On August 24, 2010, Harvard Medical School and Cell Signaling Technology of the United States jointly published Science Signaling articles. This article explores that receptor tyrosine kinases (RTKs) play important roles in controlling cell growth, proliferation and survival through serine threonine kinase signaling pathways such as PI3K-Akt, Ras-MAPK-RSK and mTOR-p70 S6.
Akt, RSK, and p70 protein kinases of the S6 family transmit signals through the RxRxxS / T motif that phosphorylates substrate proteins. This study developed a large-scale proteomics method to identify receptor cases such as c-Met, epidermal growth factor receptor (EGFR), or platelet-derived growth factor receptor alpha (PDGFRα) in tumor cell lines More than 300 substrates of tyrosine kinase. This identified a group of proteins with RxRxxS / T sites. The phosphorylation of these proteins can be attenuated by RTK inhibitors (RTKIs), and of course by PI3K, mTOR, and MAPK pathway inhibitors; further through RNA interference The method determines the effect of these proteins on cell viability. In PDGFRα-dependent cancer cells, phosphorylation of serine at position 305 of the protein molecular chaperone SGTA (small glutamine-rich tetratricopeptide repeat-containing protein α) is necessary for PDGFRα stability and cell survival. This method provides a new field of view for the RTK and Akt-RSK-S6 kinase signaling pathways, revealing the previously unidentified substrates of Akt-RSK-S6 kinase, and these substrates are worthy of further study as RTKIs combined therapy targets.
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