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A proteolytic system that compensates for loss of proteasome function

Author

Listed:
  • Rickard Glas

    (Center for Cancer Research, Massachusetts Institute of Technology
    Harvard Medical School)

  • Matthew Bogyo

    (Center for Cancer Research, Massachusetts Institute of Technology
    Harvard Medical School)

  • John S. McMaster

    (Center for Cancer Research, Massachusetts Institute of Technology
    University of Utah Department of Biochemistry)

  • Maria Gaczynska

    (Center for Cancer Research, Massachusetts Institute of Technology
    Univesity of Texas Health Science Center)

  • Hidde L. Ploegh

    (Center for Cancer Research, Massachusetts Institute of Technology
    Harvard Medical School)

Abstract

Proteolysis is essential for the execution of many cellular functions. These include removal of incorrectly folded or damaged proteins1, the activation of transcription factors2, the ordered degradation of proteins involved in cell cycle control3, and the generation of peptides destined for presentation by class I molecules of the major histocompatibility complex4. A multisubunit protease complex, the proteasome5, accomplishes these tasks. Here we show that in mammalian cells inactivation of the proteasome by covalent inhibitors allows the outgrowth of inhibitor-resistant cells. The growth of such adapted cells is apparently maintained by the induction of other proteolytic systems that compensate for the loss of proteasomal activity.

Suggested Citation

  • Rickard Glas & Matthew Bogyo & John S. McMaster & Maria Gaczynska & Hidde L. Ploegh, 1998. "A proteolytic system that compensates for loss of proteasome function," Nature, Nature, vol. 392(6676), pages 618-622, April.
    • Handle: RePEc:nat:nature:v:392:y:1998:i:6676:d:10.1038_33443
    DOI: 10.1038/33443
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    Cited by:

    1. Liam C. Hunt & Vishwajeeth Pagala & Anna Stephan & Boer Xie & Kiran Kodali & Kanisha Kavdia & Yong-Dong Wang & Abbas Shirinifard & Michelle Curley & Flavia A. Graca & Yingxue Fu & Suresh Poudel & Yuxi, 2023. "An adaptive stress response that confers cellular resilience to decreased ubiquitination," Nature Communications, Nature, vol. 14(1), pages 1-22, December.

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