Light-Induced Dynamic Change of Phytochrome B and Cryptochrome 1 Stabilizes SINATs in Arabidopsis
Ubiquitin-dependent protein degradation plays an important role in many plant developmental processes. We previously identified a class of SINA RING-type E3 ligases of Arabidopsis thaliana (SINATs), whose protein levels decrease in the dark and increase in red and blue light, but the underlying mech...
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doaj-ce20cb64e3e844329c78e234917ac5172021-08-20T13:14:29ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2021-08-011210.3389/fpls.2021.722733722733Light-Induced Dynamic Change of Phytochrome B and Cryptochrome 1 Stabilizes SINATs in ArabidopsisJin Hu0Jin Hu1Yinmeng Hu2Mengran Yang3Xiaotong Hu4Xiaotong Hu5Xuelu Wang6College of Life Science and Technology, Huazhong Agricultural University, Wuhan, ChinaState Key Laboratory of Crop Stress Adaptation and Improvement, Henan University, Kaifeng, ChinaCollege of Life Science and Technology, Huazhong Agricultural University, Wuhan, ChinaState Key Laboratory of Genetic Engineering and Department of Genetics, School of Life Sciences, Fudan University, Shanghai, ChinaCollege of Life Science and Technology, Huazhong Agricultural University, Wuhan, ChinaState Key Laboratory of Crop Stress Adaptation and Improvement, Henan University, Kaifeng, ChinaState Key Laboratory of Crop Stress Adaptation and Improvement, Henan University, Kaifeng, ChinaUbiquitin-dependent protein degradation plays an important role in many plant developmental processes. We previously identified a class of SINA RING-type E3 ligases of Arabidopsis thaliana (SINATs), whose protein levels decrease in the dark and increase in red and blue light, but the underlying mechanism is unclear. In this study, we created transgenic lines carrying point mutations in SINAT genes and photoreceptors-NLS or -NES transgenic plants to investigate the regulatory mechanism of SINAT protein stability. We demonstrated that the degradation of SINATs is self-regulated, and SINATs interact with photoreceptors phytochrome B (phyB) and cryptochrome 1 (CRY1) in the cytoplasm, which leads to the degradation of SINATs in the dark. Furthermore, we observed that the red light-induced subcellular localization change of phyB and blue light-induced the dissociation of CRY1 from SINATs and was the major determinant for the light-promoted SINATs accumulation. Our findings provide a novel mechanism of how the stability and degradation of the E3 ligase SINATs are regulated by an association and dissociation mechanism through the red light-induced subcellular movement of phyB and the blue light-induced dissociation of CRY1 from SINATs.https://www.frontiersin.org/articles/10.3389/fpls.2021.722733/fullphytochrome Bcryptochrome 1lightphotoreceptorsSINA of Arabidopsis thaliana |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Jin Hu Jin Hu Yinmeng Hu Mengran Yang Xiaotong Hu Xiaotong Hu Xuelu Wang |
spellingShingle |
Jin Hu Jin Hu Yinmeng Hu Mengran Yang Xiaotong Hu Xiaotong Hu Xuelu Wang Light-Induced Dynamic Change of Phytochrome B and Cryptochrome 1 Stabilizes SINATs in Arabidopsis Frontiers in Plant Science phytochrome B cryptochrome 1 light photoreceptors SINA of Arabidopsis thaliana |
author_facet |
Jin Hu Jin Hu Yinmeng Hu Mengran Yang Xiaotong Hu Xiaotong Hu Xuelu Wang |
author_sort |
Jin Hu |
title |
Light-Induced Dynamic Change of Phytochrome B and Cryptochrome 1 Stabilizes SINATs in Arabidopsis |
title_short |
Light-Induced Dynamic Change of Phytochrome B and Cryptochrome 1 Stabilizes SINATs in Arabidopsis |
title_full |
Light-Induced Dynamic Change of Phytochrome B and Cryptochrome 1 Stabilizes SINATs in Arabidopsis |
title_fullStr |
Light-Induced Dynamic Change of Phytochrome B and Cryptochrome 1 Stabilizes SINATs in Arabidopsis |
title_full_unstemmed |
Light-Induced Dynamic Change of Phytochrome B and Cryptochrome 1 Stabilizes SINATs in Arabidopsis |
title_sort |
light-induced dynamic change of phytochrome b and cryptochrome 1 stabilizes sinats in arabidopsis |
publisher |
Frontiers Media S.A. |
series |
Frontiers in Plant Science |
issn |
1664-462X |
publishDate |
2021-08-01 |
description |
Ubiquitin-dependent protein degradation plays an important role in many plant developmental processes. We previously identified a class of SINA RING-type E3 ligases of Arabidopsis thaliana (SINATs), whose protein levels decrease in the dark and increase in red and blue light, but the underlying mechanism is unclear. In this study, we created transgenic lines carrying point mutations in SINAT genes and photoreceptors-NLS or -NES transgenic plants to investigate the regulatory mechanism of SINAT protein stability. We demonstrated that the degradation of SINATs is self-regulated, and SINATs interact with photoreceptors phytochrome B (phyB) and cryptochrome 1 (CRY1) in the cytoplasm, which leads to the degradation of SINATs in the dark. Furthermore, we observed that the red light-induced subcellular localization change of phyB and blue light-induced the dissociation of CRY1 from SINATs and was the major determinant for the light-promoted SINATs accumulation. Our findings provide a novel mechanism of how the stability and degradation of the E3 ligase SINATs are regulated by an association and dissociation mechanism through the red light-induced subcellular movement of phyB and the blue light-induced dissociation of CRY1 from SINATs. |
topic |
phytochrome B cryptochrome 1 light photoreceptors SINA of Arabidopsis thaliana |
url |
https://www.frontiersin.org/articles/10.3389/fpls.2021.722733/full |
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