Met1-linked ubiquitination in immune signalling.
N-terminal methionine-linked ubiquitin (Met1-Ub), or linear ubiquitin, has emerged as a central post-translational modification in innate immune signalling. The molecular machinery that assembles, senses and, more recently, disassembles Met1-Ub has been identified, and technical advances have enable...
| Main Authors: | , |
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| Format: | Journal article |
| Language: | English |
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2014
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| _version_ | 1797050793198616576 |
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| author | Fiil, B Gyrd-Hansen, M |
| author_facet | Fiil, B Gyrd-Hansen, M |
| author_sort | Fiil, B |
| collection | OXFORD |
| description | N-terminal methionine-linked ubiquitin (Met1-Ub), or linear ubiquitin, has emerged as a central post-translational modification in innate immune signalling. The molecular machinery that assembles, senses and, more recently, disassembles Met1-Ub has been identified, and technical advances have enabled the identification of physiological substrates for Met1-Ub in response to activation of innate immune receptors. These discoveries have significantly advanced our understanding of how nondegradative ubiquitin modifications control proinflammatory responses mediated by nuclear factor-κB and mitogen-activated protein kinases. In this review, we discuss the current data on Met1-Ub function and regulation, and point to some of the questions that still remain unanswered. |
| first_indexed | 2024-03-06T18:10:27Z |
| format | Journal article |
| id | oxford-uuid:02d58943-7ffc-4407-83e1-65c5021977da |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T18:10:27Z |
| publishDate | 2014 |
| record_format | dspace |
| spelling | oxford-uuid:02d58943-7ffc-4407-83e1-65c5021977da2022-03-26T08:42:58ZMet1-linked ubiquitination in immune signalling.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:02d58943-7ffc-4407-83e1-65c5021977daEnglishSymplectic Elements at Oxford2014Fiil, BGyrd-Hansen, MN-terminal methionine-linked ubiquitin (Met1-Ub), or linear ubiquitin, has emerged as a central post-translational modification in innate immune signalling. The molecular machinery that assembles, senses and, more recently, disassembles Met1-Ub has been identified, and technical advances have enabled the identification of physiological substrates for Met1-Ub in response to activation of innate immune receptors. These discoveries have significantly advanced our understanding of how nondegradative ubiquitin modifications control proinflammatory responses mediated by nuclear factor-κB and mitogen-activated protein kinases. In this review, we discuss the current data on Met1-Ub function and regulation, and point to some of the questions that still remain unanswered. |
| spellingShingle | Fiil, B Gyrd-Hansen, M Met1-linked ubiquitination in immune signalling. |
| title | Met1-linked ubiquitination in immune signalling. |
| title_full | Met1-linked ubiquitination in immune signalling. |
| title_fullStr | Met1-linked ubiquitination in immune signalling. |
| title_full_unstemmed | Met1-linked ubiquitination in immune signalling. |
| title_short | Met1-linked ubiquitination in immune signalling. |
| title_sort | met1 linked ubiquitination in immune signalling |
| work_keys_str_mv | AT fiilb met1linkedubiquitinationinimmunesignalling AT gyrdhansenm met1linkedubiquitinationinimmunesignalling |