Hectd3 promotes pathogenic Th17 lineage through Stat3 activation and Malt1 signaling in neuroinflammation
Ubiquitination may control protein stability or function. Here the authors show that an ubiquitination enzyme, Hectd3, ubiquitinates Stat3 and Malt1 to modulate their function but not degradation in T cells, and thereby promoting the differentiation of pathogenic Th17 cells and susceptibility to a m...
Main Authors: | Jonathan J. Cho, Zhiwei Xu, Upasana Parthasarathy, Theodore T. Drashansky, Eric Y. Helm, Ashley N. Zuniga, Kyle J. Lorentsen, Samira Mansouri, Joshua Y. Cho, Mariola J. Edelmann, Duc M. Duong, Torben Gehring, Thomas Seeholzer, Daniel Krappmann, Mohammad N. Uddin, Danielle Califano, Rejean L. Wang, Lei Jin, Hongmin Li, Dongwen Lv, Daohong Zhou, Liang Zhou, Dorina Avram |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Portfolio
2019-02-01
|
Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-019-08605-3 |
Similar Items
-
The HECTD3 E3 Ubiquitin Ligase Suppresses Cisplatin-Induced Apoptosis via Stabilizing MALT1
by: Yi Li, et al.
Published: (2013-01-01) -
TRAF6 controls T cell homeostasis by maintaining the equilibrium of MALT1 scaffolding and protease functions
by: Thomas J. O’Neill, et al.
Published: (2023-01-01) -
Molecular architecture and regulation of BCL10-MALT1 filaments
by: Florian Schlauderer, et al.
Published: (2018-10-01) -
CircHECTD1 mediates pulmonary fibroblast activation HECTD1
by: Han Chu, et al.
Published: (2019-11-01) -
BCL10 – Bridging CARDs to Immune Activation
by: Torben Gehring, et al.
Published: (2018-07-01)