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The BTB protein MEL-26 is a substrate-specific adaptor of the CUL-3 ubiquitin-ligase | | Lionel Pintard
; John H Willis
; Andrew Willems
; Jacque-Lynne F Johnson
; Martin Srayko
; Thimo Kurz
; Sarah Glaser
; Paul E Mains
; Mike Tyers
; Bruce Bowerman
; Matthias Peter
; | | Date: |
18 Sep 2003 | | Journal: | Nature, 425 (6955), 311-6 | | Abstract: | Many biological processes, such as development and cell cycle progression are tightly controlled by selective ubiquitin-dependent degradation of key substrates. In this pathway, the E3-ligase recognizes the substrate and targets it for degradation by the 26S proteasome. The SCF (Skp1-Cul1-F-box) and ECS (Elongin C-Cul2-SOCS box) complexes are two well-defined cullin-based E3-ligases. The cullin subunits serve a scaffolding function and interact through their C terminus with the RING-finger-containing protein Hrt1/Roc1/Rbx1, and through their N terminus with Skp1 or Elongin C, respectively. In Caenorhabditis elegans, the ubiquitin-ligase activity of the CUL-3 complex is required for degradation of the microtubule-severing protein MEI-1/katanin at the meiosis-to-mitosis transition. However, the molecular composition of this cullin-based E3-ligase is not known. Here we identified the BTB-containing protein MEL-26 as a component required for degradation of MEI-1 in vivo. Importantly, MEL-26 specifically interacts with CUL-3 and MEI-1 in vivo and in vitro, and displays properties of a substrate-specific adaptor. Our results suggest that BTB-containing proteins may generally function as substrate-specific adaptors in Cul3-based E3-ubiquitin ligases. | | Source: | PubMed, pmid13679921 doi: 10.1038/nature01959 | | Services: | Forum | Review | Favorites | |
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