Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-2929
Science 2004 Oct 01;3065693:117-20. doi: 10.1126/science.1100946.
Show Gene links Show Anatomy links

Ubistatins inhibit proteasome-dependent degradation by binding the ubiquitin chain.

Verma R , Peters NR , D'Onofrio M , Tochtrop GP , Sakamoto KM , Varadan R , Zhang M , Coffino P , Fushman D , Deshaies RJ , King RW .


???displayArticle.abstract???
To identify previously unknown small molecules that inhibit cell cycle machinery, we performed a chemical genetic screen in Xenopus extracts. One class of inhibitors, termed ubistatins, blocked cell cycle progression by inhibiting cyclin B proteolysis and inhibited degradation of ubiquitinated Sic1 by purified proteasomes. Ubistatins blocked the binding of ubiquitinated substrates to the proteasome by targeting the ubiquitin-ubiquitin interface of Lys(48)-linked chains. The same interface is recognized by ubiquitin-chain receptors of the proteasome, indicating that ubistatins act by disrupting a critical protein-protein interaction in the ubiquitin-proteasome system.

???displayArticle.pubmedLink??? 15459393
???displayArticle.link??? Science
???displayArticle.grants??? [+]

Species referenced: Xenopus laevis
Genes referenced: ccnb1.2

References :
Bellows, Cell biology. Chemical genetics hits. 2004, Pubmed, Xenbase