The Met1-linked ubiquitin machinery in inflammation and infection

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The Met1-linked ubiquitin machinery in inflammation and infection. / Fiil, Berthe Katrine; Gyrd-Hansen, Mads.

In: Cell Death and Differentiation, Vol. 28, 2021, p. 557–569.

Research output: Contribution to journal › Review › Research › peer-review

Harvard

Fiil, BK & Gyrd-Hansen, M 2021, 'The Met1-linked ubiquitin machinery in inflammation and infection', Cell Death and Differentiation, vol. 28, pp. 557–569. https://doi.org/10.1038/s41418-020-00702-x

APA

Fiil, B. K., & Gyrd-Hansen, M. (2021). The Met1-linked ubiquitin machinery in inflammation and infection. Cell Death and Differentiation, 28, 557–569. https://doi.org/10.1038/s41418-020-00702-x

Vancouver

Fiil BK, Gyrd-Hansen M. The Met1-linked ubiquitin machinery in inflammation and infection. Cell Death and Differentiation. 2021;28:557–569. https://doi.org/10.1038/s41418-020-00702-x

Author

Fiil, Berthe Katrine ; Gyrd-Hansen, Mads. / The Met1-linked ubiquitin machinery in inflammation and infection. In: Cell Death and Differentiation. 2021 ; Vol. 28. pp. 557–569.

Bibtex

@article{de03ddda88334c48a9692714946f2b89,
title = "The Met1-linked ubiquitin machinery in inflammation and infection",
abstract = "Ubiquitination is an essential post-translational modification that regulates most cellular processes. The assembly of ubiquitin into polymeric chains by E3 ubiquitin ligases underlies the pleiotropic functions ubiquitin chains regulate. Ubiquitin chains assembled via the N-terminal methionine, termed Met1-linked ubiquitin chains or linear ubiquitin chains, have emerged as essential signalling scaffolds that regulate pro-inflammatory responses, anti-viral interferon responses, cell death and xenophagy of bacterial pathogens downstream of innate immune receptors. Met1-linked ubiquitin chains are exclusively assembled by the linear ubiquitin chain assembly complex, LUBAC, and are disassembled by the deubiquitinases OTULIN and CYLD. Genetic defects that perturb the regulation of Met1-linked ubiquitin chains causes severe immune-related disorders, illustrating their potent signalling capacity. Here, we review the current knowledge about the cellular machinery that conjugates, recognises, and disassembles Met1-linked ubiquitin chains, and discuss the function of this unique posttranslational modification in regulating inflammation, cell death and immunity to pathogens.",
author = "Fiil, {Berthe Katrine} and Mads Gyrd-Hansen",
year = "2021",
doi = "10.1038/s41418-020-00702-x",
language = "English",
volume = "28",
pages = "557–569",
journal = "Cell Differentiation and Development",
issn = "1350-9047",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - The Met1-linked ubiquitin machinery in inflammation and infection

AU - Fiil, Berthe Katrine

AU - Gyrd-Hansen, Mads

PY - 2021

Y1 - 2021

N2 - Ubiquitination is an essential post-translational modification that regulates most cellular processes. The assembly of ubiquitin into polymeric chains by E3 ubiquitin ligases underlies the pleiotropic functions ubiquitin chains regulate. Ubiquitin chains assembled via the N-terminal methionine, termed Met1-linked ubiquitin chains or linear ubiquitin chains, have emerged as essential signalling scaffolds that regulate pro-inflammatory responses, anti-viral interferon responses, cell death and xenophagy of bacterial pathogens downstream of innate immune receptors. Met1-linked ubiquitin chains are exclusively assembled by the linear ubiquitin chain assembly complex, LUBAC, and are disassembled by the deubiquitinases OTULIN and CYLD. Genetic defects that perturb the regulation of Met1-linked ubiquitin chains causes severe immune-related disorders, illustrating their potent signalling capacity. Here, we review the current knowledge about the cellular machinery that conjugates, recognises, and disassembles Met1-linked ubiquitin chains, and discuss the function of this unique posttranslational modification in regulating inflammation, cell death and immunity to pathogens.

AB - Ubiquitination is an essential post-translational modification that regulates most cellular processes. The assembly of ubiquitin into polymeric chains by E3 ubiquitin ligases underlies the pleiotropic functions ubiquitin chains regulate. Ubiquitin chains assembled via the N-terminal methionine, termed Met1-linked ubiquitin chains or linear ubiquitin chains, have emerged as essential signalling scaffolds that regulate pro-inflammatory responses, anti-viral interferon responses, cell death and xenophagy of bacterial pathogens downstream of innate immune receptors. Met1-linked ubiquitin chains are exclusively assembled by the linear ubiquitin chain assembly complex, LUBAC, and are disassembled by the deubiquitinases OTULIN and CYLD. Genetic defects that perturb the regulation of Met1-linked ubiquitin chains causes severe immune-related disorders, illustrating their potent signalling capacity. Here, we review the current knowledge about the cellular machinery that conjugates, recognises, and disassembles Met1-linked ubiquitin chains, and discuss the function of this unique posttranslational modification in regulating inflammation, cell death and immunity to pathogens.

U2 - 10.1038/s41418-020-00702-x

DO - 10.1038/s41418-020-00702-x

M3 - Review

C2 - 33473179

AN - SCOPUS:85099555626

VL - 28

SP - 557

EP - 569

JO - Cell Differentiation and Development

JF - Cell Differentiation and Development

SN - 1350-9047

ER -

ID: 256069085