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2014 Fiscal Year Final Research Report

Regulatory mechanism of p53 deubiquitinating enzyme USP7

Research Project

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Project/Area Number 25830078
Research Category

Grant-in-Aid for Young Scientists (B)

Allocation TypeMulti-year Fund
Research Field Tumor biology
Research InstitutionNagoya 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
KeywordsUSP7 / 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.

Free Research Field

腫瘍生物学

URL: 

Published: 2016-06-03  

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