VPS34 K29/K48 branched ubiquitination governed by UBE3C and TRABID regulates autophagy, proteostasis and liver metabolism
Autophagy and the ubiquitin–proteasome system (UPS) are cellular quality control processes, but their coordination remains unclear. Here, the authors show that branched ubiquitination of VPS34 functions as a switch between UPS and autophagy and has an important role in lipid metabolism in the liver....
Main Authors: | Yu-Hsuan Chen, Tzu-Yu Huang, Yu-Tung Lin, Shu-Yu Lin, Wen-Hsin Li, Hsiang-Jung Hsiao, Ruei-Liang Yan, Hong-Wen Tang, Zhao-Qing Shen, Guang-Chao Chen, Kuen-Phon Wu, Ting-Fen Tsai, Ruey-Hwa Chen |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Publishing Group
2021-02-01
|
Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-021-21715-1 |
Similar Items
-
UBE3C-Mediated VPS34 Degradation Regulates Autophagy and Proteostasis
by: Tzu-Yu Huang, et al.
Published: (2019) -
Ubiquitination status does not affect Vps34 degradation
by: Jing Tang, et al.
Published: (2020-09-01) -
Beyond K48 and K63: non-canonical protein ubiquitination
by: Michal Tracz, et al.
Published: (2021-01-01) -
Both K63 and K48 ubiquitin linkages signal lysosomal degradation of the LDL receptor
by: Li Zhang, et al.
Published: (2013-05-01) -
Ubiquitination-induced fluorescence complementation (UiFC) for detection of K48 ubiquitin chains in vitro and in live cells.
by: Zhiliang Chen, et al.
Published: (2013-01-01)