2014 Fiscal Year Final Research Report
Regulatory mechanism of p53 deubiquitinating enzyme USP7
Project/Area Number |
25830078
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Multi-year Fund |
Research Field |
Tumor biology
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Research Institution | Nagoya University |
Principal Investigator |
KATO Takuya 名古屋大学, 医学(系)研究科(研究院), 特任助教 (00551970)
|
Project Period (FY) |
2013-04-01 – 2015-03-31
|
Keywords | USP7 / RFP |
Outline of Final Research Achievements |
We found that a SUMO E3 ligase RFP and de-ubiquitiantion enzyme USP7 stabilise p53 protein through their interaction. USP7 contribute to the stabilisation of RFP and stabilised RFP SUMOylate p53 at lysine 386 residue. We further showed that both USP7 and RFP confer cancer cells resistance to UV-induced apoptosis in a p53 expression dependent manner. These data suggest that USP7 and RFP increase the cell survival during DNA damage by stabilising p53 protein.
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Free Research Field |
腫瘍生物学
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