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The serine/threonine kinase AKT is mutated in about 10% of cancers, which largely explains its carcinogenic effect in cancer.
In addition to mutations in the AKT gene, dysregulation of the upstream signaling pathways of growth factors can often activate AKT in cancer cells.
GSK3β, FOXO and TSC2 are the three main downstream genes of AKT, which can mediate the response of AKT to different stimuli and perform multiple functions.
Previous studies have shown that AKT-mediated phosphorylation and inhibition of TSC2 has been considered to be the main mechanism by which AKT activates mTORC1 (rapamycin complex 1).
mTORC1 is a central regulator of cell proliferation in response to growth factors and nutrients, and its expression is dysregulated in cancer.
Arginine can activate mTORC1.
Schematic diagram of related mechanisms
CASTOR1 (mTORC1 subunit 1) is a newly discovered cytoplasmic arginine sensor that responds to arginine and regulates the activity of mTORC1.
Interestingly, high levels of CASTOR1 protein inhibit the activation of mTORC1 by AAS (including arginine).
CASTOR1 (mTORC1 subunit 1) is a newly discovered cytoplasmic arginine sensor that responds to arginine and regulates the activity of mTORC1.
RNF167-mediated ubiquitination and AKT1-mediated phosphorylation promote the occurrence and development of breast cancer
Breast cancerFurther studies have shown that several cell types with higher CASTOR1 expression are not sensitive to the regulation of arginine.
It is worth noting that the degradation of CASTOR1 mediated by AKT and RNF167 can activate mTORC1 independent of arginine, and ultimately promote the occurrence and development of breast cancer.
All in all, the results of the study revealed the relevant regulatory mechanism of mTORC1 and identified RNF167 as a therapeutic target for mTORC1 dysregulation-related diseases.
The results of this study revealed the relevant regulatory mechanism of mTORC1 and identified RNF167 as a therapeutic target for mTORC1 dysregulation-related diseases.
The results of this study revealed the relevant regulatory mechanism of mTORC1 and identified RNF167 as a therapeutic target for mTORC1 dysregulation-related diseases.
org/10.
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