Photoreceptor ubiquitination by COP1 E3 ligase desensitizes phytochrome A signaling

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 l...

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Bibliographic Details
Published in:Genes & development 2004-03, Vol.18 (6), p.617-622
Main Authors: Seo, Hak Soo, Watanabe, Etsuko, Tokutomi, Satoru, Nagatani, Akira, Chua, Nam-Hai
Format: Article
Language:English
Subjects:
Arabidopsis - enzymology
Arabidopsis Proteins - metabolism
Genes, Reporter
Phytochrome - metabolism
Phytochrome A
Research Communications
Signal Transduction - physiology
Staining and Labeling
Ubiquitin - metabolism
Ubiquitin-Protein Ligases - metabolism
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Summary: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.
ISSN:0890-9369
1549-5477
DOI:10.1101/gad.1187804