Reversible Ubiquitylation in Plant Biology
Reversible ubiquitylation plays an important regulatory role in almost all aspects of cellular and organismal processes in plants. Its pervasive regulatory role in plant biology is primarily due to the involvement of a large set of ubiquitin system constituents (encoded by approximately 6% Arabidops...
Gardado en:
| Main Authors: | , , |
|---|---|
| Formato: | Online |
| Idioma: | inglés |
| Publicado: |
Frontiers Media SA
2021
|
| Subjects: | |
| Acceso en liña: | 18587 |
| Tags: |
Sen Etiquetas, Sexa o primeiro en etiquetar este rexistro!
|
| _version_ | 1869516991905136640 |
|---|---|
| author | Hongyong Fu Pascal Genschik Daphne Goring |
| author_browse | Daphne Goring Hongyong Fu Pascal Genschik |
| author_facet | Hongyong Fu Pascal Genschik Daphne Goring |
| author_sort | Hongyong Fu |
| collection | Directory of Open Access Books |
| description | Reversible ubiquitylation plays an important regulatory role in almost all aspects of cellular and organismal processes in plants. Its pervasive regulatory role in plant biology is primarily due to the involvement of a large set of ubiquitin system constituents (encoded by approximately 6% Arabidopsis genome), the huge number of important cellular proteins targeted as substrates, and various drastic effects on the modified proteins. The major components of the ubiquitin system include a large set of enzymes and proteins involved in ubiquitin conjugation (E1s, E2s, and E3s) and deconjugation (deubiquitinases of different classes) and post ubiquitin conjugation components such as ubiquitin receptors, endocytic machineries, and 26S proteasome. The established substrates include transcriptional activators and repressors, signaling components, key metabolic enzymes, and critical mechanistic components of major cellular processes and regulatory mechanisms. Post-translational modification of proteins by reversible ubiquitylation could drastically affects the modified proteins by proteolytic processing and turnover, altering catalytic activity, subcellular targeting, and protein-protein interaction. Continued efforts are being carried out to identify novel substrates critical for various cellular and organismal processes, to determine effects of reversible ubiquitylation on the modified substrates, to determine signaling determinants triggering reversible ubiquitylation of specific substrates, to illustrate individual components of the ubiquitin system for their in vivo functions and involved mechanistic roles, and to determine mechanistic roles of modification acting on critical components of major cellular processes and regulatory mechanisms. The aim of this special topic is to serve as a platform to report most recent advances on those above listed current research endeavors. We welcome article types including original research, review, mini review, method, and perspective/opinion/hypothesis. |
| format | Online |
| id | doab-20.500.12854ir-58392 |
| institution | Directory of Open Access Books |
| language | eng |
| publishDate | 2021 |
| publishDateRange | 2021 |
| publishDateSort | 2021 |
| publisher | Frontiers Media SA |
| publisherStr | Frontiers Media SA |
| record_format | ojs |
| spelling | doab-20.500.12854ir-583922024-04-05T17:31:12Z Reversible Ubiquitylation in Plant Biology Hongyong Fu Pascal Genschik Daphne Goring QK1-989 Q1-390 Ubiquitin ubiquitin ligase plant innate immunity NEDD8/RUB self-incompatibility deubiquitination histone abiotic stress thema EDItEUR::P Mathematics and Science::PS Biology, life sciences::PST Botany and plant sciences Reversible ubiquitylation plays an important regulatory role in almost all aspects of cellular and organismal processes in plants. Its pervasive regulatory role in plant biology is primarily due to the involvement of a large set of ubiquitin system constituents (encoded by approximately 6% Arabidopsis genome), the huge number of important cellular proteins targeted as substrates, and various drastic effects on the modified proteins. The major components of the ubiquitin system include a large set of enzymes and proteins involved in ubiquitin conjugation (E1s, E2s, and E3s) and deconjugation (deubiquitinases of different classes) and post ubiquitin conjugation components such as ubiquitin receptors, endocytic machineries, and 26S proteasome. The established substrates include transcriptional activators and repressors, signaling components, key metabolic enzymes, and critical mechanistic components of major cellular processes and regulatory mechanisms. Post-translational modification of proteins by reversible ubiquitylation could drastically affects the modified proteins by proteolytic processing and turnover, altering catalytic activity, subcellular targeting, and protein-protein interaction. Continued efforts are being carried out to identify novel substrates critical for various cellular and organismal processes, to determine effects of reversible ubiquitylation on the modified substrates, to determine signaling determinants triggering reversible ubiquitylation of specific substrates, to illustrate individual components of the ubiquitin system for their in vivo functions and involved mechanistic roles, and to determine mechanistic roles of modification acting on critical components of major cellular processes and regulatory mechanisms. The aim of this special topic is to serve as a platform to report most recent advances on those above listed current research endeavors. We welcome article types including original research, review, mini review, method, and perspective/opinion/hypothesis. 2021-02-12T02:09:52Z 2021-02-12T02:09:52Z 2016-02-05 17:24:33 2015 book 18587 16648714 9782889194414 https://directory.doabooks.org/handle/20.500.12854/58392 eng Frontiers Research Topics image/jpeg Attribution 4.0 International http://www.frontiersin.org/books/Reversible_Ubiquitylation_in_Plant_Biology/480#nogo http://journal.frontiersin.org/researchtopic/1866/reversible-ubiquitylation-in-plant-biology Frontiers Media SA 10.3389/978-2-88919-441-4 10.3389/978-2-88919-441-4 bf5ce210-e72e-4860-ba9b-c305640ff3ae 9782889194414 115 open access |
| spellingShingle | QK1-989 Q1-390 Ubiquitin ubiquitin ligase plant innate immunity NEDD8/RUB self-incompatibility deubiquitination histone abiotic stress thema EDItEUR::P Mathematics and Science::PS Biology, life sciences::PST Botany and plant sciences Hongyong Fu Pascal Genschik Daphne Goring Reversible Ubiquitylation in Plant Biology |
| title | Reversible Ubiquitylation in Plant Biology |
| title_full | Reversible Ubiquitylation in Plant Biology |
| title_fullStr | Reversible Ubiquitylation in Plant Biology |
| title_full_unstemmed | Reversible Ubiquitylation in Plant Biology |
| title_short | Reversible Ubiquitylation in Plant Biology |
| title_sort | reversible ubiquitylation in plant biology |
| topic | QK1-989 Q1-390 Ubiquitin ubiquitin ligase plant innate immunity NEDD8/RUB self-incompatibility deubiquitination histone abiotic stress thema EDItEUR::P Mathematics and Science::PS Biology, life sciences::PST Botany and plant sciences |
| topic_facet | QK1-989 Q1-390 Ubiquitin ubiquitin ligase plant innate immunity NEDD8/RUB self-incompatibility deubiquitination histone abiotic stress thema EDItEUR::P Mathematics and Science::PS Biology, life sciences::PST Botany and plant sciences |
| url | 18587 |
| work_keys_str_mv | AT hongyongfu reversibleubiquitylationinplantbiology AT pascalgenschik reversibleubiquitylationinplantbiology AT daphnegoring reversibleubiquitylationinplantbiology |