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pubmed-article:14528312pubmed:dateCreated2003-10-31lld:pubmed
pubmed-article:14528312pubmed:abstractTextThe concentrations and functions of many cellular proteins are regulated by the ubiquitin pathway. Cullin family proteins bind with the RING-finger protein Roc1 to recruit the ubiquitin-conjugating enzyme (E2) to the ubiquitin ligase complex (E3). Cul1 and Cul7, but not other cullins, bind to an adaptor protein, Skp1. Cul1 associates with one of many F-box proteins through Skp1 to assemble various SCF-Roc1 E3 ligases that each selectively ubiquitinate one or more specific substrates. Here, we show that Cul3, but not other cullins, binds directly to multiple BTB domains through a conserved amino-terminal domain. In vitro, Cul3 promoted ubiquitination of Caenorhabditis elegans MEI-1, a katanin-like protein whose degradation requires the function of both Cul3 and BTB protein MEL-26. We suggest that in vivo there exists a potentially large number of BCR3 (BTB-Cul3-Roc1) E3 ubiquitin ligases.lld:pubmed
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pubmed-article:14528312pubmed:monthNovlld:pubmed
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pubmed-article:14528312pubmed:authorpubmed-author:XiongYueYlld:pubmed
pubmed-article:14528312pubmed:authorpubmed-author:FurukawaManab...lld:pubmed
pubmed-article:14528312pubmed:authorpubmed-author:BorchersChris...lld:pubmed
pubmed-article:14528312pubmed:authorpubmed-author:HeYizhou...lld:pubmed
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pubmed-article:14528312pubmed:pagination1001-7lld:pubmed
pubmed-article:14528312pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:14528312pubmed:year2003lld:pubmed
pubmed-article:14528312pubmed:articleTitleTargeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases.lld:pubmed
pubmed-article:14528312pubmed:affiliationLineberger Comprehensive Cancer Center, Department of Biochemistry and Biophysics, and Program in Molecular Biology and Biotechnology, University of North Carolina at Chapel Hill, NC 27599-7295, USA.lld:pubmed
pubmed-article:14528312pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:14528312pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:14528312pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed
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