2010 Fiscal Year Final Research Report
Analysis of hepatocarcinogenesis due to monoubiquitylation of gankyrin that is one of the proteasome-interacting proteins
Project/Area Number |
20590773
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Gastroenterology
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Research Institution | Kyoto University |
Principal Investigator |
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Project Period (FY) |
2008 – 2010
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Keywords | プロテアソーム / ガンキリン / モノユビキチン / 肝細胞癌 |
Research Abstract |
Gankyrin is monoubiquitylated at specific lysine residue posttranslationally. However, other ubiquitin like modifiers, that is, NEDD8, SUMO1-4, ISG15, or URM1, does not bind to gankyrin. Monoubiquitylation of oncogenic gankyrin induces hepatic cell transformation more stimulatedly than wild type nonmodified gankyrin posttranslationally. In hepatoma cell lines, monoubiquitylated gankyrin binds to S6 ATPase and MDM2. Nevertheless, monoubiquitylated gankyrin targets more effectively pRB than p53 toward MDM2 E3 lubiquitin ligase activity. Some of gankyrin monoubiquitylation systems consisting of E1, E2, E3, E4, and DUB will become targets of anti-cancer drugs.
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[Journal Article] MDM2 is a novel E3 ligase for HIV-1 Vif.2009
Author(s)
Izumi T, Takaori-Kondo A, Shirakawa K, Higashitsuji H, Itoh K, Io K, Matsui M, Iwai K, Kondoh H, Sato T, Tomonaga M, Ikeda S, Akari H, Koyanagi Y, Fujita J, Uchiyama T.
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Journal Title
Retrovirology 6
Pages: 1-10
Peer Reviewed
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