The mTOR signal transduction pathway in Kristen virus-transformed murine embryonic fibroblast (KBalb) was studied. Regulatory proteins and phosphoproteins associated with this pathway were identified in different cell fractions and compared to the levels detected in the parental cell line (Balb 3T3). In KBalb cells, mTOR and its regulatory proteins (Rictor, Raptor, and G�L) appeared to be present at higher levels than Balb 3T3 cells. These regulatory proteins are important in mTOR's interaction with downstream targets. Sites on mTOR phosphorylated by Akt also appeared to be different between the two cell lines. Rictor-mTOR complex phosphorylates Akt at Serine 473, which is necessary for the phosphorylation of Akt at Threonine 308 by PDK1 and its full activation. The increased levels of Rictor and mTOR proteins and the increased phosphorylation of Akt at Serine 473 and Threonine 308 support this idea that mTOR is more active in K-ras transformed cells.

Studies of mTOR and its substrates in Kirsten virus-transformed murine fibroblasts

245th National Meeting (2013)

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