News and Views


Nature Cell Biology 5, 950 - 951 (2003)
doi:10.1038/ncb1103-950

BTB proteins as henchmen of Cul3-based ubiquitin ligases

Wilhelm Krek1

  1. Wilhelm Krek is in the Institute of Cell Biology, ETH-Hönggerberg, CH-8093 Zurich, Switzerland. e-mail: wilhelm.krek@cell.biol.ethz.ch


The choice of ubiquitination substrates of Cul1- and Cul2-based E3 ubiquitin protein ligase complexes is dictated by the identity of their substrate-specific adaptors, known as F-box and BC-box proteins, respectively. Recent work suggests that members of the large family of BTB-domain proteins define a new class of substrate-specific adaptors of Cul3-based E3 complexes. This finding places many signalling pathways in which BTB-domain proteins participate under direct control of the ubiquitination pathway.

Top


MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated

REVIEWS
Nedd8 on cullin: building an expressway to protein destruction
Oncogene Reviews (15 Mar 2004)
 See all 7 matches for Reviews

NEWS AND VIEWS
VHL takes HIF's breath away
Nature Cell Biology News and Views (01 Jul 2000)
Cdc34: cycling on and off the SCF
Nature Cell Biology News and Views (01 Oct 2003)
 See all 3 matches for News And Views

RESEARCH
BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3
Nature Letters to Editor (18 Sep 2003)
The BTB protein MEL-26 is a substrate-specific adaptor of the CUL-3 ubiquitin-ligase
Nature Letters to Editor (18 Sep 2003)
 See all 13 matches for Research


Extra navigation

Subscribe to Nature Cell Biology

Subscribe

Search PubMed for

Open Innovation Challenges

naturejobs