Oligomerization-primed coiled-coil domain interaction with Ubc13 confers processivity to TRAF6 ubiquitin ligase activity

Ubiquitin ligase TRAF6 catalyzes assembly of free polyubiquitin chains for TAK1 activation in the IL-1R/TLR pathways, but the mechanism underlying its processivity is unclear. Here, the authors show that TRAF6 coiled-coil oligomerization domain primes its interaction with Ubc13/Ub~Ubc13 to confer pr...

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Autores principales: Lin Hu, Jiafeng Xu, Xiaomei Xie, Yiwen Zhou, Panfeng Tao, Haidong Li, Xu Han, Chong Wang, Jian Liu, Pinglong Xu, Dante Neculai, Zongping Xia
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Lenguaje:EN
Publicado: Nature Portfolio 2017
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Acceso en línea:https://doaj.org/article/eecb74c302b344b8a72513b69c603458
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spelling oai:doaj.org-article:eecb74c302b344b8a72513b69c6034582021-12-02T15:38:56ZOligomerization-primed coiled-coil domain interaction with Ubc13 confers processivity to TRAF6 ubiquitin ligase activity10.1038/s41467-017-01290-02041-1723https://doaj.org/article/eecb74c302b344b8a72513b69c6034582017-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-01290-0https://doaj.org/toc/2041-1723Ubiquitin ligase TRAF6 catalyzes assembly of free polyubiquitin chains for TAK1 activation in the IL-1R/TLR pathways, but the mechanism underlying its processivity is unclear. Here, the authors show that TRAF6 coiled-coil oligomerization domain primes its interaction with Ubc13/Ub~Ubc13 to confer processivity.Lin HuJiafeng XuXiaomei XieYiwen ZhouPanfeng TaoHaidong LiXu HanChong WangJian LiuPinglong XuDante NeculaiZongping XiaNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-13 (2017)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Lin Hu
Jiafeng Xu
Xiaomei Xie
Yiwen Zhou
Panfeng Tao
Haidong Li
Xu Han
Chong Wang
Jian Liu
Pinglong Xu
Dante Neculai
Zongping Xia
Oligomerization-primed coiled-coil domain interaction with Ubc13 confers processivity to TRAF6 ubiquitin ligase activity
description Ubiquitin ligase TRAF6 catalyzes assembly of free polyubiquitin chains for TAK1 activation in the IL-1R/TLR pathways, but the mechanism underlying its processivity is unclear. Here, the authors show that TRAF6 coiled-coil oligomerization domain primes its interaction with Ubc13/Ub~Ubc13 to confer processivity.
format article
author Lin Hu
Jiafeng Xu
Xiaomei Xie
Yiwen Zhou
Panfeng Tao
Haidong Li
Xu Han
Chong Wang
Jian Liu
Pinglong Xu
Dante Neculai
Zongping Xia
author_facet Lin Hu
Jiafeng Xu
Xiaomei Xie
Yiwen Zhou
Panfeng Tao
Haidong Li
Xu Han
Chong Wang
Jian Liu
Pinglong Xu
Dante Neculai
Zongping Xia
author_sort Lin Hu
title Oligomerization-primed coiled-coil domain interaction with Ubc13 confers processivity to TRAF6 ubiquitin ligase activity
title_short Oligomerization-primed coiled-coil domain interaction with Ubc13 confers processivity to TRAF6 ubiquitin ligase activity
title_full Oligomerization-primed coiled-coil domain interaction with Ubc13 confers processivity to TRAF6 ubiquitin ligase activity
title_fullStr Oligomerization-primed coiled-coil domain interaction with Ubc13 confers processivity to TRAF6 ubiquitin ligase activity
title_full_unstemmed Oligomerization-primed coiled-coil domain interaction with Ubc13 confers processivity to TRAF6 ubiquitin ligase activity
title_sort oligomerization-primed coiled-coil domain interaction with ubc13 confers processivity to traf6 ubiquitin ligase activity
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/eecb74c302b344b8a72513b69c603458
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