2011 Fiscal Year Final Research Report
Mechanism of the proteasome nuclear localization
Project/Area Number |
22657037
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Research Category |
Grant-in-Aid for Challenging Exploratory Research
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Allocation Type | Single-year Grants |
Research Field |
Functional biochemistry
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Research Institution | 財団法人東京都医学総合研究所 (2011) Tokyo Metropolitan Organization for Medical Research (2010) |
Principal Investigator |
SAEKI Yasushi 財団法人東京都医学総合研究所, 生体分子先端研究分野, 主席研究員 (80462779)
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Project Period (FY) |
2010 – 2011
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Keywords | 細胞内タンパク質分解 |
Research Abstract |
The 26S proteasome is a highly organized protease complex that is responsible for targeted protein degradation in both the cytosolic and nuclear compartment. In budding yeast and several cancer cells, it is known that the 26S proteasome is mainly localized in the nucleus. Although several studies have described the mechanism of the nuclear translocation, it is still unclear when the proteasomes enter the nucleus upon their assembly process. Using dual color fluorescence cross correlation spectrometry(FCCS), we determined local concentration and dynamics of the 26S proteasome in living yeast cells. Surprisingly, almost all the proteasome subunits were incorporated into the 26S proteasome in both the cytosol and nucleus. Importantly, the proteasome dynamics was not changed in the importin.(srp1-49) mutant cells in which the 26S proteasome retains the cytosol. These results suggest that the 26S proteasome is fully assembled in the cytoplasm prior to the nuclear translocation.
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Research Products
(23 results)
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[Journal Article] Structural basis for specific recognition of Rpt1p, an ATPase subunit of the 26S proteasome, by the proteasome-dedicated chaperone Hsm3p2012
Author(s)
Takagi, K., Kim, S., Yukii, H., Ueno, M., Morishita, R., Endo, Y., Kato, K., Tanaka, K., Saeki, Y., and Mizushima, Y.
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Journal Title
J Biol Chem
Volume: 287
Pages: 12172-12182
Peer Reviewed
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[Journal Article] Localization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryomicroscopy2012
Author(s)
Sakata, E., Bohn, S., Mihalache, O., Kiss, P., Beck, F., Nagy, I., Nickell, S., Tanaka, K., Saeki, Y., Forster, F., and Baumeister, W.
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Journal Title
Proc Natl Acad Sci USA
Volume: 109
Pages: 1479-1484
Peer Reviewed
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[Journal Article] The catalytic activity of Ubp6 enhances maturation of the proteasomal regulatory particle2011
Author(s)
Sakata, E., Stengel, F., Fukunaga, K., Zhou, M., Saeki, Y., Forster, F., Baumeister, W., Tanaka, K., and Robinson, CV.
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Journal Title
Mol Cell
Volume: 42
Pages: 637-649
Peer Reviewed
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[Journal Article] Sharpin is a component of the NF-κB activating linear ubiquitin chain assembly complex2011
Author(s)
Tokunaga, F., Nakagawa, T., Nakahara1, M., Saeki, Y., Taniguchi, M., Sakata, S., Tanaka, K., Nakano, H., and Iwai, I.
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Journal Title
Nature
Volume: 471
Pages: 633-636
Peer Reviewed
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[Journal Article] Crystal structure of yeast Rpn14, a chaperone of the 19S regulatory particles of the proteasome2010
Author(s)
Kim, S., Saeki, Y., Fukunaga, K., Suzuki, A., Takagi, K., Yamane, T., Tanaka, K., Mizushima, T., and Kato, K.
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Journal Title
J Biol Chem
Volume: 285
Pages: 15159-151566
Peer Reviewed
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[Journal Article] Polyubiquitin conjugation to NEMO by triparite motif protein 23(TRIM23) is critical in antiviral defense2010
Author(s)
Arimoto, K. I., Funami, K., Saeki, Y., Tanaka, K., Okawa, K., Takeuchi, O., Akira, S., Murakami, Y., and Shimotohno, K.
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Journal Title
Proc Natl Acad Sci USA
Volume: 107
Pages: 15856-15861
Peer Reviewed
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[Presentation] The 26S proteasome completes its assembly process in the cytoplasm prior to the nuclear translocation2011
Author(s)
Haruka Yukii, Yasushi Saeki, Changi Pack, Keisuke Fukunaga, Eri Sakata, Yasushi Sako, Akio Toh-e, Wolfgang Baumeister, Keiji Tanaka
Organizer
EMBO Conference, Ubiquitin and ubiquitin-like modifiers
Place of Presentation
Cavtat, Croatia
Year and Date
20110921-25
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