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Updated: Jul 1, 2026

In vivo and in vitro Studies of Adaptor-clathrin Interaction
Published on: January 26, 2011
Schizosaccharomyces pombe Ddb1 recruits substrate-specific adaptor proteins through a novel protein motif, the
Yasunori Fukumoto1, Naoshi Dohmae, Fumio Hanaoka
1Faculty of Science, Gakushuin University, 1-5-1 Mejiro, Toshima-ku, Tokyo 171-8588, Japan. fumio.hanaoka@gakushuin.ac.jp.
Abstract:
DDB1 was isolated as a UV-damaged DNA-binding protein, but recent studies established that it plays a role as a component of cullin 4A ubiquitin ligases. Cullin-RING complexes are the largest known ubiquitin ligase family, with hundreds of substrate-specific adaptor subunits and which are defined by characteristic motifs. A common motif for DDB1/cullin 4 ubiquitin ligases, a WDXR motif, was recently reported. Here, we show that Schizosaccharomyces pombe Ddb1 associates with several WD40 repeat proteins that share a novel protein motif designated the DDB-box, a motif essential for interaction with Ddb1 and independent of WD40 repeats, unlike the WDXR motif. We also show that ddb1(+) and the putative CSA homolog ckn1(+) are involved in transcription-coupled nucleotide excision repair and that the DDB-box is essential for the ckn1(+) function in vivo. These data indicate that the DDB-box is another common motif which defines adaptor proteins for DDB1/cullin 4 ubiquitin ligases.
Insights
Researchers discovered a new protein motif, the DDB-box, crucial for DDB1/cullin 4 ubiquitin ligase function. This motif is essential for DNA repair pathways, specifically transcription-coupled nucleotide excision repair.
Area of Science:
- Molecular Biology
- Biochemistry
- Genetics
Background:
- DNA Damage Binding Protein 1 (DDB1) is a key component of cullin 4A ubiquitin ligases.
- Cullin-RING complexes represent a large family of ubiquitin ligases with diverse substrate adaptors.
- A WDXR motif has been identified as common in DDB1/cullin 4 ubiquitin ligases.
Purpose of the Study:
- To identify novel protein motifs involved in DDB1/cullin 4 ubiquitin ligase interactions.
- To investigate the role of these motifs in DNA repair mechanisms.
- To characterize the function of the DDB-box in vivo.
Main Methods:
- Protein association studies in Schizosaccharomyces pombe.
- Identification and characterization of a novel protein motif (DDB-box).
- Analysis of gene function in transcription-coupled nucleotide excision repair.
Main Results:
- Schizosaccharomyces pombe Ddb1 interacts with WD40 repeat proteins containing a novel DDB-box motif.
- The DDB-box is essential for Ddb1 interaction and is independent of WD40 repeats.
- The DDB-box is critical for the in vivo function of ckn1(+) in DNA repair.
Conclusions:
- The DDB-box is a novel motif defining adaptor proteins for DDB1/cullin 4 ubiquitin ligases.
- DDB1 and ckn1(+) are involved in transcription-coupled nucleotide excision repair.
- The DDB-box plays a vital role in DNA repair processes.
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