The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Arabidopsis COP10 forms a complex with DDB1 and DET1 in vivo and enhances the activity of ubiquitin conjugating enzymes
Open accessAbstract
COP10 is a ubiquitin-conjugating enzyme variant (UEV), which is thought to act together with COP1, DET1, and the COP9 signalosome (CSN) in Arabidopsis to repress photomorphogenesis. Here, we demonstrate that COP10 interacts with ubiquitin-conjugating enzymes (E2s) in vivo, and can enhance their activity in vitro, an activity distinct from previous characterized UEVs such as MMS2 and UEV1. Furthermore, we show that COP10 forms a complex with UV-damaged DNA-binding protein 1a (DDB1a) and de-etiolated 1 (DET1), and physically interacts with COP1 and the CSN. Purified CDD (COP10, DDB1, DET1) complex also shows enhancement of E2 activity (UEA) similar to that observed with COP10 itself. Our data suggests that COP10, along with COP1 and the CSN, promotes the degradation of positive regulators of photomorphogenesis, such as the transcription factor HY5, via the ubiquitin/26S proteasome system. Thus, the CDD complex may act as a ubiquitylation-promoting factor to regulate photomorphogenesis.
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Hwang, B. J., Ford, J. M., Hanawalt, P. C., & Chu, G. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.2.424 · Cited by 581
Human Damage-specific DNA-binding Protein p48
Nichols, A. F., Itoh, T., Graham, J. A., Liu, W., Yamaizumi, M., & Linn, S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000960200 · Cited by 137
Cited by
The Ubiquitin-Proteasome Pathway and Plant Development
Moon, J., Parry, G., & Estelle, M. (2004) · The Plant Cell · doi:10.1105/tpc.104.161220 · Cited by 586
Phytochrome Signaling Mechanisms
Li, J., Li, G., Wang, H., & Wang Deng, X. (2011) · The Arabidopsis Book · doi:10.1199/tab.0148 · Cited by 561
Ubiquitin, Hormones and Biotic Stress in Plants
Dreher, K., & Callis, J. (2007) · Annals of Botany · doi:10.1093/aob/mcl255 · Cited by 503
Lee, J.-H., Terzaghi, W., Gusmaroli, G., Charron, J.-B. F., Yoon, H.-J., Chen, H., He, Y. J., Xiong, Y., & Deng, X. W. (2008) · The Plant Cell · doi:10.1105/tpc.107.055418 · Cited by 256
Self-citationKimura, S., & Sakaguchi, K. (2006) · Chemical Reviews · doi:10.1021/cr040482n · Cited by 167
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Metadata
- Authors
- Yanagawa, Y., Sullivan, J. A., Komatsu, S., Gusmaroli, G., Suzuki, G., Yin, J., Ishibashi, T., Saijo, Y., Rubio, V., Kimura, S., Wang, J., & Deng, X. W.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2004-09-01
- Volume
- 18
- Issue
- 17
- Pages
- 2172-2181
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W2107440564
- Cited by
- 205
- References
- 2
- Type
- posted content
- Language
- en
- Open access
- diamond
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- Yanagawa, Y., Sullivan, J. A., Komatsu, S., Gusmaroli, G., Suzuki, G., Yin, J., Ishibashi, T., Saijo, Y., Rubio, V., Kimura, S., Wang, J., & Deng, X. W. (2004). Arabidopsis COP10 forms a complex with DDB1 and DET1 in vivo and enhances the activity of ubiquitin conjugating enzymes. Genes & Development. https://doi.org/10.1101/gad.1229504
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