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PMID: 15071497 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Cullin-based ubiquitin ligases: Cul3-BTB complexes join the family.

The EMBO journal ·Vol. 23 ·No. 8 ·2004-04-21 ·Pages 1681-7

Pintard L, Willems A, Peter M

Abstract

Cullin-based E3 ligases target substrates for ubiquitin-dependent degradation by the 26S proteasome. The SCF (Skp1-Cul1-F-box) and ECS (ElonginC-Cul2-SOCS box) complexes are so far the best-characterized cullin-based ligases. Their atomic structure has been solved recently, and several substrates have been described in different organisms. In addition to Cul1 and Cul2, higher eucaryotic genomes encode for three other cullins: Cul3, Cul4, and Cul5. Recent results have shed light on the molecular composition and function of Cul3-based E3 ligases. In these complexes, BTB-domain-containing proteins may bridge the cullin to the substrate in a single polypeptide, while Skp1/F-box or ElonginC/SOCS heterodimers fulfill this function in the SCF and ECS complexes. BTB-containing proteins are evolutionary conserved and involved in diverse biological processes, but their function has not previously been linked to ubiquitin-dependent degradation. In this review, we present these new findings and compare the composition of Cul3-based ligases to the well-defined SCF and ECS ligases.

MeSH Terms
Animals Cell Cycle Proteins/chemistry,metabolism Cullin Proteins/chemistry,metabolism Humans Protein Binding Protein Subunits/chemistry,metabolism SKP Cullin F-Box Protein Ligases/chemistry,metabolism Substrate Specificity
Chemicals
CUL3 protein, human Cell Cycle Proteins Cullin Proteins Protein Subunits SKP Cullin F-Box Protein Ligases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Pintard Lionel
Institute of Biochemistry, ETH Hoenggerberg, Zuerich, Switzerland. [email protected]
Willems Andrew
Peter Matthias
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
2004-04-21
Epub
2004-00-08
Pages
1681-7
Language
English
Region
England
NLM ID
8208664
PMCID
PMC394240
Subset
IM
Corrections
ErratumIn
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