Cargando…

Arabidopsis COP1 SUPPRESSOR 2 Represses COP1 E3 Ubiquitin Ligase Activity through Their Coiled-Coil Domains Association

CONSTITUTIVE PHOTOMORPHOGENIC 1 (COP1) functions as an E3 ubiquitin ligase and mediates a variety of developmental processes in Arabidopsis by targeting a number of key regulators for ubiquitination and degradation. Here, we identify a novel COP1 interacting protein, COP1 SUPPRESSOR 2 (CSU2). Loss o...

Descripción completa

Detalles Bibliográficos
Autores principales: Xu, Dongqing, Lin, Fang, Jiang, Yan, Ling, Junjie, Hettiarachchi, Chamari, Tellgren-Roth, Christian, Holm, Magnus, Wei, Ning, Deng, Xing Wang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4694719/
https://www.ncbi.nlm.nih.gov/pubmed/26714275
http://dx.doi.org/10.1371/journal.pgen.1005747
_version_ 1782407507521568768
author Xu, Dongqing
Lin, Fang
Jiang, Yan
Ling, Junjie
Hettiarachchi, Chamari
Tellgren-Roth, Christian
Holm, Magnus
Wei, Ning
Deng, Xing Wang
author_facet Xu, Dongqing
Lin, Fang
Jiang, Yan
Ling, Junjie
Hettiarachchi, Chamari
Tellgren-Roth, Christian
Holm, Magnus
Wei, Ning
Deng, Xing Wang
author_sort Xu, Dongqing
collection PubMed
description CONSTITUTIVE PHOTOMORPHOGENIC 1 (COP1) functions as an E3 ubiquitin ligase and mediates a variety of developmental processes in Arabidopsis by targeting a number of key regulators for ubiquitination and degradation. Here, we identify a novel COP1 interacting protein, COP1 SUPPRESSOR 2 (CSU2). Loss of function mutations in CSU2 suppress the constitutive photomorphogenic phenotype of cop1-6 in darkness. CSU2 directly interacts with COP1 via their coiled-coil domains and is recruited by COP1 into nuclear speckles in living plant cells. Furthermore, CSU2 inhibits COP1 E3 ubiquitin ligase activity in vitro, and represses COP1 mediated turnover of HY5 in cell-free extracts. We propose that in csu2 cop1-6 mutants, the lack of CSU2’s repression of COP1 allows the low level of COP1 to exhibit higher activity that is sufficient to prevent accumulation of HY5 in the dark, thus restoring the etiolated phenotype. In addition, CSU2 is required for primary root development under normal light growth condition.
format Online
Article
Text
id pubmed-4694719
institution National Center for Biotechnology Information
language English
publishDate 2015
publisher Public Library of Science
record_format MEDLINE/PubMed
spelling pubmed-46947192016-01-13 Arabidopsis COP1 SUPPRESSOR 2 Represses COP1 E3 Ubiquitin Ligase Activity through Their Coiled-Coil Domains Association Xu, Dongqing Lin, Fang Jiang, Yan Ling, Junjie Hettiarachchi, Chamari Tellgren-Roth, Christian Holm, Magnus Wei, Ning Deng, Xing Wang PLoS Genet Research Article CONSTITUTIVE PHOTOMORPHOGENIC 1 (COP1) functions as an E3 ubiquitin ligase and mediates a variety of developmental processes in Arabidopsis by targeting a number of key regulators for ubiquitination and degradation. Here, we identify a novel COP1 interacting protein, COP1 SUPPRESSOR 2 (CSU2). Loss of function mutations in CSU2 suppress the constitutive photomorphogenic phenotype of cop1-6 in darkness. CSU2 directly interacts with COP1 via their coiled-coil domains and is recruited by COP1 into nuclear speckles in living plant cells. Furthermore, CSU2 inhibits COP1 E3 ubiquitin ligase activity in vitro, and represses COP1 mediated turnover of HY5 in cell-free extracts. We propose that in csu2 cop1-6 mutants, the lack of CSU2’s repression of COP1 allows the low level of COP1 to exhibit higher activity that is sufficient to prevent accumulation of HY5 in the dark, thus restoring the etiolated phenotype. In addition, CSU2 is required for primary root development under normal light growth condition. Public Library of Science 2015-12-29 /pmc/articles/PMC4694719/ /pubmed/26714275 http://dx.doi.org/10.1371/journal.pgen.1005747 Text en © 2015 Xu et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Xu, Dongqing
Lin, Fang
Jiang, Yan
Ling, Junjie
Hettiarachchi, Chamari
Tellgren-Roth, Christian
Holm, Magnus
Wei, Ning
Deng, Xing Wang
Arabidopsis COP1 SUPPRESSOR 2 Represses COP1 E3 Ubiquitin Ligase Activity through Their Coiled-Coil Domains Association
title Arabidopsis COP1 SUPPRESSOR 2 Represses COP1 E3 Ubiquitin Ligase Activity through Their Coiled-Coil Domains Association
title_full Arabidopsis COP1 SUPPRESSOR 2 Represses COP1 E3 Ubiquitin Ligase Activity through Their Coiled-Coil Domains Association
title_fullStr Arabidopsis COP1 SUPPRESSOR 2 Represses COP1 E3 Ubiquitin Ligase Activity through Their Coiled-Coil Domains Association
title_full_unstemmed Arabidopsis COP1 SUPPRESSOR 2 Represses COP1 E3 Ubiquitin Ligase Activity through Their Coiled-Coil Domains Association
title_short Arabidopsis COP1 SUPPRESSOR 2 Represses COP1 E3 Ubiquitin Ligase Activity through Their Coiled-Coil Domains Association
title_sort arabidopsis cop1 suppressor 2 represses cop1 e3 ubiquitin ligase activity through their coiled-coil domains association
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4694719/
https://www.ncbi.nlm.nih.gov/pubmed/26714275
http://dx.doi.org/10.1371/journal.pgen.1005747
work_keys_str_mv AT xudongqing arabidopsiscop1suppressor2repressescop1e3ubiquitinligaseactivitythroughtheircoiledcoildomainsassociation
AT linfang arabidopsiscop1suppressor2repressescop1e3ubiquitinligaseactivitythroughtheircoiledcoildomainsassociation
AT jiangyan arabidopsiscop1suppressor2repressescop1e3ubiquitinligaseactivitythroughtheircoiledcoildomainsassociation
AT lingjunjie arabidopsiscop1suppressor2repressescop1e3ubiquitinligaseactivitythroughtheircoiledcoildomainsassociation
AT hettiarachchichamari arabidopsiscop1suppressor2repressescop1e3ubiquitinligaseactivitythroughtheircoiledcoildomainsassociation
AT tellgrenrothchristian arabidopsiscop1suppressor2repressescop1e3ubiquitinligaseactivitythroughtheircoiledcoildomainsassociation
AT holmmagnus arabidopsiscop1suppressor2repressescop1e3ubiquitinligaseactivitythroughtheircoiledcoildomainsassociation
AT weining arabidopsiscop1suppressor2repressescop1e3ubiquitinligaseactivitythroughtheircoiledcoildomainsassociation
AT dengxingwang arabidopsiscop1suppressor2repressescop1e3ubiquitinligaseactivitythroughtheircoiledcoildomainsassociation