期刊
SCIENCE
卷 306, 期 5693, 页码 117-120出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1100946
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资金
- NCI NIH HHS [CA78048, P50 CA92131, R21CA108545] Funding Source: Medline
- NIGMS NIH HHS [GM66492, GM65334, R01 GM-45335, GM068276] Funding Source: Medline
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.
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