RNF167 activates mTORC1 and promotes tumorigenesis by targeting CASTOR1 for ubiquitination and degradation
CASTOR1 is an arginine sensor that inhibits mTORC1 activation, for which this pathway is frequently dysregulated in cancers. Here the authors show that AKT and E3 ubiquitin ligase RNF167 mediate CASTOR1 phosphorylation and degradation to activate mTORC1 and promote tumorigenesis.
Main Authors: | Tingting Li, Xian Wang, Enguo Ju, Suzane Ramos da Silva, Luping Chen, Xinquan Zhang, Shan Wei, Shou-Jiang Gao |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Publishing Group
2021-02-01
|
Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-021-21206-3 |
Similar Items
-
The CASTOR Proteins Are Arginine Sensors for the mTORC1 Pathway
by: Gygi, Melanie P., et al.
Published: (2017) -
Mechanism of arginine sensing by CASTOR1 upstream of mTORC1
by: Knockenhauer, Kevin E., et al.
Published: (2018) -
Pathogenic Role of mTORC1 and mTORC2 in Pulmonary Hypertension
by: Haiyang Tang, PhD, et al.
Published: (2018-12-01) -
Regulation of Autophagy through TORC1 and mTORC1
by: Takeshi Noda
Published: (2017-07-01) -
UBE3A-mediated p18/LAMTOR1 ubiquitination and degradation regulate mTORC1 activity and synaptic plasticity
by: Jiandong Sun, et al.
Published: (2018-07-01)