BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3

Lai Xu, Yue Wei, Jerome Reboul, Philippe Vaglio, Tae-Ho Shin, Marc Vidal, Stephen J. Elledge and J. Wade Harper ()
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Lai Xu: Baylor College of Medicine
Yue Wei: Baylor College of Medicine
Jerome Reboul: Harvard Medical School
Philippe Vaglio: Harvard Medical School
Tae-Ho Shin: Baylor College of Medicine
Marc Vidal: Harvard Medical School
Stephen J. Elledge: Baylor College of Medicine
J. Wade Harper: Baylor College of Medicine

Nature, 2003, vol. 425, issue 6955, 316-321

Abstract: Abstract Programmed destruction of regulatory proteins through the ubiquitin–proteasome system is a widely used mechanism for controlling signalling pathways1,2. Cullins3 are proteins that function as scaffolds for modular ubiquitin ligases typified by the SCF (Skp1–Cul1–F-box) complex4,5,6. The substrate selectivity of these E3 ligases is dictated by a specificity module that binds cullins. In the SCF complex, this module is composed of Skp1, which binds directly to Cul1, and a member of the F-box family of proteins4,5,6,7. F-box proteins bind Skp1 through the F-box motif7, and substrates by means of carboxy-terminal protein interaction domains1,2,5. Similarly, Cul2 and Cul5 interact with BC-box-containing specificity factors through the Skp1-like protein elongin C2. Cul3 is required for embryonic development in mammals and Caenorhabditis elegans8,9,10 but its specificity module is unknown. Here we report the identification of a large family of BTB-domain proteins as substrate-specific adaptors for C. elegans CUL-3. Biochemical studies using the BTB protein MEL-26 and its genetic target MEI-1 (refs 12, 13) indicate that BTB proteins merge the functional properties of Skp1 and F-box proteins into a single polypeptide.

Date: 2003
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DOI: 10.1038/nature01985

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