ArticleThe Journal of biological chemistry2018
Receptor recognition by the peroxisomal AAA complex depends on the presence of the ubiquitin moiety and is mediated by Pex1p.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Structure of the peroxisomal Pex1/Pex6 ATPase complex bound to a substrate.Nature communications · 2023Article
- Insights into the Structure and Function of the Pex1/Pex6 AAA-ATPase in Peroxisome Homeostasis.Cells · 2022Review
- Balancing the Opposing Principles That Govern Peroxisome Homeostasis.Trends in biochemical sciences · 2021Review
- The selectivity filter of the mitochondrial protein import machinery.BMC biology · 2020Article
- Mitotic phosphorylation of Pex14p regulates peroxisomal import machinery.The Journal of cell biology · 2020Article
- Membrane Processing and Steady-State Regulation of the Alternative Peroxisomal Import Receptor Pex9p.Frontiers in cell and developmental biology · 2020Article
- 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 biogenesis, membrane contact sites, and quality control.EMBO reports · 2019Review
- Chemically monoubiquitinated PEX5 binds to the components of the peroxisomal docking and export machinery.Scientific reports · 2018Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The receptor cycle of type I peroxisomal matrix protein import is completed by ubiquitination of the membrane-bound peroxisome biogenesis factor 5 (Pex5p) and its subsequent export back to the cytosol. The receptor export is the only ATP-dependent step of the whole process and is facilitated by two members of the AAA family of proteins (ATPases associated with various cellular activities), namely Pex1p and Pex6p. To gain further insight into substrate recognition by the AAA complex, we generated an N-terminally linked ubiquitin-Pex5p fusion protein. This fusion protein displayed biological activity because it is able to functionally complement a PEX5-deletion in
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