| Literature DB >> 19246003 |
Isao Fukuda1, Akihiro Ito, Go Hirai, Shinichi Nishimura, Hisashi Kawasaki, Hisato Saitoh, Ken-Ichi Kimura, Mikiko Sodeoka, Minoru Yoshida.
Abstract
Protein modification by small ubiquitin-related modifier proteins (SUMOs) controls diverse cellular functions. Dysregulation of SUMOylation or deSUMOylation processes has been implicated in the development of cancer and neurodegenerative diseases. However, no small-molecule inhibiting protein SUMOylation has been reported so far. Here, we report inhibition of SUMOylation by ginkgolic acid and its analog, anacardic acid. Ginkgolic acid and anacardic acid inhibit protein SUMOylation both in vitro and in vivo without affecting in vivo ubiquitination. Binding assays with a fluorescently labeled probe showed that ginkgolic acid directly binds E1 and inhibits the formation of the E1-SUMO intermediate. These studies will provide not only a useful tool for investigating the roles of SUMO conjugations in a variety of pathways in cells, but also a basis for the development of drugs targeted against diseases involving aberrant SUMOylation.Entities:
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Year: 2009 PMID： 19246003 DOI： 10.1016/j.chembiol.2009.01.009
Source DB: PubMed Journal: Chem Biol ISSN： 1074-5521