The ubiquitin ligase ZNRF1 promotes caveolin-1 ubiquitination and degradation to modulate inflammation

Caveolae and their major constituent Caveolin-1 (CAV1) play an important role in signalling pathways involved in inflammation, but regulators of CAV1 protein stability are unknown. Here, the authors show that E3 ubiquitin ligase ZNRF1 induces degradation of CAV1 in response to TLR4 activation, and m...

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Autores principales: Chih-Yuan Lee, Ting-Yu Lai, Meng-Kun Tsai, Yung-Chi Chang, Yu-Hsin Ho, I-Shing Yu, Tzu-Wen Yeh, Chih-Chang Chou, You-Sheng Lin, Toby Lawrence, Li-Chung Hsu
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Lenguaje:EN
Publicado: Nature Portfolio 2017
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Acceso en línea:https://doaj.org/article/c30b0e30686342fe9db885694ae7780d
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spelling oai:doaj.org-article:c30b0e30686342fe9db885694ae7780d2021-12-02T14:42:16ZThe ubiquitin ligase ZNRF1 promotes caveolin-1 ubiquitination and degradation to modulate inflammation10.1038/ncomms155022041-1723https://doaj.org/article/c30b0e30686342fe9db885694ae7780d2017-06-01T00:00:00Zhttps://doi.org/10.1038/ncomms15502https://doaj.org/toc/2041-1723Caveolae and their major constituent Caveolin-1 (CAV1) play an important role in signalling pathways involved in inflammation, but regulators of CAV1 protein stability are unknown. Here, the authors show that E3 ubiquitin ligase ZNRF1 induces degradation of CAV1 in response to TLR4 activation, and mediates the pro-inflammatory response bothin vitro and in vivo.Chih-Yuan LeeTing-Yu LaiMeng-Kun TsaiYung-Chi ChangYu-Hsin HoI-Shing YuTzu-Wen YehChih-Chang ChouYou-Sheng LinToby LawrenceLi-Chung HsuNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-14 (2017)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Chih-Yuan Lee
Ting-Yu Lai
Meng-Kun Tsai
Yung-Chi Chang
Yu-Hsin Ho
I-Shing Yu
Tzu-Wen Yeh
Chih-Chang Chou
You-Sheng Lin
Toby Lawrence
Li-Chung Hsu
The ubiquitin ligase ZNRF1 promotes caveolin-1 ubiquitination and degradation to modulate inflammation
description Caveolae and their major constituent Caveolin-1 (CAV1) play an important role in signalling pathways involved in inflammation, but regulators of CAV1 protein stability are unknown. Here, the authors show that E3 ubiquitin ligase ZNRF1 induces degradation of CAV1 in response to TLR4 activation, and mediates the pro-inflammatory response bothin vitro and in vivo.
format article
author Chih-Yuan Lee
Ting-Yu Lai
Meng-Kun Tsai
Yung-Chi Chang
Yu-Hsin Ho
I-Shing Yu
Tzu-Wen Yeh
Chih-Chang Chou
You-Sheng Lin
Toby Lawrence
Li-Chung Hsu
author_facet Chih-Yuan Lee
Ting-Yu Lai
Meng-Kun Tsai
Yung-Chi Chang
Yu-Hsin Ho
I-Shing Yu
Tzu-Wen Yeh
Chih-Chang Chou
You-Sheng Lin
Toby Lawrence
Li-Chung Hsu
author_sort Chih-Yuan Lee
title The ubiquitin ligase ZNRF1 promotes caveolin-1 ubiquitination and degradation to modulate inflammation
title_short The ubiquitin ligase ZNRF1 promotes caveolin-1 ubiquitination and degradation to modulate inflammation
title_full The ubiquitin ligase ZNRF1 promotes caveolin-1 ubiquitination and degradation to modulate inflammation
title_fullStr The ubiquitin ligase ZNRF1 promotes caveolin-1 ubiquitination and degradation to modulate inflammation
title_full_unstemmed The ubiquitin ligase ZNRF1 promotes caveolin-1 ubiquitination and degradation to modulate inflammation
title_sort ubiquitin ligase znrf1 promotes caveolin-1 ubiquitination and degradation to modulate inflammation
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/c30b0e30686342fe9db885694ae7780d
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