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

Pack, C.-G., Yukii, H., Toh-e, A., Kudo, T., Tsuchiya, H., Kaiho, A., et al. (2014). Quantitative live-cell imaging reveals spatio-temporal dynamics and cytoplasmic assembly of the 26S proteasome. NATURE COMMUNICATIONS, 5: 3396. doi:10.1038/ncomms4396.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-8B80-1 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-8B81-0
Genre: Journal Article

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 Creators:
Pack, Chan-Gi1, Author
Yukii, Haruka1, Author
Toh-e, Akio1, Author
Kudo, Tai1, Author
Tsuchiya, Hikaru1, Author
Kaiho, Ai1, Author
Sakata, Eri2, Author              
Murata, Shigeo1, Author
Yokosawa, Hideyoshi1, Author
Sako, Yasushi1, Author
Baumeister, Wolfgang2, Author              
Tanaka, Keiji1, Author
Saeki, Yasushi1, Author
Affiliations:
1external, ou_persistent22              
2Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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Free keywords: FLUORESCENCE FLUCTUATION SPECTROSCOPY; NUCLEAR-PORE COMPLEX; REGULATORY PARTICLE; SACCHAROMYCES-CEREVISIAE; LIVING CELLS; YEAST-CELLS; LOCALIZATION; UBIQUITIN; PATHWAY; TRANSCRIPTION
 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-alpha 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.

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Language(s): eng - English
 Dates: 2014-03
 Publication Status: Published online
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: ISI: 000334298400001
DOI: 10.1038/ncomms4396
 Degree: -

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Title: NATURE COMMUNICATIONS
Source Genre: Journal
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Publ. Info: MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND : NATURE PUBLISHING GROUP
Pages: - Volume / Issue: 5 Sequence Number: 3396 Start / End Page: - Identifier: ISSN: 2041-1723