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Golgi organization is regulated by proteasomal degradation

Author

Listed:
  • Avital Eisenberg-Lerner

    (Weizmann Institute of Science)

  • Ron Benyair

    (Weizmann Institute of Science)

  • Noa Hizkiahou

    (Weizmann Institute of Science)

  • Neta Nudel

    (Weizmann Institute of Science)

  • Roey Maor

    (Weizmann Institute of Science)

  • Matthias P. Kramer

    (Weizmann Institute of Science)

  • Merav D. Shmueli

    (Weizmann Institute of Science)

  • Inbal Zigdon

    (Weizmann Institute of Science)

  • Marina Cherniavsky Lev

    (Weizmann Institute of Science)

  • Adi Ulman

    (Weizmann Institute of Science)

  • Jitka Yehudith Sagiv

    (Weizmann Institute of Science)

  • Molly Dayan

    (Weizmann Institute of Science)

  • Bareket Dassa

    (Weizmann Institute of Science)

  • Mercedes Rosenwald

    (Weizmann Institute of Science)

  • Idit Shachar

    (Weizmann Institute of Science)

  • Jie Li

    (University of Michigan)

  • Yanzhuang Wang

    (University of Michigan)

  • Nili Dezorella

    (Weizmann Institute of Science)

  • Suman Khan

    (Weizmann Institute of Science)

  • Ziv Porat

    (Weizmann Institute of Science)

  • Eyal Shimoni

    (Weizmann Institute of Science)

  • Ori Avinoam

    (Weizmann Institute of Science)

  • Yifat Merbl

    (Weizmann Institute of Science)

Abstract

The Golgi is a dynamic organelle whose correct assembly is crucial for cellular homeostasis. Perturbations in Golgi structure are associated with numerous disorders from neurodegeneration to cancer. However, whether and how dispersal of the Golgi apparatus is actively regulated under stress, and the consequences of Golgi dispersal, remain unknown. Here we demonstrate that 26S proteasomes are associated with the cytosolic surface of Golgi membranes to facilitate Golgi Apparatus-Related Degradation (GARD) and degradation of GM130 in response to Golgi stress. The degradation of GM130 is dependent on p97/VCP and 26S proteasomes, and required for Golgi dispersal. Finally, we show that perturbation of Golgi homeostasis induces cell death of multiple myeloma in vitro and in vivo, offering a therapeutic strategy for this malignancy. Taken together, this work reveals a mechanism of Golgi-localized proteasomal degradation, providing a functional link between proteostasis control and Golgi architecture, which may be critical in various secretion-related pathologies.

Suggested Citation

  • Avital Eisenberg-Lerner & Ron Benyair & Noa Hizkiahou & Neta Nudel & Roey Maor & Matthias P. Kramer & Merav D. Shmueli & Inbal Zigdon & Marina Cherniavsky Lev & Adi Ulman & Jitka Yehudith Sagiv & Moll, 2020. "Golgi organization is regulated by proteasomal degradation," Nature Communications, Nature, vol. 11(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-019-14038-9
    DOI: 10.1038/s41467-019-14038-9
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    Cited by:

    1. Yannick Weyer & Sinead I. Schwabl & Xuechen Tang & Astha Purwar & Konstantin Siegmann & Angela Ruepp & Theresia Dunzendorfer-Matt & Michael A. Widerin & Veronika Niedrist & Noa J. M. Mutsters & Maria , 2024. "The Dsc ubiquitin ligase complex identifies transmembrane degrons to degrade orphaned proteins at the Golgi," Nature Communications, Nature, vol. 15(1), pages 1-19, December.
    2. Wiebke Sachs & Lukas Blume & Desiree Loreth & Lisa Schebsdat & Favian Hatje & Sybille Koehler & Uta Wedekind & Marlies Sachs & Stephanie Zieliniski & Johannes Brand & Christian Conze & Bogdan I. Flore, 2024. "The proteasome modulates endocytosis specifically in glomerular cells to promote kidney filtration," Nature Communications, Nature, vol. 15(1), pages 1-21, December.

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