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RNF167 activates mTORC1 and promotes tumorigenesis by targeting CASTOR1 for ubiquitination and degradation

Nat Commun. 2021-02; 
Tingting Li, Xian Wang, Enguo Ju, Suzane Ramos da Silva, Luping Chen, Xinquan Zhang, Shan Wei, Shou-Jiang Gao
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Proteins, Expression, Isolation and Analysis To detect all proteins except CASTOR1, samples were separated with 4–20% SDS-polyacrylamide gels (Genscript M00656 and M00657) Get A Quote

摘要

mTORC1, a central controller of cell proliferation in response to growth factors and nutrients, is dysregulated in cancer. Whereas arginine activates mTORC1, it is overridden by high expression of cytosolic arginine sensor for mTORC1 subunit 1 (CASTOR1). Because cancer cells often encounter low levels of?nutrients, an alternative mechanism might exist to regulate CASTOR1 expression. Here we show K29-linked polyubiquitination and degradation of CASTOR1 by E3 ubiquitin ligase RNF167. Furthermore, AKT phosphorylates CASTOR1 at S14, significantly increasing its binding to RNF167, and?hence its?ubiquitination and degradation, while simultaneously decreasing its affinity to MIOS, leading to mTORC1 activation. Ther... More

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