ArticleThe EMBO journal2007
Novel peroxisomal protease Tysnd1 processes PTS1- and PTS2-containing enzymes involved in beta-oxidation of fatty acids.
Article in The EMBO journal, 2007. 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.
- Building peroxisomes: perspectives on plant peroxins.Biochemical Society transactions · 2026Review
- Colab-PEX19BS: An Automated Google Colab Notebook-Based Tool for Detecting PEX19-Binding Sites.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Ribosome-binding protein 1 maintains peroxisome biogenesis.Journal of cell science · 2025Article
- Systemic inflammation-induced adipose tissue remodeling drives psoriasis exacerbation in obesity through epigenetic and immunometabolic dysregulation.Theranostics · 2025Article
- Peroxisomal ROS control cytosolic Mycobacterium tuberculosis replication in human macrophages.The Journal of cell biology · 2023Article
- The mammalian peroxisomal membrane is permeable to both GSH and GSSG - Implications for intraperoxisomal redox homeostasis.Redox biology · 2023Article
- Learning biologically-interpretable latent representations for gene expression data: Pathway Activity Score Learning Algorithm.Machine learning · 2023Article
- Fusarium verticillioides Pex7/20 mediates peroxisomal PTS2 pathway import, pathogenicity, and fumonisin B1 biosynthesis.Applied microbiology and biotechnology · 2022Article
- Translating theFrontiers in cell and developmental biology · 2022Review
- Insights Into the Peroxisomal Protein Inventory of Zebrafish.Frontiers in physiology · 2022Article
- Article
- A missense allele of PEX5 is responsible for the defective import of PTS2 cargo proteins into peroxisomes.Human genetics · 2021Article
- Mammalian Homologue NME3 of DYNAMO1 Regulates Peroxisome Division.International journal of molecular sciences · 2020Article
- Non-AUG Translation Initiation Generates Peroxisomal Isoforms of 6-Phosphogluconate Dehydrogenase in Fungi.Frontiers in cell and developmental biology · 2020Article
- APlant direct · 2019Article
- A newly identified mutation in theCold Spring Harbor molecular case studies · 2019Article
- Sequential Molecular Events of Functional Trade-Offs in 5-Hydroxyisourate Hydrolase Before and After Gene Duplication Led to the Evolution of Transthyretin During Chordate Diversification.Journal of molecular evolution · 2018Article
- Redox Regulation of Homeostasis and Proteostasis in Peroxisomes.Physiological reviews · 2018Review
- The peroxisomal matrix protein translocon is a large cavity-forming protein assembly into which PEX5 protein enters to release its cargo.The Journal of biological chemistry · 2017Article
- Genome-wide analysis of mRNAs associated with mouse peroxisomes.BMC genomics · 2016Article
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6 authors.
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Abstract
Peroxisomes play an important role in beta-oxidation of fatty acids. All peroxisomal matrix proteins are synthesized in the cytosol and post-translationally sorted to the organelle. Two distinct peroxisomal signal targeting sequences (PTSs), the C-terminal PTS1 and the N-terminal PTS2, have been defined. Import of precursor PTS2 proteins into the peroxisomes is accompanied by a proteolytic removal of the N-terminal targeting sequence. Although the PTS1 signal is preserved upon translocation, many PTS1 proteins undergo a highly selective and limited cleavage. Here, we demonstrate that Tysnd1, a previously uncharacterized protein, is responsible both for the removal of the leader peptide from PTS2 proteins and for the specific processing of PTS1 proteins. All of the identified Tysnd1 substrates catalyze peroxisomal beta-oxidation. Tysnd1 itself undergoes processing through the removal of the presumably inhibitory N-terminal fragment. Tysnd1 expression is induced by the proliferator-activated receptor alpha agonist bezafibrate, along with the increase in its substrates. A model is proposed where the Tysnd1-mediated processing of the peroxisomal enzymes promotes their assembly into a supramolecular complex to enhance the rate of beta-oxidation.
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