ArticleProceedings of the National Academy of Sciences of the United States of America2009
Crystal structure of the conserved N-terminal domain of the peroxisomal matrix protein import receptor, Pex14p.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 37 citations in OpenAlex.
- Building peroxisomes: perspectives on plant peroxins.Biochemical Society transactions · 2026Review
- Pex6 and ubiquitination regulate topological remodeling of the peroxisomal membrane protein Pex14.The Journal of biological chemistry · 2026Article
- PEX14 condensates recruit receptor and cargo pairs for peroxisomal protein import.Nature structural & molecular biology · 2025Article
- Two Pex5 Proteins With Different Cargo Specificity Are Critical for Peroxisome Function in Ustilago maydis.Frontiers in cell and developmental biology · 2022Article
- Mitotic phosphorylation of Pex14p regulates peroxisomal import machinery.The Journal of cell biology · 2020Article
- An HTRF based high-throughput screening for discovering chemical compounds that inhibit the interaction betweenBiochemistry and biophysics reports · 2016Article
- Peroxisome protein import: a complex journey.Biochemical Society transactions · 2016Review
- A novel Pex14 protein-interacting site of human Pex5 is critical for matrix protein import into peroxisomes.The Journal of biological chemistry · 2014Article
- Import of proteins into the peroxisomal matrix.Frontiers in physiology · 2013Review
- The exportomer: the peroxisomal receptor export machinery.Cellular and molecular life sciences : CMLS · 2013Review
- TubStain: a universal peptide-tool to label microtubules.Histochemistry and cell biology · 2012Article
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Authors and funding
5 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Pex14p is a central component of the peroxisomal protein import machinery, in which the conserved N-terminal domain mediates dynamic interactions with other peroxins including Pex5p, Pex13p, and Pex19p. Here, we report the crystal structure of the conserved N-terminal domain of Pex14p with a three-helix bundle. A hydrophobic surface is composed of the conserved residues, of which two phenylalanine residues (Phe-35 and Phe-52) protrude to the solvent. Consequently, two putative binding pockets suitable for recognizing the helical WXXXF/Y motif of Pex5p are formed on the surface by the two phenylalanine residues accompanying with positively charged residues. The structural feature agrees well with our earlier findings where F35A/L36A and F52A/L53A mutants were impaired in the interactions with other peroxins such as Pex5p and Pex13p. Pex14p variants each with Phe-to-Ala mutation at positions 35, 52, and 35/52, respectively, were defective in restoring the impaired peroxisomal protein import in pex14 Chinese hamster ovary mutant ZP161 cells. Moreover, in GST pull-down assays His(6)-Pex5pL bound only to GST-Pex14p(25-70), not to any of GST-Pex14p(25-70)F35A, GST-Pex14p(25-70)F52A, and GST-Pex14p(25-70)F35A/F52A. Endogenous Pex5p was recruited to FLAG-Pex14p on peroxisomes in vivo but barely to FLAG-Pex14pF35A, FLAG-Pex14pF52A, and FLAG-Pex14pF35A/F52A. Collectively, Phe-35 and Phe-52 are essential for the Pex14p functions, including the interaction between Pex14p and Pex5p.
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