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Altering Kinase Specificity to Limit Cell Growth
Metabolic signals are coupled to pathways that mediate cellular growth and proliferation through mTORC1, a complex consisting of the kinase mechanistic target of rapamycin (mTOR) and the regulatory component raptor. Insulin and other growth factors activate the kinase Akt, which then phosphorylates and suppresses the activity of a complex that inhibits mTORC1. Several mechanisms have been proposed to explain how mTORC1 signaling is inhibited by REDD1 (regulated in DNA damage and development 1), a stress-inducible protein. Dennis et al. found that REDD1 acted as a targeting unit for a phosphatase that dephosphorylated Akt at a specific site. Once dephosphorylated by this REDD1-phosphatase complex, Akt had different substrate specificity and did not phosphorylate and inactivate the mTORC1 inhibitor. By changing the substrate specificity of Akt, REDD1 could potentially affect the activity of other signaling pathways in which Akt participates.
