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Quantitative live-cell imaging reveals spatio-temporal dynamics and cytoplasmic assembly of the 26S proteasome

Author

Listed:
  • Chan-Gi Pack

    (Cellular Informatics Laboratory, RIKEN, 2-1 Hirosawa, Wako)

  • Haruka Yukii

    (Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku)

  • Akio Toh-e

    (Medical Mycology Center, Chiba University, 1-8-1 Inohana)

  • Tai Kudo

    (Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku)

  • Hikaru Tsuchiya

    (Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku)

  • Ai Kaiho

    (Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku)

  • Eri Sakata

    (Max-Planck-Institute of Biochemistry)

  • Shigeo Murata

    (Laboratory of Protein Metabolism, Graduate School of Pharmaceutical Sciences, the University of Tokyo, 7-3-1 Hongo, Bunkyo-ku)

  • Hideyoshi Yokosawa

    (School of Pharmacy, Aichi Gakuin University, 1-100 Kusumoto-cho, Chikusa-ku)

  • Yasushi Sako

    (Cellular Informatics Laboratory, RIKEN, 2-1 Hirosawa, Wako)

  • Wolfgang Baumeister

    (Max-Planck-Institute of Biochemistry)

  • Keiji Tanaka

    (Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku)

  • Yasushi Saeki

    (Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku)

Abstract

The 26S proteasome is a 2.5-MDa multisubunit protease complex that degrades polyubiquitylated proteins. Although its functions and structure have been extensively characterized, little is known about its dynamics in living cells. Here, we investigate the absolute concentration, spatio-temporal dynamics and complex formation of the proteasome in living cells using fluorescence correlation spectroscopy. We find that the 26S proteasome complex is highly mobile, and that almost all proteasome subunits throughout the cell are stably incorporated into 26S proteasomes. The interaction between 19S and 20S particles is stable even in an importin-α mutant, suggesting that the 26S proteasome is assembled in the cytoplasm. Furthermore, a genetically stabilized 26S proteasome mutant is able to enter the nucleus. These results suggest that the 26S proteasome completes its assembly process in the cytoplasm and translocates into the nucleus through the nuclear pore complex as a holoenzyme.

Suggested Citation

  • Chan-Gi Pack & Haruka Yukii & Akio Toh-e & Tai Kudo & Hikaru Tsuchiya & Ai Kaiho & Eri Sakata & Shigeo Murata & Hideyoshi Yokosawa & Yasushi Sako & Wolfgang Baumeister & Keiji Tanaka & Yasushi Saeki, 2014. "Quantitative live-cell imaging reveals spatio-temporal dynamics and cytoplasmic assembly of the 26S proteasome," Nature Communications, Nature, vol. 5(1), pages 1-10, May.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms4396
    DOI: 10.1038/ncomms4396
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    Cited by:

    1. Eshita Das & Linh Le & Vladyslava Sokolova & James D. Orth & Soyeon Park, 2025. "Spatial mechanisms of quality control during chaperone-mediated assembly of the proteasome," Nature Communications, Nature, vol. 16(1), pages 1-17, December.
    2. Mireia Casasampere & Hector Carneros & Tania Roda & Alice Zuin & Núria Gallisà-Suñé & Alba González-Artero & Bernat Coll-Martínez & José Luis Abad & Abdulateef Alqahtani & Josefina Casas & Patricia Fe, 2026. "Expanding the targeted protein degradation approach with small molecule chimeras directed to the 26S proteasome," Nature Communications, Nature, vol. 17(1), pages 1-16, December.
    3. Hanna L. Brunner & Robert W. Kalis & Lorenz Grundmann & Zuzana Hodáková & Zuzana Koskova & Irina Grishkovskaya & Melanie de Almeida & Matthias Hinterndorfer & Hannah Knaudt & Simon Höfflin & Florian A, 2026. "A multivalent adaptor mechanism drives the nuclear import of proteasomes," Nature Communications, Nature, vol. 17(1), pages 1-17, December.

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