ArticleThe Journal of biological chemistry2012
Identification of ubiquitin-specific protease 9X (USP9X) as a deubiquitinase acting on ubiquitin-peroxin 5 (PEX5) thioester conjugate.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 99 citations in OpenAlex.
- PEX39 facilitates the peroxisomal import of PTS2-containing proteins.Nature cell biology · 2025Article
- Import mechanism of peroxisomal proteins with an N-terminal signal sequence.Nature cell biology · 2025Article
- Towards solving the mystery of peroxisomal matrix protein import.Trends in cell biology · 2024Review
- Mammalian pexophagy at a glance.Journal of cell science · 2024Review
- Noncanonical and reversible cysteine ubiquitination prevents the overubiquitination of PEX5 at the peroxisomal membrane.PLoS biology · 2024Article
- Roles of USP9X in cellular functions and tumorigenesis (Review).Oncology letters · 2023Review
- A Cell-Free In Vitro Import System for Peroxisomal Proteins Containing a Type 2 Targeting Signal (PTS2).Methods in molecular biology (Clifton, N.J.) · 2023Article
- Deciphering non-canonical ubiquitin signaling: biology and methodology.Frontiers in molecular biosciences · 2023Review
- Protein import into peroxisomes occurs through a nuclear pore-like phase.Science (New York, N.Y.) · 2022Article
- PEX5 translocation into and out of peroxisomes drives matrix protein import.Molecular cell · 2022Article
- Insights into the Structure and Function of the Pex1/Pex6 AAA-ATPase in Peroxisome Homeostasis.Cells · 2022Review
- Peroxisomal Stress Response and Inter-Organelle Communication in Cellular Homeostasis and Aging.Antioxidants (Basel, Switzerland) · 2022Review
- Non-lysine ubiquitylation: Doing things differently.Frontiers in molecular biosciences · 2022Review
- A missense allele of PEX5 is responsible for the defective import of PTS2 cargo proteins into peroxisomes.Human genetics · 2021Article
- Emerging Role of Ubiquitination in the Regulation of PD-1/PD-L1 in Cancer Immunotherapy.Molecular therapy : the journal of the American Society of Gene Therapy · 2021Review
- Balancing the Opposing Principles That Govern Peroxisome Homeostasis.Trends in biochemical sciences · 2021Review
- Pexophagy: A Model for Selective Autophagy.International journal of molecular sciences · 2020Review
- Peroxisome: Metabolic Functions and Biogenesis.Advances in experimental medicine and biology · 2020Review
- Cellular functions and molecular mechanisms of non-lysine ubiquitination.Open biology · 2019Review
- Overexpression of the Ubiquitin-Specific Peptidase 9 X-Linked (USP9X) Gene is Associated with Upregulation of Cyclin D1 (CCND1) and Downregulation of Cyclin-Dependent Inhibitor Kinase 1A (CDKN1A) in Breast Cancer Tissue and Cell Lines.Medical science monitor : international medical journal of experimental and clinical research · 2019Article
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Authors and funding
12 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peroxin 5 (PEX5), the peroxisomal protein shuttling receptor, binds newly synthesized peroxisomal matrix proteins in the cytosol and promotes their translocation across the organelle membrane. During the translocation step, PEX5 itself becomes inserted into the peroxisomal docking/translocation machinery. PEX5 is then monoubiquitinated at a conserved cysteine residue and extracted back into the cytosol in an ATP-dependent manner. We have previously shown that the ubiquitin-PEX5 thioester conjugate (Ub-PEX5) released into the cytosol can be efficiently disrupted by physiological concentrations of glutathione, raising the possibility that a fraction of Ub-PEX5 is nonenzymatically deubiquitinated in vivo. However, data suggesting that Ub-PEX5 is also a target of a deubiquitinase were also obtained in that work. Here, we used an unbiased biochemical approach to identify this enzyme. Our results suggest that ubiquitin-specific protease 9X (USP9X) is by far the most active deubiquitinase acting on Ub-PEX5, both in female rat liver and HeLa cells. We also show that USP9X is an elongated monomeric protein with the capacity to hydrolyze thioester, isopeptide, and peptide bonds. The strategy described here will be useful in identifying deubiquitinases acting on other ubiquitin conjugates.
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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.