Decoys provide a scalable platform for the identification of plant E3 ubiquitin ligases that regulate circadian function
The circadian clock relies on regulated degradation of clock proteins to maintain rhythmicity. Despite this, we know few components that mediate protein degradation. This is due to high levels of functional redundancy within plant E3 ubiquitin ligase families. In order to overcome this issue and dis...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2019-04-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/44558 |
| _version_ | 1828169051143143424 |
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| author | Ann Feke Wei Liu Jing Hong Man-Wah Li Chin-Mei Lee Elton K Zhou Joshua M Gendron |
| author_facet | Ann Feke Wei Liu Jing Hong Man-Wah Li Chin-Mei Lee Elton K Zhou Joshua M Gendron |
| author_sort | Ann Feke |
| collection | DOAJ |
| description | The circadian clock relies on regulated degradation of clock proteins to maintain rhythmicity. Despite this, we know few components that mediate protein degradation. This is due to high levels of functional redundancy within plant E3 ubiquitin ligase families. In order to overcome this issue and discover E3 ubiquitin ligases that control circadian function, we generated a library of transgenic Arabidopsis plants expressing dominant-negative ‘decoy’ E3 ubiquitin ligases. We determined their effects on the circadian clock and identified dozens of new potential regulators of circadian function. To demonstrate the potency of the decoy screening methodology to overcome redundancy and identify bona fide clock regulators, we performed follow-up studies on MAC3A (PUB59) and MAC3B (PUB60). We show that they redundantly control circadian period by regulating splicing. This work demonstrates the viability of ubiquitin ligase decoys as a screening platform to overcome genetic challenges and discover E3 ubiquitin ligases that regulate plant development. |
| first_indexed | 2024-04-12T02:44:49Z |
| format | Article |
| id | doaj.art-fb5ef723079a4e3c96d3d8ae7bf8d0fa |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T02:44:49Z |
| publishDate | 2019-04-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-fb5ef723079a4e3c96d3d8ae7bf8d0fa2022-12-22T03:51:14ZengeLife Sciences Publications LtdeLife2050-084X2019-04-01810.7554/eLife.44558Decoys provide a scalable platform for the identification of plant E3 ubiquitin ligases that regulate circadian functionAnn Feke0https://orcid.org/0000-0002-8246-0056Wei Liu1Jing Hong2Man-Wah Li3Chin-Mei Lee4https://orcid.org/0000-0003-3870-4268Elton K Zhou5Joshua M Gendron6https://orcid.org/0000-0001-8605-3047Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, United StatesDepartment of Molecular, Cellular and Developmental Biology, Yale University, New Haven, United StatesDepartment of Molecular, Cellular and Developmental Biology, Yale University, New Haven, United States; School of Food Science and Engineering, South China University of Technology, Guangzhou, ChinaDepartment of Molecular, Cellular and Developmental Biology, Yale University, New Haven, United StatesDepartment of Molecular, Cellular and Developmental Biology, Yale University, New Haven, United StatesDepartment of Molecular, Cellular and Developmental Biology, Yale University, New Haven, United StatesDepartment of Molecular, Cellular and Developmental Biology, Yale University, New Haven, United StatesThe circadian clock relies on regulated degradation of clock proteins to maintain rhythmicity. Despite this, we know few components that mediate protein degradation. This is due to high levels of functional redundancy within plant E3 ubiquitin ligase families. In order to overcome this issue and discover E3 ubiquitin ligases that control circadian function, we generated a library of transgenic Arabidopsis plants expressing dominant-negative ‘decoy’ E3 ubiquitin ligases. We determined their effects on the circadian clock and identified dozens of new potential regulators of circadian function. To demonstrate the potency of the decoy screening methodology to overcome redundancy and identify bona fide clock regulators, we performed follow-up studies on MAC3A (PUB59) and MAC3B (PUB60). We show that they redundantly control circadian period by regulating splicing. This work demonstrates the viability of ubiquitin ligase decoys as a screening platform to overcome genetic challenges and discover E3 ubiquitin ligases that regulate plant development.https://elifesciences.org/articles/44558protein ubiquitylationcircadian clockE3 ubiquitin ligase decoypost-translational modification |
| spellingShingle | Ann Feke Wei Liu Jing Hong Man-Wah Li Chin-Mei Lee Elton K Zhou Joshua M Gendron Decoys provide a scalable platform for the identification of plant E3 ubiquitin ligases that regulate circadian function eLife protein ubiquitylation circadian clock E3 ubiquitin ligase decoy post-translational modification |
| title | Decoys provide a scalable platform for the identification of plant E3 ubiquitin ligases that regulate circadian function |
| title_full | Decoys provide a scalable platform for the identification of plant E3 ubiquitin ligases that regulate circadian function |
| title_fullStr | Decoys provide a scalable platform for the identification of plant E3 ubiquitin ligases that regulate circadian function |
| title_full_unstemmed | Decoys provide a scalable platform for the identification of plant E3 ubiquitin ligases that regulate circadian function |
| title_short | Decoys provide a scalable platform for the identification of plant E3 ubiquitin ligases that regulate circadian function |
| title_sort | decoys provide a scalable platform for the identification of plant e3 ubiquitin ligases that regulate circadian function |
| topic | protein ubiquitylation circadian clock E3 ubiquitin ligase decoy post-translational modification |
| url | https://elifesciences.org/articles/44558 |
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