ArticleThe Journal of biological chemistry2014
A novel Pex14 protein-interacting site of human Pex5 is critical for matrix protein import into peroxisomes.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 69 citations in OpenAlex.
- Building peroxisomes: perspectives on plant peroxins.Biochemical Society transactions · 2026Review
- PEX39 facilitates the peroxisomal import of PTS2-containing proteins.Nature cell biology · 2025Article
- Modular Nanoparticle Platform for Solution-Phase Optical Sensing of Protein-Protein Interactions.ACS applied optical materials · 2025Article
- Modulation of peroxisomal import by the PEX13 SH3 domain and a proximal FxxxF binding motif.Nature communications · 2024Article
- Noncanonical and reversible cysteine ubiquitination prevents the overubiquitination of PEX5 at the peroxisomal membrane.PLoS biology · 2024Article
- Chilling stress response in tobacco seedlings: insights from transcriptome, proteome, and phosphoproteome analyses.Frontiers in plant science · 2024Article
- The Cys-N-degron pathway modulates pexophagy through the N-terminal oxidation and arginylation of ACAD10.Autophagy · 2023Article
- Molecular basis of the glycosomal targeting of PEX11 and its mislocalization to mitochondrion in trypanosomes.Frontiers in cell and developmental biology · 2023Article
- PEX5 translocation into and out of peroxisomes drives matrix protein import.Molecular cell · 2022Article
- Diffusion and interaction dynamics of the cytosolic peroxisomal import receptor PEX5.Biophysical reports · 2022Article
- Proteome-scale mapping of binding sites in the unstructured regions of the human proteome.Molecular systems biology · 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
- Translating theFrontiers in cell and developmental biology · 2022Review
- A missense allele of PEX5 is responsible for the defective import of PTS2 cargo proteins into peroxisomes.Human genetics · 2021Article
- Membrane Interactions of the Peroxisomal Proteins PEX5 and PEX14.Frontiers in cell and developmental biology · 2021Article
- A Mechanistic Perspective on PEX1 and PEX6, Two AAA+ Proteins of the Peroxisomal Protein Import Machinery.International journal of molecular sciences · 2019Review
- Peroxisomal monoubiquitinated PEX5 interacts with the AAA ATPases PEX1 and PEX6 and is unfolded during its dislocation into the cytosol.The Journal of biological chemistry · 2018Article
- Relevance of autophagy to fatty liver diseases and potential therapeutic applications.Amino acids · 2017Review
- 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
- An HTRF based high-throughput screening for discovering chemical compounds that inhibit the interaction betweenBiochemistry and biophysics reports · 2016Article
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Authors and funding
12 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein import into peroxisomes relies on the import receptor Pex5, which recognizes proteins with a peroxisomal targeting signal 1 (PTS1) in the cytosol and directs them to a docking complex at the peroxisomal membrane. Receptor-cargo docking occurs at the membrane-associated protein Pex14. In human cells, this interaction is mediated by seven conserved diaromatic penta-peptide motifs (WXXX(F/Y) motifs) in the N-terminal half of Pex5 and the N-terminal domain of Pex14. A systematic screening of a Pex5 peptide library by ligand blot analysis revealed a novel Pex5-Pex14 interaction site of Pex5. The novel motif composes the sequence LVAEF with the evolutionarily conserved consensus sequence LVXEF. Replacement of the amino acid LVAEF sequence by alanines strongly affects matrix protein import into peroxisomes in vivo. The NMR structure of a complex of Pex5-(57-71) with the Pex14-N-terminal domain showed that the novel motif binds in a similar α-helical orientation as the WXXX(F/Y) motif but that the tryptophan pocket is now occupied by a leucine residue. Surface plasmon resonance analyses revealed 33 times faster dissociation rates for the LVXEF ligand when compared with a WXXX(F/Y) motif. Surprisingly, substitution of the novel motif with the higher affinity WXXX(F/Y) motif impairs protein import into peroxisomes. These data indicate that the distinct kinetic properties of the novel Pex14-binding site in Pex5 are important for processing of the peroxisomal targeting signal 1 receptor at the peroxisomal membrane. The novel Pex14-binding site may represent the initial tethering site of Pex5 from which the cargo-loaded receptor is further processed in a sequential manner.
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