Gene interactions and pathways from curated databases and text-mining
Mol Biol Cell 2012, PMID: 22696681

Phosphatidylinositol 3,5-bisphosphate plays a role in the activation and subcellular localization of mechanistic target of rapamycin 1.

Bridges, Dave; Ma, Jing-Tyan; Park, Sujin; Inoki, Ken; Weisman, Lois S; Saltiel, Alan R

The kinase complex mechanistic target of rapamycin 1 (mTORC1) plays an important role in controlling growth and metabolism. We report here that the stepwise formation of phosphatidylinositol 3-phosphate (PI(3)P) and phosphatidylinositol 3,5-bisphosphate (PI(3,5)P(2)) regulates the cell type-specific activation and localization of mTORC1. PI(3)P formation depends on the class II phosphatidylinositol 3-kinase (PI3K) PI3K-C2α, as well as the class III PI3K Vps34, while PI(3,5)P(2) requires the phosphatidylinositol-3-phosphate-5-kinase PIKFYVE. In this paper, we show that PIKFYVE and PI3K-C2α are necessary for activation of mTORC1 and its translocation to the plasma membrane in 3T3-L1 adipocytes. Furthermore, the mTORC1 component Raptor directly interacts with PI(3,5)P(2). Together these results suggest that PI(3,5)P(2) is an essential mTORC1 regulator that defines the localization of the complex.

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Text Mining Data

mTORC1 → PIKFYVE: " In this paper, we show that PIKFYVE and PI3K-C2a are necessary for activation of mTORC1 and its translocation to the plasma membrane in 3T3-L1 adipocytes "

mTORC1 → PI3K-C2a: " In this paper, we show that PIKFYVE and PI3K-C2a are necessary for activation of mTORC1 and its translocation to the plasma membrane in 3T3-L1 adipocytes "

Manually curated Databases

No curated data.