Warm congratulations to the research group of Ying Liu, a senior customer of KS-V, for publishing a paper in Molecular Cell

Warm congratulations to KS-V's senior customer, the Institute of Molecular Medicine, Peking University School of Future Technology, Peking University-Tsinghua Life Science Joint Center, and Beijing Future Gene Diagnosis Advanced Innovation Center Liu Ying's research group on February 2, 2022 in Molecular Cell magazine Published a research paper titled" E3 ligase RNF167 and deubiquitinase STAMBPL1 modulate mTOR and cancer progression".

KS-V is honored to provide a series of customized peptide reagents for the research of Ying Liu's research group.

Original link:

https://www.cell.com/molecular-cell/pdf/S1097-2765(22)00002-8.pdf

Cells need to accurately sense the content of external nutrients to change their own metabolic processes, thereby adjusting the state of cell growth. The mTORC1 complex acts as a key nutrient sensory regulator. When nutrients are sufficient, the mTORC1 signaling pathway is activated to promote anabolism, while when nutrients are deficient, mTORC1 is inhibited, promotes catabolism, and then slows cell growth.

Amino acids, as key protein synthesis elements, are generally believed to be sensed by cells by binding to direct sensory proteins (amino acid receptors), which in turn transmit signals to mTORC1. Leucine is an essential amino acid for mTORC1 activation, and its sensing mechanism is important and complex. In addition to the recently reported leucine receptor protein SAR1B (Nature | Ying Liu's group reported that SAR1B senses intracellular leucine concentration to regulate mTORC1 activity), another receptor protein, Sestrin2, was previously reported to be critical for mTORC1 activation , however, how leucine affects downstream biological processes by binding to Sestrin2 is unclear.

This research paper by Ying Liu's group reports the mechanism by which the ubiquitin ligase RNF167 and the deubiquitinase STAMBPL1 coordinately regulate the K63 type polyubiquitination of the leucine-sensing protein Sestrin2 to affect the regulation of mTOR by Sestrin2, and its effect on colorectal cancer.