Differential photoregulation of the nuclear and cytoplasmic CRY1 in Arabidopsis

© 2022 The Authors. New Phytologist © 2022 New Phytologist Foundation.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 234(2022), 4 vom: 30. Mai, Seite 1332-1346
1. Verfasser: Liu, Siyuan (VerfasserIn)
Weitere Verfasser: Zhang, Li, Gao, Lin, Chen, Ziyin, Bie, Yaxue, Zhao, Qiannan, Zhang, Shanshan, Hu, Xiaohua, Liu, Qing, Wang, Xu, Wang, Qin
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2022
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Arabidopsis COP1-SPA CRY1 blue light photobody protein degradation Arabidopsis Proteins CRY1 protein, Arabidopsis mehr... Cryptochromes Transcription Factors
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500 |a CommentIn: New Phytol. 2022 May;234(4):1109-1111. - PMID 35357013 
500 |a Citation Status MEDLINE 
520 |a © 2022 The Authors. New Phytologist © 2022 New Phytologist Foundation. 
520 |a Arabidopsis cryptochrome 1 (CRY1) is a blue light receptor distributed in the nucleus and cytoplasm. The nuclear CRY1, but not cytoplasmic CRY1, mediates blue light inhibition of hypocotyl elongation. However, the photobiochemical mechanisms distinguishing the CRY1 protein in the two subcellular compartments remains unclear. Here we show that the nuclear CRY1, but not the cytoplasmic CRY1, is regulated by phosphorylation, polyubiquitination and 26S proteasome-dependent proteolysis in response to blue light. The blue light-dependent CRY1 degradation is observed only under high fluences of blue light. The nuclear specificity and high fluence dependency of CRY1 explain why this photochemical regulatory mechanism of CRY1 was not observed previously and it further supports the hypothesis that CRY1 is a high light receptor regulating photomorphogenesis. We further show that the nuclear CRY1, but not cytoplasmic CRY1, undergoes blue light-dependent phosphorylation by photoregulatory protein kinase 1 (PPK1) followed by polyubiquitination by the E3 ubiquitin ligase Cul4COP1/SPAs , resulting in the blue light-dependent proteolysis. Both phosphorylation and ubiquitination of nuclear CRY1 are inhibited by blue-light inhibitor of cryptochromes 1 (BIC1), demonstrating the involvement of photo-oligomerization of the nuclear CRY1. These finding reveals a photochemical mechanism that differentially regulates the physiological activity of the CRY1 photoreceptor in distinct subcellular compartments 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Arabidopsis 
650 4 |a COP1-SPA 
650 4 |a CRY1 
650 4 |a blue light 
650 4 |a photobody 
650 4 |a protein degradation 
650 7 |a Arabidopsis Proteins  |2 NLM 
650 7 |a CRY1 protein, Arabidopsis  |2 NLM 
650 7 |a Cryptochromes  |2 NLM 
650 7 |a Transcription Factors  |2 NLM 
700 1 |a Zhang, Li  |e verfasserin  |4 aut 
700 1 |a Gao, Lin  |e verfasserin  |4 aut 
700 1 |a Chen, Ziyin  |e verfasserin  |4 aut 
700 1 |a Bie, Yaxue  |e verfasserin  |4 aut 
700 1 |a Zhao, Qiannan  |e verfasserin  |4 aut 
700 1 |a Zhang, Shanshan  |e verfasserin  |4 aut 
700 1 |a Hu, Xiaohua  |e verfasserin  |4 aut 
700 1 |a Liu, Qing  |e verfasserin  |4 aut 
700 1 |a Wang, Xu  |e verfasserin  |4 aut 
700 1 |a Wang, Qin  |e verfasserin  |4 aut 
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773 1 8 |g volume:234  |g year:2022  |g number:4  |g day:30  |g month:05  |g pages:1332-1346 
856 4 0 |u http://dx.doi.org/10.1111/nph.18007  |3 Volltext 
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