Detecting UV-lesions in the genome: The modular CRL4 ubiquitin ligase does it best!

Abstract

The DDB1-DDB2-CUL4-RBX1 complex serves as the primary detection device for UV-induced lesions in the genome. It simultaneously functions as a CUL4 type E3 ubiquitin ligase. We review the current understanding of this dual function ubiquitin ligase and damage detection complex. The DDB2 damage binding module is merely one of a large family of possible DDB1-CUL4 associated factors (DCAF), most of which are substrate receptors for other DDB1-CUL4 complexes. DDB2 and the Cockayne-syndrome A protein (CSA) function in nucleotide excision repair, whereas the remaining receptors operate in a wide range of other biological pathways. We will examine the modular architecture of DDB1-CUL4 in complex with DDB2, CSA and CDT2 focusing on shared architectural, targeting and regulatory principles.

• Authors: Andrea Scrima, Eric S Fischer, Gondichatnahalli M Lingaraju, Kerstin Böhm, Simone Cavadini, Nicolas H Thomä
• Journal: FEBS letters (FEBS Lett) Vol. 585 Issue 18 Pg. 2818-25 (Sep 16 2011) ISSN: 1873-3468 [Electronic] England
• PMID: 21550341 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)
• Copyright: Copyright © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Chemical References

• CUL4A protein, human
• Cullin Proteins
• DDB1 protein, human
• DDB2 protein, human
• DNA-Binding Proteins
• DTL protein, human
• ERCC8 protein, human
• Nuclear Proteins
• Transcription Factors
• Ubiquitin-Protein Ligases
• DNA Repair Enzymes

Topics

• Cullin Proteins (metabolism)
• DNA Damage
• DNA Repair
• DNA Repair Enzymes (metabolism)
• DNA-Binding Proteins (metabolism)
• Genome, Human (genetics, radiation effects)
• Humans
• Models, Genetic
• Nuclear Proteins (metabolism)
• Transcription Factors (metabolism)
• Ubiquitin-Protein Ligases (metabolism)
• Ultraviolet Rays