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Photoreceptor ubiquitination by COP1 E3 ligase desensitizes phytochrome A signaling

Open access
Seo, Hak Soo, Watanabe, Etsuko, Tokutomi, Satoru, Nagatani, Akira, Chua, Nam-Hai·2004·Genes & Development

Abstract

Desensitization of activated receptors is an important mechanism for terminating signal transduction. Here we show that phytochrome (phy) A, a predominant photoreceptor for seedling deetiolation, colocalizes in nuclear bodies with CONSTITUTIVELY PHOTOMORPHOGENIC (COP) 1, a RING motif-containing E3 ligase. The phyA PAS domain interacts with the COP1 WD40 domain. Both the Pr and the Pfr forms of phyA, as well as the PHYA apoprotein, are ubiquitinated by COP1 in vitro. The phyA destruction rate is decreased in cop1 mutants and by expression of a COP1 RING motif mutant. Our results indicate that COP1 acts as an E3 ligase to regulate phyA signaling by targeting elimination of the phyA photoreceptor itself.

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Metadata

Authors
Seo, H. S., Watanabe, E., Tokutomi, S., Nagatani, A., & Chua, N.-H.
Venue
Genes & Development
Published
2004-03-15
Volume
18
Issue
6
Pages
617-622
ISSN
  • 0890-9369 (ISSN-L)
  • 1549-5477
OpenAlex
W2133307159
Cited by
324
References
0
Type
posted content
Language
en
Open access
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CoChat. (2026). Citation check: Photoreceptor ubiquitination by COP1 E3 ligase desensitizes phytochrome A signaling. https://app.cochat.ai/papers/10.1101/gad.1187804
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Seo, H. S., Watanabe, E., Tokutomi, S., Nagatani, A., & Chua, N.-H. (2004). Photoreceptor ubiquitination by COP1 E3 ligase desensitizes phytochrome A signaling. Genes & Development. https://doi.org/10.1101/gad.1187804

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.