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The proteasome antechamber maintains substrates in an unfolded state

Author

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  • Amy M. Ruschak

    (Biochemistry and Chemistry, The University of Toronto, Toronto, Ontario M5S 1A8, Canada)

  • Tomasz L. Religa

    (Biochemistry and Chemistry, The University of Toronto, Toronto, Ontario M5S 1A8, Canada)

  • Sarah Breuer

    (Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany)

  • Susanne Witt

    (Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany)

  • Lewis E. Kay

    (Biochemistry and Chemistry, The University of Toronto, Toronto, Ontario M5S 1A8, Canada)

Abstract

Proteasome antechamber hosts unfolded proteins The proteasome is a multi-protein complex that degrades proteins enzymatically. Proteolysis occurs in a barrel-shaped 20S core particle comprising three interconnected cavities, including a pair of antechambers in which substrates are held before degradation. In this study, Lewis Kay and colleagues demonstrate that substrates interact actively with the antechamber walls, and that the environment in this compartment is optimized to maintain the substrate in an unfolded 'ready to eat' state, easily accessible for hydrolysis.

Suggested Citation

  • Amy M. Ruschak & Tomasz L. Religa & Sarah Breuer & Susanne Witt & Lewis E. Kay, 2010. "The proteasome antechamber maintains substrates in an unfolded state," Nature, Nature, vol. 467(7317), pages 868-871, October.
    • Handle: RePEc:nat:nature:v:467:y:2010:i:7317:d:10.1038_nature09444
    DOI: 10.1038/nature09444
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    Cited by:

    1. Wai Tuck Soh & Hanna P. Roetschke & John A. Cormican & Bei Fang Teo & Nyet Cheng Chiam & Monika Raabe & Ralf Pflanz & Fabian Henneberg & Stefan Becker & Ashwin Chari & Haiyan Liu & Henning Urlaub & Ju, 2024. "Protein degradation by human 20S proteasomes elucidates the interplay between peptide hydrolysis and splicing," Nature Communications, Nature, vol. 15(1), pages 1-25, December.

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