ArticleThe Journal of biological chemistry2011
PEX5 protein binds monomeric catalase blocking its tetramerization and releases it upon binding the N-terminal domain of PEX14.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 92 citations in OpenAlex.
- Structure of Trypanosoma peroxisomal import complex unveils conformational heterogeneity.Nature communications · 2025Article
- PEX14 condensates recruit receptor and cargo pairs for peroxisomal protein import.Nature structural & molecular biology · 2025Article
- Targeting catalase in cancer.Redox biology · 2024Review
- Key homeobox transcription factors regulate the development of the firefly's adult light organ and bioluminescence.Nature communications · 2024Article
- The mammalian peroxisomal membrane is permeable to both GSH and GSSG - Implications for intraperoxisomal redox homeostasis.Redox biology · 2023Article
- Hepatitis C virus alters the morphology and function of peroxisomes.Frontiers in microbiology · 2023Article
- Insights into the Structure and Function of the Pex1/Pex6 AAA-ATPase in Peroxisome Homeostasis.Cells · 2022Review
- Diffusion and interaction dynamics of the cytosolic peroxisomal import receptor PEX5.Biophysical reports · 2022Article
- Nuclear and peroxisomal targeting of catalase.Plant, cell & environment · 2022Article
- Studying the interaction between PEX5 and its full-length cargo proteins in living cells by a novel Försteŕs resonance energy transfer-based competition assay.Frontiers in cell and developmental biology · 2022Article
- Protein-protein interactions in plant antioxidant defense.Frontiers in plant science · 2022Review
- Dimerization Drives Proper Folding of Human Alanine:Glyoxylate Aminotransferase But Is Dispensable for Peroxisomal Targeting.Journal of personalized medicine · 2021Article
- A Mechanistic Perspective on PEX1 and PEX6, Two AAA+ Proteins of the Peroxisomal Protein Import Machinery.International journal of molecular sciences · 2019Review
- Current Advances in Protein Import into Peroxisomes.The protein journal · 2019Review
- Peroxisome Function, Biogenesis, and Dynamics in Plants.Plant physiology · 2018Review
- Allostery between two binding sites in the ion channel subunit TRIP8b confers binding specificity to HCN channels.The Journal of biological chemistry · 2017Article
- 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
- Peroxisomal Dysfunction in Age-Related Diseases.Trends in endocrinology and metabolism: TEM · 2017Review
- Pnc1 piggy-back import into peroxisomes relies on Gpd1 homodimerisation.Scientific reports · 2017Article
- A cell-free organelle-based in vitro system for studying the peroxisomal protein import machinery.Nature protocols · 2016Article
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Newly synthesized peroxisomal matrix proteins are targeted to the organelle by PEX5. PEX5 has a dual role in this process. First, it acts as a soluble receptor recognizing these proteins in the cytosol. Subsequently, at the peroxisomal docking/translocation machinery, PEX5 promotes their translocation across the organelle membrane. Despite significant advances made in recent years, several aspects of this pathway remain unclear. Two important ones regard the formation and disruption of the PEX5-cargo protein interaction in the cytosol and at the docking/translocation machinery, respectively. Here, we provide data on the interaction of PEX5 with catalase, a homotetrameric enzyme in its native state. We found that PEX5 interacts with monomeric catalase yielding a stable protein complex; no such complex was detected with tetrameric catalase. Binding of PEX5 to monomeric catalase potently inhibits its tetramerization, a property that depends on domains present in both the N- and C-terminal halves of PEX5. Interestingly, the PEX5-catalase interaction is disrupted by the N-terminal domain of PEX14, a component of the docking/translocation machinery. One or two of the seven PEX14-binding diaromatic motifs present in the N-terminal half of PEX5 are probably involved in this phenomenon. These results suggest the following: 1) catalase domain(s) involved in the interaction with PEX5 are no longer accessible upon tetramerization of the enzyme; 2) the catalase-binding interface in PEX5 is not restricted to its C-terminal peroxisomal targeting sequence type 1-binding domain and also involves PEX5 N-terminal domain(s); and 3) PEX14 participates in the cargo protein release step.
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