Ubiquitylation in innate and adaptive immunity

Vijay G. Bhoj; Zhijian J. Chen

doi:10.1038/nature07959

Ubiquitylation in innate and adaptive immunity

Vijay G. Bhoj, Zhijian J. Chen

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

479 Scopus citations

Abstract

Protein ubiquitylation has emerged as a key mechanism that regulates immune responses. Much like phosphorylation, ubiquitylation is a reversible covalent modification that regulates the stability, activity and localization of target proteins. As such, ubiquitylation regulates the development of the immune system and many phases of the immune response, including its initiation, propagation and termination. Recent work has shown that several ubiquitin ligases help to prevent the immune system from attacking self tissues. The dysfunction of several ubiquitin ligases has been linked to autoimmune diseases.

Original language	English (US)
Pages (from-to)	430-437
Number of pages	8
Journal	Nature
Volume	458
Issue number	7237
DOIs	https://doi.org/10.1038/nature07959
State	Published - Mar 26 2009

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title = "Ubiquitylation in innate and adaptive immunity",

abstract = "Protein ubiquitylation has emerged as a key mechanism that regulates immune responses. Much like phosphorylation, ubiquitylation is a reversible covalent modification that regulates the stability, activity and localization of target proteins. As such, ubiquitylation regulates the development of the immune system and many phases of the immune response, including its initiation, propagation and termination. Recent work has shown that several ubiquitin ligases help to prevent the immune system from attacking self tissues. The dysfunction of several ubiquitin ligases has been linked to autoimmune diseases.",

author = "Bhoj, {Vijay G.} and Chen, {Zhijian J.}",

note = "Funding Information: Acknowledgements We apologize to the many authors whose publications are not cited directly because of space limitations. We thank J. Cabrera for graphic support. Research in our laboratory is supported by the Howard Hughes Medical Institute and by grants from the US National Institutes of Health and the Welch Foundation.",

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N1 - Funding Information: Acknowledgements We apologize to the many authors whose publications are not cited directly because of space limitations. We thank J. Cabrera for graphic support. Research in our laboratory is supported by the Howard Hughes Medical Institute and by grants from the US National Institutes of Health and the Welch Foundation.

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N2 - Protein ubiquitylation has emerged as a key mechanism that regulates immune responses. Much like phosphorylation, ubiquitylation is a reversible covalent modification that regulates the stability, activity and localization of target proteins. As such, ubiquitylation regulates the development of the immune system and many phases of the immune response, including its initiation, propagation and termination. Recent work has shown that several ubiquitin ligases help to prevent the immune system from attacking self tissues. The dysfunction of several ubiquitin ligases has been linked to autoimmune diseases.

AB - Protein ubiquitylation has emerged as a key mechanism that regulates immune responses. Much like phosphorylation, ubiquitylation is a reversible covalent modification that regulates the stability, activity and localization of target proteins. As such, ubiquitylation regulates the development of the immune system and many phases of the immune response, including its initiation, propagation and termination. Recent work has shown that several ubiquitin ligases help to prevent the immune system from attacking self tissues. The dysfunction of several ubiquitin ligases has been linked to autoimmune diseases.

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Ubiquitylation in innate and adaptive immunity

Abstract

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