Western blot analysis of extracts from serum-starved HeLa cells, untreated or treated with IGF-1 (50 ng/ml, 30 minutes) and λ phosphatase, using Phospho-Rictor (Thr1135) (D30A3) Rabbit mAb (upper) or Rictor (53A2) Rabbit mAb #2114 (lower).
Western blot analysis of extracts from various cell lines, using Rictor (53A2) Rabbit mAb.
PhosphoPlus® Duets from Cell Signaling Technology (CST) provide a means to assess protein activation status. Each Duet contains an activation-state and total protein antibody to your target of interest. These antibodies have been selected from CST's product offering based upon superior performance in specified applications.
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 (1). 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 (1). The mTOR-rictor complex phosphorylates Ser473 of Akt/PKB in vitro (2). This phosphorylation is essential for full Akt/PKB activation. Furthermore, an siRNA knockdown of rictor inhibits Ser473 phosphorylation in 3T3-L1 adipocytes (3). This complex has also been shown to phosphorylate the rapamycin-resistant mutants of S6K1, another effector of mTOR (4).
Phosphorylation of Thr1135 on rictor was identified at Cell Signaling Technology (CST) using PhosphoScan®, CST's LC-MS/MS platform for phosphorylation site discovery (5). 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 (6-8).
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