BTB proteins as henchmen of Cul3-based ubiquitin ligases
W Krek - Nature cell biology, 2003 - nature.com
Nature cell biology, 2003•nature.com
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.
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.
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.
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