Rabbit polyclonal antibody to Rictor (Phospho~Thr1135)

Cell growth is a fundamental biological process whereby cells accumulate mass and increase in size. The mammalian TOR (mTOR) pathway regulates growth by coordinating energy and nutrient signals with growth factor~derived signals. mTOR is a large protein kinase with two different complexes. One complex contains mTOR, GβL and raptor, which is a target of rapamycin. The other complex, insensitive to rapamycin, includes mTOR, GβL, Sin1, and rictor. The mTOR~rictor complex phosphorylates Ser473 of Akt/PKB in vitro. This phosphorylation is essential for full Akt/PKB activation. Furthermore, an siRNA knockdown of rictor inhibits Ser473 phosphorylation in 3T3~L1 adipocytes. This complex has also been shown to phosphorylate the rapamycin~resistant mutants of S6K1, another effector of mTOR. Phosphorylation of Thr1135 on rictor was identified at Cell Signaling Technology (CST) using PhosphoScan®, CST's LC~MS/MS platform for phosphorylation site discovery. Additional research indicates that rictor is phosphorylated at Thr1135 by p70 S6K, which negatively regulates mTORC2 protein complex as part of a negative feedback mechanism controlling Akt activity.