Regulation of Arabidopsis photoreceptor CRY2 by two distinct E3 ubiquitin ligases

The fate of proteins in cells is determined by not only synthesis but also degradation. Here Chen et al. show that degradation of the plant blue light receptor CRY2 is determined by two distinct E3 ubiquitin ligases, Cul4COP1/SPAs and Cul3LRBs, regulating the function of CRY2 under different light c...

Full description

Bibliographic Details
Main Authors: Yadi Chen, Xiaohua Hu, Siyuan Liu, Tiantian Su, Hsiaochi Huang, Huibo Ren, Zhensheng Gao, Xu Wang, Deshu Lin, James A. Wohlschlegel, Qin Wang, Chentao Lin
Format: Article
Language:English
Published: Nature Publishing Group 2021-04-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-021-22410-x
id doaj-433915f079e646c48c5a0e595d94b622
record_format Article
spelling doaj-433915f079e646c48c5a0e595d94b6222021-04-18T11:14:29ZengNature Publishing GroupNature Communications2041-17232021-04-0112111410.1038/s41467-021-22410-xRegulation of Arabidopsis photoreceptor CRY2 by two distinct E3 ubiquitin ligasesYadi Chen0Xiaohua Hu1Siyuan Liu2Tiantian Su3Hsiaochi Huang4Huibo Ren5Zhensheng Gao6Xu Wang7Deshu Lin8James A. Wohlschlegel9Qin Wang10Chentao Lin11College of Life Sciences, Basic Forestry and Proteomics Research Center, Fujian Agriculture and Forestry UniversityCollege of Life Sciences, Basic Forestry and Proteomics Research Center, Fujian Agriculture and Forestry UniversityCollege of Life Sciences, Basic Forestry and Proteomics Research Center, Fujian Agriculture and Forestry UniversityDepartment of Molecular, Cell & Developmental Biology, University of CaliforniaDepartment of Molecular, Cell & Developmental Biology, University of CaliforniaCollege of Life Sciences, Basic Forestry and Proteomics Research Center, Fujian Agriculture and Forestry UniversityCollege of Life Sciences, Basic Forestry and Proteomics Research Center, Fujian Agriculture and Forestry UniversityCollege of Life Sciences, Basic Forestry and Proteomics Research Center, Fujian Agriculture and Forestry UniversityCollege of Life Sciences, Basic Forestry and Proteomics Research Center, Fujian Agriculture and Forestry UniversityDepartment of Biological Chemistry, University of CaliforniaCollege of Life Sciences, Basic Forestry and Proteomics Research Center, Fujian Agriculture and Forestry UniversityDepartment of Molecular, Cell & Developmental Biology, University of CaliforniaThe fate of proteins in cells is determined by not only synthesis but also degradation. Here Chen et al. show that degradation of the plant blue light receptor CRY2 is determined by two distinct E3 ubiquitin ligases, Cul4COP1/SPAs and Cul3LRBs, regulating the function of CRY2 under different light conditions.https://doi.org/10.1038/s41467-021-22410-x
collection DOAJ
language English
format Article
sources DOAJ
author Yadi Chen
Xiaohua Hu
Siyuan Liu
Tiantian Su
Hsiaochi Huang
Huibo Ren
Zhensheng Gao
Xu Wang
Deshu Lin
James A. Wohlschlegel
Qin Wang
Chentao Lin
spellingShingle Yadi Chen
Xiaohua Hu
Siyuan Liu
Tiantian Su
Hsiaochi Huang
Huibo Ren
Zhensheng Gao
Xu Wang
Deshu Lin
James A. Wohlschlegel
Qin Wang
Chentao Lin
Regulation of Arabidopsis photoreceptor CRY2 by two distinct E3 ubiquitin ligases
Nature Communications
author_facet Yadi Chen
Xiaohua Hu
Siyuan Liu
Tiantian Su
Hsiaochi Huang
Huibo Ren
Zhensheng Gao
Xu Wang
Deshu Lin
James A. Wohlschlegel
Qin Wang
Chentao Lin
author_sort Yadi Chen
title Regulation of Arabidopsis photoreceptor CRY2 by two distinct E3 ubiquitin ligases
title_short Regulation of Arabidopsis photoreceptor CRY2 by two distinct E3 ubiquitin ligases
title_full Regulation of Arabidopsis photoreceptor CRY2 by two distinct E3 ubiquitin ligases
title_fullStr Regulation of Arabidopsis photoreceptor CRY2 by two distinct E3 ubiquitin ligases
title_full_unstemmed Regulation of Arabidopsis photoreceptor CRY2 by two distinct E3 ubiquitin ligases
title_sort regulation of arabidopsis photoreceptor cry2 by two distinct e3 ubiquitin ligases
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2021-04-01
description The fate of proteins in cells is determined by not only synthesis but also degradation. Here Chen et al. show that degradation of the plant blue light receptor CRY2 is determined by two distinct E3 ubiquitin ligases, Cul4COP1/SPAs and Cul3LRBs, regulating the function of CRY2 under different light conditions.
url https://doi.org/10.1038/s41467-021-22410-x
work_keys_str_mv AT yadichen regulationofarabidopsisphotoreceptorcry2bytwodistincte3ubiquitinligases
AT xiaohuahu regulationofarabidopsisphotoreceptorcry2bytwodistincte3ubiquitinligases
AT siyuanliu regulationofarabidopsisphotoreceptorcry2bytwodistincte3ubiquitinligases
AT tiantiansu regulationofarabidopsisphotoreceptorcry2bytwodistincte3ubiquitinligases
AT hsiaochihuang regulationofarabidopsisphotoreceptorcry2bytwodistincte3ubiquitinligases
AT huiboren regulationofarabidopsisphotoreceptorcry2bytwodistincte3ubiquitinligases
AT zhenshenggao regulationofarabidopsisphotoreceptorcry2bytwodistincte3ubiquitinligases
AT xuwang regulationofarabidopsisphotoreceptorcry2bytwodistincte3ubiquitinligases
AT deshulin regulationofarabidopsisphotoreceptorcry2bytwodistincte3ubiquitinligases
AT jamesawohlschlegel regulationofarabidopsisphotoreceptorcry2bytwodistincte3ubiquitinligases
AT qinwang regulationofarabidopsisphotoreceptorcry2bytwodistincte3ubiquitinligases
AT chentaolin regulationofarabidopsisphotoreceptorcry2bytwodistincte3ubiquitinligases
_version_ 1721522492396273664