2015 Fiscal Year Final Research Report
Regulation of heme oxygenase activity by posttranslational modification
| Project/Area Number |
25440056
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Functional biochemistry
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| Research Institution | Kurume University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
MATSUI Takanori 久留米大学, 医学部, 講師 (10425233)
TAIRA Junichi 九州工業大学, 情報工学部, 助教 (20549612)
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| Project Period (FY) |
2013-04-01 – 2016-03-31
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| Keywords | ヘムオキシゲナーゼ / 翻訳後修飾 |
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| Outline of Final Research Achievements |
We investigated the cellular mechanism underlying the degradation of heme oxygenase-1 (HO-1). 1) The turnover of HO-1 induced in HEK293 was significantly attenuated by proteasome inhibitors, suggesting the involvement of a proteasome-mediated pathway. 2) High molecular weight ubiquitin conjugates were co-immunoprecipitated with HO-1 from HEK293 after proteasome inhibition. 3) HO-1 ubiquitination in HEK293 cells was enhanced by zinc chloride, but suppressed with a zinc chelator, suggesting the involvement of a RING-E3 ligase in this process. 4) We identified TRC8 as the E3 ligase responsible for HO ubiquitination and degradation using mass spectrometry, yeast two-hybrid assay and cDNA array.
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| Free Research Field |
生化学
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