Overview:

DDB1, or DNA damage-binding protein 1, is a crucial component of the CUL4-RING E3 ubiquitin ligase (CRL4) complex, playing a central role in DNA repair, cell cycle regulation and chromatin remodeling. The CRL4-DDB1 complex is involved in the ubiquitin-mediated proteolysis of target proteins, thereby regulating their stability and influencing diverse cellular functions. DDB1 was initially identified for its ability to bind to DNA lesions induced by UV radiation, and it was later found to be a key adaptor protein that links CUL4A/B scaffold proteins to the substrate receptor DDB2. This interaction facilitates the recruitment of specific target proteins to the CRL4 complex for ubiquitination and subsequent degradation. DDB1 has also been implicated in the recognition and repair of various types of DNA damage, including UV-induced lesions and DNA interstrand crosslinks.

Genbank Number:

Q16531

References:

1. Sugasawa K, Okuda Y, Saijo M, et al. UV-induced ubiquitylation of XPC protein mediated by UV-DDB-ubiquitin ligase complex. Cell. 2005;121(3):387-400.
2. He YJ, McCall CM, Hu J, et al. DDB1 functions as a linker to recruit receptor WD40 proteins to CUL4-ROC1 ubiquitin ligases. Genes Dev. 2006;20(21):2949-2954.
3. Jin J, Arias EE, Chen J, Harper JW, Walter JC. A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1. Mol Cell. 2006;23(5):709-721.