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

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Affiliations

  • 1. Department of Biology, Howard Hughes Medical Institute (HHMI), California Institute of Technology, Pasadena, CA 91125, USA.
      Authors
    • Verma R 1
    (1 author)

ORCIDs linked to this article

Science, 01 Oct 2004, 306(5693):117-120
https://doi.org/10.1126/science.1100946 PMID: 15459393 

This article has been corrected. See Science. 2008 May 16;320(5878):874. A comment on this article appears in "Cell biology. Chemical genetics hits." Science. 2004 Oct 1;306(5693):67-8.

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.

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Read article at publisher's site: https://doi.org/10.1126/science.1100946

Read article for free, from open access legal sources, via Unpaywall: https://authors.library.caltech.edu/51961/13/Verma_2008p874.pdfUnpaywall

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Funding 

Funders who supported this work.

NCI NIH HHS (3)

NIGMS NIH HHS (4)