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Deubiquitination of BES1 by UBP12/UBP13 promotes brassinosteroid signaling and plant growth

As a key transcription factor in the brassinosteroid (BR) signaling pathway, the activity and expression of BES1 (BRI1-EMS-SUPPRESSOR 1) are stringently regulated. BES1 degradation is mediated by ubiquitin-related 26S proteasomal and autophagy pathways, which attenuate and terminate BR signaling; ho...

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Autores principales: Park, Su-Hyun, Jeong, Jin Seo, Zhou, Yu, Binte Mustafa, Nur Fatimah, Chua, Nam-Hai
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9483116/
https://www.ncbi.nlm.nih.gov/pubmed/35706355
http://dx.doi.org/10.1016/j.xplc.2022.100348
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author Park, Su-Hyun
Jeong, Jin Seo
Zhou, Yu
Binte Mustafa, Nur Fatimah
Chua, Nam-Hai
author_facet Park, Su-Hyun
Jeong, Jin Seo
Zhou, Yu
Binte Mustafa, Nur Fatimah
Chua, Nam-Hai
author_sort Park, Su-Hyun
collection PubMed
description As a key transcription factor in the brassinosteroid (BR) signaling pathway, the activity and expression of BES1 (BRI1-EMS-SUPPRESSOR 1) are stringently regulated. BES1 degradation is mediated by ubiquitin-related 26S proteasomal and autophagy pathways, which attenuate and terminate BR signaling; however, the opposing deubiquitinases (DUBs) are still unknown. Here, we showed that the ubp12-2w/13-3 double mutant phenocopies the BR-deficient dwarf mutant, suggesting that the two DUBs UBP12/UBP13 antagonize ubiquitin-mediated degradation to stabilize BES1. These two DUBs can trim tetraubiquitin with K46 and K63 linkages in vitro. UBP12/BES1 and UBP13/BES1 complexes are localized in both cytosol and nuclei. UBP12/13 can deubiquitinate polyubiquitinated BES1 in vitro and in planta, and UBP12 interacts with and deubiquitinates both inactive, phosphorylated BES1 and active, dephosphorylated BES1 in vivo. UBP12 overexpression in BES1(OE) plants significantly enhances cell elongation in hypocotyls and petioles and increases the ratio of leaf length to width compared with BES1(OE) or UBP12(OE) plants. Hypocotyl elongation and etiolation result from elevated BES1 levels because BES1 degradation is retarded by UBP12 in darkness or in light with BR. Protein degradation inhibitor experiments show that the majority of BES1 can be degraded by either the proteasomal or the autophagy pathway, but a minor BES1 fraction remains pathway specific. In conclusion, UBP12/UBP13 deubiquitinate BES1 to stabilize the latter as a positive regulator for BR responses.
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spelling pubmed-94831162022-09-20 Deubiquitination of BES1 by UBP12/UBP13 promotes brassinosteroid signaling and plant growth Park, Su-Hyun Jeong, Jin Seo Zhou, Yu Binte Mustafa, Nur Fatimah Chua, Nam-Hai Plant Commun Research Article As a key transcription factor in the brassinosteroid (BR) signaling pathway, the activity and expression of BES1 (BRI1-EMS-SUPPRESSOR 1) are stringently regulated. BES1 degradation is mediated by ubiquitin-related 26S proteasomal and autophagy pathways, which attenuate and terminate BR signaling; however, the opposing deubiquitinases (DUBs) are still unknown. Here, we showed that the ubp12-2w/13-3 double mutant phenocopies the BR-deficient dwarf mutant, suggesting that the two DUBs UBP12/UBP13 antagonize ubiquitin-mediated degradation to stabilize BES1. These two DUBs can trim tetraubiquitin with K46 and K63 linkages in vitro. UBP12/BES1 and UBP13/BES1 complexes are localized in both cytosol and nuclei. UBP12/13 can deubiquitinate polyubiquitinated BES1 in vitro and in planta, and UBP12 interacts with and deubiquitinates both inactive, phosphorylated BES1 and active, dephosphorylated BES1 in vivo. UBP12 overexpression in BES1(OE) plants significantly enhances cell elongation in hypocotyls and petioles and increases the ratio of leaf length to width compared with BES1(OE) or UBP12(OE) plants. Hypocotyl elongation and etiolation result from elevated BES1 levels because BES1 degradation is retarded by UBP12 in darkness or in light with BR. Protein degradation inhibitor experiments show that the majority of BES1 can be degraded by either the proteasomal or the autophagy pathway, but a minor BES1 fraction remains pathway specific. In conclusion, UBP12/UBP13 deubiquitinate BES1 to stabilize the latter as a positive regulator for BR responses. Elsevier 2022-06-15 /pmc/articles/PMC9483116/ /pubmed/35706355 http://dx.doi.org/10.1016/j.xplc.2022.100348 Text en © 2022 The Author(s) https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Research Article
Park, Su-Hyun
Jeong, Jin Seo
Zhou, Yu
Binte Mustafa, Nur Fatimah
Chua, Nam-Hai
Deubiquitination of BES1 by UBP12/UBP13 promotes brassinosteroid signaling and plant growth
title Deubiquitination of BES1 by UBP12/UBP13 promotes brassinosteroid signaling and plant growth
title_full Deubiquitination of BES1 by UBP12/UBP13 promotes brassinosteroid signaling and plant growth
title_fullStr Deubiquitination of BES1 by UBP12/UBP13 promotes brassinosteroid signaling and plant growth
title_full_unstemmed Deubiquitination of BES1 by UBP12/UBP13 promotes brassinosteroid signaling and plant growth
title_short Deubiquitination of BES1 by UBP12/UBP13 promotes brassinosteroid signaling and plant growth
title_sort deubiquitination of bes1 by ubp12/ubp13 promotes brassinosteroid signaling and plant growth
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9483116/
https://www.ncbi.nlm.nih.gov/pubmed/35706355
http://dx.doi.org/10.1016/j.xplc.2022.100348
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