Devolopment of a novel method to identify E3 ligase substrates
Project/Area Number |
15K15058
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Research Category |
Grant-in-Aid for Challenging Exploratory Research
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Allocation Type | Multi-year Fund |
Research Field |
General medical chemistry
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Research Institution | Hokkaido University |
Principal Investigator |
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Project Period (FY) |
2015-04-01 – 2017-03-31
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Project Status |
Completed (Fiscal Year 2016)
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Budget Amount *help |
¥3,640,000 (Direct Cost: ¥2,800,000、Indirect Cost: ¥840,000)
Fiscal Year 2016: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2015: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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Keywords | ユビキチン / ユビキチンリガーゼ |
Outline of Final Research Achievements |
Since ubiquitin ligase (E3) has the substrate specificity of ubiquitination, identifications of specific substrates of each E3 enzymes and of their ubiquitination sites are important for understanding various biological phenomena. In recent years, Toczyski and colleagues have proposed a ligase trap method using a fusion probe of an ubiquitin-binding domain (UBA) and an E3, and Yoshida and colleagues have proposed a TR-TUBE method combining Tandem Ubiquitin Binding Entity (TUBE) and K-εGG-specific antibody. We attempted to develop a more advanced substrate identification method by adding some improvements in their methods and succeeded in improving the sensitivity. By using this method, it is expected that the functional analysis of E3 would be accelerated.
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Report
(3 results)
Research Products
(12 results)
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[Journal Article] The novel heart-specific RING finger protein 207 is involved in energy metabolism in cardiomyocytes.2016
Author(s)
Mizushima, W., Takahashi , H., Watanabe, M., Kinugawa, S., Matsushima, S., Takada, S., Yokota, T., Furihata, T., Matsumoto, J., Tsuda, M., Chiba, I., Nagashima, S., Yanagi, S., Matsumoto, M., Nakayama, K.I., Tsutsui, H. and Hatakeyama, S.
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Journal Title
J. Mol. Cell. Cardiol.
Volume: 100
Pages: 43-53
DOI
NAID
Related Report
Peer Reviewed / Int'l Joint Research / Acknowledgement Compliant
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[Journal Article] p53 represses the transcription of snRNA genes by preventing the formation of little elongation complex2016
Author(s)
Anwar, D., Takahashia, H., Watanabe, M., Suzuki, M., Fukuda, S., Hatakeyama, S.
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Journal Title
Biochim. Biophys. Acta-Gene Regul. Mech.
Volume: 1859
Issue: 8
Pages: 975-982
DOI
NAID
Related Report
Peer Reviewed / Acknowledgement Compliant
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[Journal Article] The E3 ubiquitin ligase TRIM23 regulates adipocyte differentiation via stabilization of the adipocyte activator PPAR gamma.2015
Author(s)
Watanabe, M., Takahashi, H., Saeki, Y., Ozaki, T., Itoh, S., Suzuki, M., Mizushima, W., Tanaka, K. and Hatakeyama, S.
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Journal Title
DOI
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
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