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  • Identification of Ubiquitin-specific Protease 9X (USP9X) as a Deubiquitinase Acting on Ubiquitin-Peroxin 5 (PEX5) Thioester Conjugate

    Author(s)
    Grou, Claudia P
    Francisco, Tania
    Rodrigues, Tony A
    Freitas, Marta O
    Pinto, Manuel P
    Carvalho, Andreia F
    Domingues, Pedro
    Wood, Stephen A
    Rodriguez-Borges, Jose E
    Sa-Miranda, Clara
    Fransen, Marc
    Azevedo, Jorge E
    Griffith University Author(s)
    Wood, Stephen A.
    Year published
    2012
    Metadata
    Show full item 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 ...
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    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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    Journal Title
    Journal of Biological Chemistry
    Volume
    287
    Issue
    16
    DOI
    https://doi.org/10.1074/jbc.M112.340158
    Subject
    Biochemistry and Cell Biology not elsewhere classified
    Biological Sciences
    Medical and Health Sciences
    Chemical Sciences
    Publication URI
    http://hdl.handle.net/10072/46986
    Collection
    • Journal articles

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