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GENES & DEVELOPMENT 20:2949-2954, 2006
©2006 by Cold Spring Harbor Laboratory Press; ISSN 0890-9369/ $5.00
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Research Communication

DDB1 functions as a linker to recruit receptor WD40 proteins to CUL4–ROC1 ubiquitin ligases

Yizhou Joseph He, Chad M. McCall, Jian Hu, Yaxue Zeng, and Yue Xiong1

Lineberger Comprehensive Cancer Center, Department of Biochemistry and Biophysics, Program in Molecular Biology and Biotechnology, University of North Carolina, Chapel Hill, North Carolina 27599, USA

Cullins assemble the largest family of ubiquitin ligases by binding with ROC1 and various substrate receptors. CUL4 function is linked with many cellular processes, but its substrate-recruiting mechanism remains elusive. We identified a protein motif, the DWD box (DDB1-binding WD40 protein), and demonstrated the binding of 15 DWD proteins with DDB1–CUL4A. We provide evidence supporting the critical function of the DWD box and DDB1’s role as the linker mediating DWD protein association with CUL4A. A database search predicts that about one-third of WD40 proteins, 90 in humans, contain the DWD box, suggesting a potentially large number of DWD–DDB1–CUL4–ROC1 E3 ligases.

[Keywords: Ubiquitin; cullin; WD40; DDB1; CUL4; DWD]

Received August 16, 2006; revised version accepted September 15, 2006.

1 Corresponding author.

E-MAIL yxiong{at}email.unc.edu; FAX (919) 966-8799.

Supplemental material is available at http://www.genesdev.org.

Article is online at http://www.genesdev.org/cgi/doi/10.1101/gad.1483206.


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