ArticleThe Journal of biological chemistry2015
Structural insights into cargo recognition by the yeast PTS1 receptor.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 30 citations in OpenAlex.
- Building peroxisomes: perspectives on plant peroxins.Biochemical Society transactions · 2026Review
- Identifying and characterizing a missing peroxin-PEX8-in Arabidopsis thaliana.The Plant cell · 2025Article
- PEX1 is essential for glycosome biogenesis and trypanosomatid parasite survival.Frontiers in cellular and infection microbiology · 2024Article
- Molecular Response ofJournal of fungi (Basel, Switzerland) · 2023Article
- 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
- The Peroxisomal-CoA Synthetase MoPcs60 Is Important for Fatty Acid Metabolism and Infectious Growth of the Rice Blast Fungus.Frontiers in plant science · 2021Article
- Uncovering targeting priority to yeast peroxisomes using an in-cell competition assay.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Current Advances in Protein Import into Peroxisomes.The protein journal · 2019Review
- 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
- 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
- Towards designer organelles by subverting the peroxisomal import pathway.Nature communications · 2017Article
- Peroxisome protein import: a complex journey.Biochemical Society transactions · 2016Review
- Towards repurposing the yeast peroxisome for compartmentalizing heterologous metabolic pathways.Nature communications · 2016Article
Corrections and comments
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Authors and funding
12 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The peroxisomal matrix protein import is facilitated by cycling import receptors that shuttle between the cytosol and the peroxisomal membrane. The import receptor Pex5p mediates the import of proteins harboring a peroxisomal targeting signal of type I (PTS1). Purified recombinant Pex5p forms a dimeric complex with the PTS1-protein Pcs60p in vitro with a KD of 0.19 μm. To analyze the structural basis for receptor-cargo recognition, the PTS1 and adjacent amino acids of Pcs60p were systematically scanned for Pex5p binding by an in vitro site-directed photo-cross-linking approach. The cross-linked binding regions of the receptor were subsequently identified by high resolution mass spectrometry. Most cross-links were found with TPR6, TPR7, as well as the 7C-loop of Pex5p. Surface plasmon resonance analysis revealed a bivalent interaction mode for Pex5p and Pcs60p. Interestingly, Pcs60p lacking its C-terminal tripeptide sequence was efficiently cross-linked to the same regions of Pex5p. The KD value of the interaction of truncated Pcs60p and Pex5p was in the range of 7.7 μm. Isothermal titration calorimetry and surface plasmon resonance measurements revealed a monovalent binding mode for the interaction of Pex5p and Pcs60p lacking the PTS1. Our data indicate that Pcs60p contains a second contact site for its receptor Pex5p, beyond the C-terminal tripeptide. The physiological relevance of the ancillary binding region was supported by in vivo import studies. The bivalent binding mode might be explained by a two-step concept as follows: first, cargo recognition and initial tethering by the PTS1-receptor Pex5p; second, lock-in of receptor and cargo.
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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.