seven decades.Histochemistry and cell biology · 2026Review
- Article
- Pex14p Phosphorylation Modulates Import of Citrate Synthase 2 Into Peroxisomes inFrontiers in cell and developmental biology · 2020Article
- Article
- Receptor recognition by the peroxisomal AAA complex depends on the presence of the ubiquitin moiety and is mediated by Pex1p.The Journal of biological chemistry · 2018Article
- Pnc1 piggy-back import into peroxisomes relies on Gpd1 homodimerisation.Scientific reports · 2017Article
- Peroxisome biogenesis disorders.Translational science of rare diseases · 2016Article
- Covalent Label Transfer between Peroxisomal Importomer Components Reveals Export-driven Import Interactions.The Journal of biological chemistry · 2016Article
- The Pex1/Pex6 complex is a heterohexameric AAA+ motor with alternating and highly coordinated subunits.Journal of molecular biology · 2015Article
- Crystal structure of peroxisomal targeting signal-2 bound to its receptor complex Pex7p-Pex21p.Nature structural & molecular biology · 2013Article
- The protein translocation systems in plants - composition and variability on the example of Solanum lycopersicum.BMC genomics · 2013Article
- Cysteine-dependent ubiquitination of Pex18p is linked to cargo translocation across the peroxisomal membrane.The Journal of biological chemistry · 2011Article
- Glycolysis in the african trypanosome: targeting enzymes and their subcellular compartments for therapeutic development.Molecular biology international · 2011Article
- Article
- Interdependence of the peroxisome-targeting receptors in Arabidopsis thaliana: PEX7 facilitates PEX5 accumulation and import of PTS1 cargo into peroxisomes.Molecular biology of the cell · 2010Article
- Two independent pathways traffic the intraperoxisomal peroxin PpPex8p into peroxisomes: mechanism and evolutionary implications.Molecular biology of the cell · 2006Article
- The Arabidopsis peroxisomal targeting signal type 2 receptor PEX7 is necessary for peroxisome function and dependent on PEX5.Molecular biology of the cell · 2005Article
- Functional similarity between the peroxisomal PTS2 receptor binding protein Pex18p and the N-terminal half of the PTS1 receptor Pex5p.Molecular and cellular biology · 2004Article
- Specification of the peroxisome targeting signals type 1 and type 2 of plant peroxisomes by bioinformatics analyses.Plant physiology · 2004Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The import of peroxisomal matrix proteins is dependent on one of two targeting signals, PTS1 and PTS2. We demonstrate in vivo that not only the import of thiolase but also that of a chimeric protein consisting of the thiolase PTS2 (amino acids 1-18) fused to the bacterial protein beta-lactamase is Pas7p dependent. In addition, using a combination of several independent approaches (two-hybrid system, co-immunoprecipitation, affinity chromatography and high copy suppression), we show that Pas7p specifically interacts with thiolase in vivo and in vitro. For this interaction, the N-terminal PTS2 of thiolase is both necessary and sufficient. The specific binding of Pas7p to thiolase does not require peroxisomes. Pas7p recognizes the PTS2 of thiolase even when this otherwise N-terminal targeting signal is fused to the C-terminus of other proteins, i.e. the activation domain of Gal4p or GST. These results demonstrate that Pas7p is the targeting signal-specific receptor of thiolase in Saccharomyces cerevisiae and, moreover, are consistent with the view that Pas7p is the general receptor of the PTS2. Our observation that Pas7p also interacts with the human peroxisomal thiolase suggests that in the human peroxisomal disorders characterized by an import defect for PTS2 proteins (classical rhizomelic chondrodysplasia punctata), a functional homologue of Pas7p may be impaired.
Indexed as
Identifiers
8670791PMC450230W1492622409What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.